Fine mapping of the antigenic epitopes of the Gc protein of Guertu virus

Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae , poses a potential health threat to humans and animals. The viral glycoprotein (GP) binds to host cell receptors to induce a neutralizing immune response in the host. Therefore, identification of the...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:PloS one Jg. 17; H. 7; S. e0271878
Hauptverfasser: Yusufu, Meilipaiti, Abula, Ayipairi, Jiang, Boyong, Zhumabai, Jiayinaguli, Deng, Fei, Li, Yijie, Zhang, Yujiang, Ding, Juntao, Sun, Surong
Format: Journal Article
Sprache:Englisch
Veröffentlicht: San Francisco Public Library of Science 26.07.2022
Public Library of Science (PLoS)
Schlagworte:
ISSN:1932-6203, 1932-6203
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Abstract Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae , poses a potential health threat to humans and animals. The viral glycoprotein (GP) binds to host cell receptors to induce a neutralizing immune response in the host. Therefore, identification of the B-cell epitopes (BCEs) in the immunodominant region of the GTV Gc protein is important for the elucidation of the virus–host cell interactions and the development of GTV epitope assays and vaccines. In this study, an improved overlapping biosynthetic peptide method and rabbit anti-GTV Gc polyclonal antibodies were used for fine mapping of the minimal motifs of linear BCEs of the GTV Gc protein. Thirteen BCE motifs were identified from eleven positive 16mer-peptides, namely EGc1 ( 19 KVCATTGRA 27 ), EGc2 ( 58 KKINLKCKK 66 ), EGc3 ( 68 SSYYVPDA 75 ), EGc4 ( 75 ARSRCTSVRR 84 ), EGc5 ( 79 CTSVRRCRWA 88 ), EGc6 ( 90 DCQSGCPS 97 ), EGc7 ( 96 PSHFTSNS 103 ), EGc8 ( 115 AGLGFSG 121 ), EGc9 ( 148 ENPHGVI 154 ), EGc10 ( 179 KVFHPMS 185 ), EGc11 ( 230 QAGMGVVG 237 ), EGc12 ( 303 RSHDSQGKIS 312 ), and EGc13 ( 430 DIPRFV 435 ). Of these, 7 could be recognized by GTV IgG-positive sheep sera. Three-dimensional structural analysis revealed that all 13 BCEs were present on the surface of the Gc protein. Sequence alignment of the 13 BCEs against homologous proteins from 10 closely related strains of severe fever with thrombocytopenia syndrome virus from different geographical regions revealed that the amino acid sequences of EGc4, EGc5, EGc8, EGc11, and EGc12 were highly conserved, with 100% similarity. The remaining 8 epitopes (EGc1, EGc2, EGc3, EGc6, EGc7, EGc9, EGc10, and EGc13) showed high sequence similarity in the range of 71.43%–87.50%. These 13 BCEs of the GTV Gc protein provide a molecular foundation for future studies of the immunological properties of GTV glycoproteins and the development of GTV multi-epitope assays and vaccines.
AbstractList Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae, poses a potential health threat to humans and animals. The viral glycoprotein (GP) binds to host cell receptors to induce a neutralizing immune response in the host. Therefore, identification of the B-cell epitopes (BCEs) in the immunodominant region of the GTV Gc protein is important for the elucidation of the virus–host cell interactions and the development of GTV epitope assays and vaccines. In this study, an improved overlapping biosynthetic peptide method and rabbit anti-GTV Gc polyclonal antibodies were used for fine mapping of the minimal motifs of linear BCEs of the GTV Gc protein. Thirteen BCE motifs were identified from eleven positive 16mer-peptides, namely EGc1 (19KVCATTGRA27), EGc2 (58KKINLKCKK66), EGc3 (68SSYYVPDA75), EGc4 (75ARSRCTSVRR84), EGc5 (79CTSVRRCRWA88), EGc6 (90DCQSGCPS97), EGc7 (96PSHFTSNS103), EGc8 (115AGLGFSG121), EGc9 (148ENPHGVI154), EGc10 (179KVFHPMS185), EGc11 (230QAGMGVVG237), EGc12 (303RSHDSQGKIS312), and EGc13 (430DIPRFV435). Of these, 7 could be recognized by GTV IgG-positive sheep sera. Three-dimensional structural analysis revealed that all 13 BCEs were present on the surface of the Gc protein. Sequence alignment of the 13 BCEs against homologous proteins from 10 closely related strains of severe fever with thrombocytopenia syndrome virus from different geographical regions revealed that the amino acid sequences of EGc4, EGc5, EGc8, EGc11, and EGc12 were highly conserved, with 100% similarity. The remaining 8 epitopes (EGc1, EGc2, EGc3, EGc6, EGc7, EGc9, EGc10, and EGc13) showed high sequence similarity in the range of 71.43%–87.50%. These 13 BCEs of the GTV Gc protein provide a molecular foundation for future studies of the immunological properties of GTV glycoproteins and the development of GTV multi-epitope assays and vaccines.
Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae , poses a potential health threat to humans and animals. The viral glycoprotein (GP) binds to host cell receptors to induce a neutralizing immune response in the host. Therefore, identification of the B-cell epitopes (BCEs) in the immunodominant region of the GTV Gc protein is important for the elucidation of the virus–host cell interactions and the development of GTV epitope assays and vaccines. In this study, an improved overlapping biosynthetic peptide method and rabbit anti-GTV Gc polyclonal antibodies were used for fine mapping of the minimal motifs of linear BCEs of the GTV Gc protein. Thirteen BCE motifs were identified from eleven positive 16mer-peptides, namely EGc1 ( 19 KVCATTGRA 27 ), EGc2 ( 58 KKINLKCKK 66 ), EGc3 ( 68 SSYYVPDA 75 ), EGc4 ( 75 ARSRCTSVRR 84 ), EGc5 ( 79 CTSVRRCRWA 88 ), EGc6 ( 90 DCQSGCPS 97 ), EGc7 ( 96 PSHFTSNS 103 ), EGc8 ( 115 AGLGFSG 121 ), EGc9 ( 148 ENPHGVI 154 ), EGc10 ( 179 KVFHPMS 185 ), EGc11 ( 230 QAGMGVVG 237 ), EGc12 ( 303 RSHDSQGKIS 312 ), and EGc13 ( 430 DIPRFV 435 ). Of these, 7 could be recognized by GTV IgG-positive sheep sera. Three-dimensional structural analysis revealed that all 13 BCEs were present on the surface of the Gc protein. Sequence alignment of the 13 BCEs against homologous proteins from 10 closely related strains of severe fever with thrombocytopenia syndrome virus from different geographical regions revealed that the amino acid sequences of EGc4, EGc5, EGc8, EGc11, and EGc12 were highly conserved, with 100% similarity. The remaining 8 epitopes (EGc1, EGc2, EGc3, EGc6, EGc7, EGc9, EGc10, and EGc13) showed high sequence similarity in the range of 71.43%–87.50%. These 13 BCEs of the GTV Gc protein provide a molecular foundation for future studies of the immunological properties of GTV glycoproteins and the development of GTV multi-epitope assays and vaccines.
Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae , poses a potential health threat to humans and animals. The viral glycoprotein (GP) binds to host cell receptors to induce a neutralizing immune response in the host. Therefore, identification of the B-cell epitopes (BCEs) in the immunodominant region of the GTV Gc protein is important for the elucidation of the virus–host cell interactions and the development of GTV epitope assays and vaccines. In this study, an improved overlapping biosynthetic peptide method and rabbit anti-GTV Gc polyclonal antibodies were used for fine mapping of the minimal motifs of linear BCEs of the GTV Gc protein. Thirteen BCE motifs were identified from eleven positive 16mer-peptides, namely EGc1 ( 19 KVCATTGRA 27 ), EGc2 ( 58 KKINLKCKK 66 ), EGc3 ( 68 SSYYVPDA 75 ), EGc4 ( 75 ARSRCTSVRR 84 ), EGc5 ( 79 CTSVRRCRWA 88 ), EGc6 ( 90 DCQSGCPS 97 ), EGc7 ( 96 PSHFTSNS 103 ), EGc8 ( 115 AGLGFSG 121 ), EGc9 ( 148 ENPHGVI 154 ), EGc10 ( 179 KVFHPMS 185 ), EGc11 ( 230 QAGMGVVG 237 ), EGc12 ( 303 RSHDSQGKIS 312 ), and EGc13 ( 430 DIPRFV 435 ). Of these, 7 could be recognized by GTV IgG-positive sheep sera. Three-dimensional structural analysis revealed that all 13 BCEs were present on the surface of the Gc protein. Sequence alignment of the 13 BCEs against homologous proteins from 10 closely related strains of severe fever with thrombocytopenia syndrome virus from different geographical regions revealed that the amino acid sequences of EGc4, EGc5, EGc8, EGc11, and EGc12 were highly conserved, with 100% similarity. The remaining 8 epitopes (EGc1, EGc2, EGc3, EGc6, EGc7, EGc9, EGc10, and EGc13) showed high sequence similarity in the range of 71.43%–87.50%. These 13 BCEs of the GTV Gc protein provide a molecular foundation for future studies of the immunological properties of GTV glycoproteins and the development of GTV multi-epitope assays and vaccines.
Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae, poses a potential health threat to humans and animals. The viral glycoprotein (GP) binds to host cell receptors to induce a neutralizing immune response in the host. Therefore, identification of the B-cell epitopes (BCEs) in the immunodominant region of the GTV Gc protein is important for the elucidation of the virus-host cell interactions and the development of GTV epitope assays and vaccines. In this study, an improved overlapping biosynthetic peptide method and rabbit anti-GTV Gc polyclonal antibodies were used for fine mapping of the minimal motifs of linear BCEs of the GTV Gc protein. Thirteen BCE motifs were identified from eleven positive 16mer-peptides, namely EGc1 (19KVCATTGRA27), EGc2 (58KKINLKCKK66), EGc3 (68SSYYVPDA75), EGc4 (75ARSRCTSVRR84), EGc5 (79CTSVRRCRWA88), EGc6 (90DCQSGCPS97), EGc7 (96PSHFTSNS103), EGc8 (115AGLGFSG121), EGc9 (148ENPHGVI154), EGc10 (179KVFHPMS185), EGc11 (230QAGMGVVG237), EGc12 (303RSHDSQGKIS312), and EGc13 (430DIPRFV435). Of these, 7 could be recognized by GTV IgG-positive sheep sera. Three-dimensional structural analysis revealed that all 13 BCEs were present on the surface of the Gc protein. Sequence alignment of the 13 BCEs against homologous proteins from 10 closely related strains of severe fever with thrombocytopenia syndrome virus from different geographical regions revealed that the amino acid sequences of EGc4, EGc5, EGc8, EGc11, and EGc12 were highly conserved, with 100% similarity. The remaining 8 epitopes (EGc1, EGc2, EGc3, EGc6, EGc7, EGc9, EGc10, and EGc13) showed high sequence similarity in the range of 71.43%-87.50%. These 13 BCEs of the GTV Gc protein provide a molecular foundation for future studies of the immunological properties of GTV glycoproteins and the development of GTV multi-epitope assays and vaccines.Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae, poses a potential health threat to humans and animals. The viral glycoprotein (GP) binds to host cell receptors to induce a neutralizing immune response in the host. Therefore, identification of the B-cell epitopes (BCEs) in the immunodominant region of the GTV Gc protein is important for the elucidation of the virus-host cell interactions and the development of GTV epitope assays and vaccines. In this study, an improved overlapping biosynthetic peptide method and rabbit anti-GTV Gc polyclonal antibodies were used for fine mapping of the minimal motifs of linear BCEs of the GTV Gc protein. Thirteen BCE motifs were identified from eleven positive 16mer-peptides, namely EGc1 (19KVCATTGRA27), EGc2 (58KKINLKCKK66), EGc3 (68SSYYVPDA75), EGc4 (75ARSRCTSVRR84), EGc5 (79CTSVRRCRWA88), EGc6 (90DCQSGCPS97), EGc7 (96PSHFTSNS103), EGc8 (115AGLGFSG121), EGc9 (148ENPHGVI154), EGc10 (179KVFHPMS185), EGc11 (230QAGMGVVG237), EGc12 (303RSHDSQGKIS312), and EGc13 (430DIPRFV435). Of these, 7 could be recognized by GTV IgG-positive sheep sera. Three-dimensional structural analysis revealed that all 13 BCEs were present on the surface of the Gc protein. Sequence alignment of the 13 BCEs against homologous proteins from 10 closely related strains of severe fever with thrombocytopenia syndrome virus from different geographical regions revealed that the amino acid sequences of EGc4, EGc5, EGc8, EGc11, and EGc12 were highly conserved, with 100% similarity. The remaining 8 epitopes (EGc1, EGc2, EGc3, EGc6, EGc7, EGc9, EGc10, and EGc13) showed high sequence similarity in the range of 71.43%-87.50%. These 13 BCEs of the GTV Gc protein provide a molecular foundation for future studies of the immunological properties of GTV glycoproteins and the development of GTV multi-epitope assays and vaccines.
Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae, poses a potential health threat to humans and animals. The viral glycoprotein (GP) binds to host cell receptors to induce a neutralizing immune response in the host. Therefore, identification of the B-cell epitopes (BCEs) in the immunodominant region of the GTV Gc protein is important for the elucidation of the virus-host cell interactions and the development of GTV epitope assays and vaccines. In this study, an improved overlapping biosynthetic peptide method and rabbit anti-GTV Gc polyclonal antibodies were used for fine mapping of the minimal motifs of linear BCEs of the GTV Gc protein. Thirteen BCE motifs were identified from eleven positive 16mer-peptides, namely EGc1 (.sup.19 KVCATTGRA.sup.27 ), EGc2 (.sup.58 KKINLKCKK.sup.66 ), EGc3 (.sup.68 SSYYVPDA.sup.75 ), EGc4 (.sup.75 ARSRCTSVRR.sup.84 ), EGc5 (.sup.79 CTSVRRCRWA.sup.88 ), EGc6 (.sup.90 DCQSGCPS.sup.97 ), EGc7 (.sup.96 PSHFTSNS.sup.103 ), EGc8 (.sup.115 AGLGFSG.sup.121 ), EGc9 (.sup.148 ENPHGVI.sup.154 ), EGc10 (.sup.179 KVFHPMS.sup.185 ), EGc11 (.sup.230 QAGMGVVG.sup.237 ), EGc12 (.sup.303 RSHDSQGKIS.sup.312 ), and EGc13 (.sup.430 DIPRFV.sup.435). Of these, 7 could be recognized by GTV IgG-positive sheep sera. Three-dimensional structural analysis revealed that all 13 BCEs were present on the surface of the Gc protein. Sequence alignment of the 13 BCEs against homologous proteins from 10 closely related strains of severe fever with thrombocytopenia syndrome virus from different geographical regions revealed that the amino acid sequences of EGc4, EGc5, EGc8, EGc11, and EGc12 were highly conserved, with 100% similarity. The remaining 8 epitopes (EGc1, EGc2, EGc3, EGc6, EGc7, EGc9, EGc10, and EGc13) showed high sequence similarity in the range of 71.43%-87.50%. These 13 BCEs of the GTV Gc protein provide a molecular foundation for future studies of the immunological properties of GTV glycoproteins and the development of GTV multi-epitope assays and vaccines.
Audience Academic
Author Jiang, Boyong
Zhumabai, Jiayinaguli
Abula, Ayipairi
Li, Yijie
Sun, Surong
Zhang, Yujiang
Ding, Juntao
Deng, Fei
Yusufu, Meilipaiti
AuthorAffiliation 1 Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, China
University of Texas Medical Branch at Galveston, UNITED STATES
2 State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China
3 Center for Disease Control and Prevention of Xinjiang Uygur Autonomous Region, Urumqi, China
AuthorAffiliation_xml – name: 3 Center for Disease Control and Prevention of Xinjiang Uygur Autonomous Region, Urumqi, China
– name: University of Texas Medical Branch at Galveston, UNITED STATES
– name: 2 State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China
– name: 1 Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, China
Author_xml – sequence: 1
  givenname: Meilipaiti
  surname: Yusufu
  fullname: Yusufu, Meilipaiti
– sequence: 2
  givenname: Ayipairi
  surname: Abula
  fullname: Abula, Ayipairi
– sequence: 3
  givenname: Boyong
  surname: Jiang
  fullname: Jiang, Boyong
– sequence: 4
  givenname: Jiayinaguli
  surname: Zhumabai
  fullname: Zhumabai, Jiayinaguli
– sequence: 5
  givenname: Fei
  surname: Deng
  fullname: Deng, Fei
– sequence: 6
  givenname: Yijie
  surname: Li
  fullname: Li, Yijie
– sequence: 7
  givenname: Yujiang
  surname: Zhang
  fullname: Zhang, Yujiang
– sequence: 8
  givenname: Juntao
  surname: Ding
  fullname: Ding, Juntao
– sequence: 9
  givenname: Surong
  surname: Sun
  fullname: Sun, Surong
BookMark eNqNkttq3DAQhk1JaQ7tGxRqKJT0YreSZcl2LwohNJuFQKCnWyHLI68Wr-RIcmjevnLXC3EIpehCYvT9_4xGc5ocGWsgSd5itMSkwJ-2dnBGdMs-hpcoK3BZlC-SE1yRbMEyRI4enY-TU--3CFFSMvYqOSa0LDFl1UlyfaUNpDvR99q0qVVp2EAqTNAtGC1T6HWwPfjDzUqmvbMBtBkjqwFcGNJ77Qb_OnmpROfhzbSfJT-vvv64vF7c3K7Wlxc3C8lYFRaqBsgqweqCNaQpCyQUJUjlTYNkjTPI6qKEBgDlqiIFECEFzbEgjJSgclGTs-Td3rfvrOdTEzzPWJVXKGMZjsR6TzRWbHnv9E64B26F5n8D1rVcuKBlB5wyleNKZRWjKqesjN1pUMUIzjMpBILo9WXKNtQ7aCSY4EQ3M53fGL3hrb3nsfPxl_JocD4ZOHs3gA98p72ErhMG7DDVzTCiY93vn6DPv26iWhEfoI2yMa8cTflFgTGlOSU0UstnqLga2GkZJ0bpGJ8JPs4EkQnwO7Ri8J6vv3_7f_b215z98IjdgOjCxttuCNoaPwc_70HprPcOFJc6iBGLleuOY8THsT_0hI9jz6exj-L8ifjwQ_-U_QFvCQZj
CitedBy_id crossref_primary_10_1371_journal_pone_0310862
Cites_doi 10.1016/j.vaccine.2015.08.020
10.1093/infdis/jis748
10.1007/978-1-4939-2999-3_1
10.1080/02648725.2007.10648092
10.1128/JVI.02076-16
10.1093/infdis/jiv144
10.1128/JVI.02628-12
10.1093/infdis/jit603
10.4269/ajtmh.16-0527
10.1016/j.meegid.2016.11.015
10.1073/pnas.1603827113
10.1371/journal.ppat.1002369
10.1155/2016/6760830
10.1371/journal.pone.0166013
10.1016/j.jiac.2016.04.001
10.1007/s00705-019-04253-6
10.1016/j.virusres.2012.10.028
10.1093/cid/cir732
10.1111/imm.12323
10.1007/BF01309700
10.1007/s12250-016-3858-6
10.1016/j.jri.2009.04.004
10.1016/j.antiviral.2014.05.016
10.1371/journal.pone.0204264
10.1371/journal.pone.0223978
10.1089/vbz.2011.0758
10.1016/j.antiviral.2013.07.006
10.1016/j.cimid.2019.101371
10.1371/journal.pone.0186097
10.1016/S0076-6879(96)66034-0
10.1038/srep34686
10.1186/1743-422X-10-301
10.1073/pnas.71.5.1743
10.1111/imm.12284
10.1038/s41426-018-0093-2
ContentType Journal Article
Copyright COPYRIGHT 2022 Public Library of Science
2022 Yusufu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
2022 Yusufu et al 2022 Yusufu et al
Copyright_xml – notice: COPYRIGHT 2022 Public Library of Science
– notice: 2022 Yusufu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: 2022 Yusufu et al 2022 Yusufu et al
DBID AAYXX
CITATION
IOV
ISR
3V.
7QG
7QL
7QO
7RV
7SN
7SS
7T5
7TG
7TM
7U9
7X2
7X7
7XB
88E
8AO
8C1
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
ABJCF
ABUWG
AEUYN
AFKRA
ARAPS
ATCPS
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
C1K
CCPQU
COVID
D1I
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
H94
HCIFZ
K9.
KB.
KB0
KL.
L6V
LK8
M0K
M0S
M1P
M7N
M7P
M7S
NAPCQ
P5Z
P62
P64
PATMY
PDBOC
PHGZM
PHGZT
PIMPY
PJZUB
PKEHL
PPXIY
PQEST
PQGLB
PQQKQ
PQUKI
PTHSS
PYCSY
RC3
7X8
5PM
DOA
DOI 10.1371/journal.pone.0271878
DatabaseName CrossRef
Gale In Context: Opposing Viewpoints
Gale In Context: Science
ProQuest Central (Corporate)
Animal Behavior Abstracts
Bacteriology Abstracts (Microbiology B)
Biotechnology Research Abstracts
Nursing & Allied Health Database
Ecology Abstracts
Entomology Abstracts (Full archive)
Immunology Abstracts
Meteorological & Geoastrophysical Abstracts
Nucleic Acids Abstracts
Virology and AIDS Abstracts
Agricultural Science Collection
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
ProQuest Pharma Collection
Public Health Database
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
ProQuest Hospital Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
Materials Science & Engineering Collection
ProQuest Central (Alumni)
One Sustainability
ProQuest Central UK/Ireland
Advanced Technologies & Computer Science Collection
Agricultural & Environmental Science Collection
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Technology collection
Natural Science Collection
Environmental Sciences and Pollution Management
ProQuest One
Coronavirus Research Database
ProQuest Materials Science Collection
ProQuest Central
Engineering Research Database
Health Research Premium Collection (UHCL Subscription)
Health Research Premium Collection (Alumni)
ProQuest Central Student
AIDS and Cancer Research Abstracts
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
Materials Science Database
Nursing & Allied Health Database (Alumni Edition)
Meteorological & Geoastrophysical Abstracts - Academic
ProQuest Engineering Collection
Biological Sciences
Agriculture Science Database
ProQuest Health & Medical Collection
Medical Database
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biological Science Database
Engineering Database
Nursing & Allied Health Premium
Advanced Technologies & Aerospace Database
ProQuest Advanced Technologies & Aerospace Collection
Biotechnology and BioEngineering Abstracts
Environmental Science Database
Materials Science Collection
ProQuest Central Premium
ProQuest One Academic
Publicly Available Content Database
ProQuest Health & Medical Research Collection
ProQuest One Academic Middle East (New)
One Health & Nursing
ProQuest One Academic Eastern Edition (DO NOT USE)
One Applied & Life Sciences
ProQuest One Academic (retired)
ProQuest One Academic UKI Edition
Engineering Collection
Environmental Science Collection
Genetics Abstracts
MEDLINE - Academic
PubMed Central (Full Participant titles)
DOAJ Directory of Open Access Journals
DatabaseTitle CrossRef
Agricultural Science Database
Publicly Available Content Database
ProQuest Central Student
ProQuest Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Nucleic Acids Abstracts
SciTech Premium Collection
Environmental Sciences and Pollution Management
ProQuest One Applied & Life Sciences
ProQuest One Sustainability
Health Research Premium Collection
Meteorological & Geoastrophysical Abstracts
Natural Science Collection
Health & Medical Research Collection
Biological Science Collection
ProQuest Central (New)
ProQuest Medical Library (Alumni)
Engineering Collection
Advanced Technologies & Aerospace Collection
Engineering Database
Virology and AIDS Abstracts
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
Agricultural Science Collection
Coronavirus Research Database
ProQuest Hospital Collection
ProQuest Technology Collection
Health Research Premium Collection (Alumni)
Biological Science Database
Ecology Abstracts
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
Environmental Science Collection
Entomology Abstracts
Nursing & Allied Health Premium
ProQuest Health & Medical Complete
ProQuest One Academic UKI Edition
Environmental Science Database
ProQuest Nursing & Allied Health Source (Alumni)
Engineering Research Database
ProQuest One Academic
Meteorological & Geoastrophysical Abstracts - Academic
ProQuest One Academic (New)
Technology Collection
Technology Research Database
ProQuest One Academic Middle East (New)
Materials Science Collection
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest One Health & Nursing
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central
ProQuest Health & Medical Research Collection
Genetics Abstracts
ProQuest Engineering Collection
Biotechnology Research Abstracts
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Agricultural & Environmental Science Collection
AIDS and Cancer Research Abstracts
Materials Science Database
ProQuest Materials Science Collection
ProQuest Public Health
ProQuest Nursing & Allied Health Source
ProQuest SciTech Collection
Advanced Technologies & Aerospace Database
ProQuest Medical Library
Animal Behavior Abstracts
Materials Science & Engineering Collection
Immunology Abstracts
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList
CrossRef


MEDLINE - Academic


Agricultural Science Database
Database_xml – sequence: 1
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  dbid: PIMPY
  name: Publicly Available Content Database
  url: http://search.proquest.com/publiccontent
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Sciences (General)
DocumentTitleAlternate Mapping of BCEs on Glycoprotein-Gc from GTV
EISSN 1932-6203
ExternalDocumentID 2694902621
oai_doaj_org_article_56f419f2965f4568866d0963142caa0e
PMC9321374
A711554535
10_1371_journal_pone_0271878
GeographicLocations China
GeographicLocations_xml – name: China
GrantInformation_xml – fundername: ;
  grantid: 81760365
– fundername: ;
  grantid: 81960369
– fundername: ;
  grantid: XJEDU2019I002
GroupedDBID ---
123
29O
2WC
53G
5VS
7RV
7X2
7X7
7XC
88E
8AO
8C1
8CJ
8FE
8FG
8FH
8FI
8FJ
A8Z
AAFWJ
AAUCC
AAWOE
AAYXX
ABDBF
ABIVO
ABJCF
ABUWG
ACCTH
ACGFO
ACIHN
ACIWK
ACPRK
ACUHS
ADBBV
AEAQA
AENEX
AEUYN
AFFHD
AFKRA
AFPKN
AFRAH
AHMBA
ALMA_UNASSIGNED_HOLDINGS
AOIJS
APEBS
ARAPS
ATCPS
BAIFH
BAWUL
BBNVY
BBTPI
BCNDV
BENPR
BGLVJ
BHPHI
BKEYQ
BPHCQ
BVXVI
BWKFM
CCPQU
CITATION
CS3
D1I
D1J
D1K
DIK
DU5
E3Z
EAP
EAS
EBD
EMOBN
ESX
EX3
F5P
FPL
FYUFA
GROUPED_DOAJ
GX1
HCIFZ
HH5
HMCUK
HYE
IAO
IEA
IGS
IHR
IHW
INH
INR
IOV
IPY
ISE
ISR
ITC
K6-
KB.
KQ8
L6V
LK5
LK8
M0K
M1P
M48
M7P
M7R
M7S
M~E
NAPCQ
O5R
O5S
OK1
OVT
P2P
P62
PATMY
PDBOC
PHGZM
PHGZT
PIMPY
PJZUB
PPXIY
PQGLB
PQQKQ
PROAC
PSQYO
PTHSS
PV9
PYCSY
RNS
RPM
RZL
SV3
TR2
UKHRP
WOQ
WOW
~02
~KM
ALIPV
BBORY
3V.
7QG
7QL
7QO
7SN
7SS
7T5
7TG
7TM
7U9
7XB
8FD
8FK
AZQEC
C1K
COVID
DWQXO
ESTFP
FR3
GNUQQ
H94
K9.
KL.
M7N
P64
PKEHL
PQEST
PQUKI
RC3
7X8
PUEGO
5PM
-
02
AAPBV
ABPTK
ADACO
BBAFP
KM
ID FETCH-LOGICAL-c669t-fbee29a6b76d3d870af530f4dd0cb12e2b78edee04f937e3aca541a3638ef4ab3
IEDL.DBID FPL
ISICitedReferencesCount 1
ISICitedReferencesURI http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000860587700006&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN 1932-6203
IngestDate Sun Jul 31 00:48:02 EDT 2022
Mon Nov 10 04:28:29 EST 2025
Tue Nov 04 01:55:51 EST 2025
Wed Oct 01 14:53:45 EDT 2025
Tue Oct 07 07:45:01 EDT 2025
Sat Nov 29 13:25:19 EST 2025
Sat Nov 29 10:08:09 EST 2025
Wed Nov 26 10:35:22 EST 2025
Wed Nov 26 09:21:21 EST 2025
Thu May 22 21:19:39 EDT 2025
Tue Nov 18 22:27:36 EST 2025
Sat Nov 29 03:36:47 EST 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 7
Language English
License This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Creative Commons Attribution License
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c669t-fbee29a6b76d3d870af530f4dd0cb12e2b78edee04f937e3aca541a3638ef4ab3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
Competing Interests: The authors have declared that no competing interests exist.
OpenAccessLink http://dx.doi.org/10.1371/journal.pone.0271878
PMID 35881569
PQID 2694902621
PQPubID 1436336
PageCount e0271878
ParticipantIDs plos_journals_2694902621
doaj_primary_oai_doaj_org_article_56f419f2965f4568866d0963142caa0e
pubmedcentral_primary_oai_pubmedcentral_nih_gov_9321374
proquest_miscellaneous_2694961051
proquest_journals_2694902621
gale_infotracmisc_A711554535
gale_infotracacademiconefile_A711554535
gale_incontextgauss_ISR_A711554535
gale_incontextgauss_IOV_A711554535
gale_healthsolutions_A711554535
crossref_citationtrail_10_1371_journal_pone_0271878
crossref_primary_10_1371_journal_pone_0271878
PublicationCentury 2000
PublicationDate 2022-07-26
PublicationDateYYYYMMDD 2022-07-26
PublicationDate_xml – month: 07
  year: 2022
  text: 2022-07-26
  day: 26
PublicationDecade 2020
PublicationPlace San Francisco
PublicationPlace_xml – name: San Francisco
– name: San Francisco, CA USA
PublicationTitle PloS one
PublicationYear 2022
Publisher Public Library of Science
Public Library of Science (PLoS)
Publisher_xml – name: Public Library of Science
– name: Public Library of Science (PLoS)
References RM Elliott (pone.0271878.ref013) 2014; 5
T Takahashi (pone.0271878.ref003) 2014; 209
A Shalitanati (pone.0271878.ref026) 2018
S Shen (pone.0271878.ref006) 2018; 7
WX Xu (pone.0271878.ref023) 2009; 81
R Zhu (pone.0271878.ref014) 2017; 44
WM Abbott (pone.0271878.ref016) 2014; 142
L Potocnakova (pone.0271878.ref015) 2016; 2016
A Moming (pone.0271878.ref025) 2018; 13
KL Mansfield (pone.0271878.ref033) 2015; 33
JF Morrow (pone.0271878.ref018) 1974; 71
F Yuan (pone.0271878.ref012) 2017; 32
J Shi (pone.0271878.ref009) 2017; 47
S Halldorsson (pone.0271878.ref011) 2016; 113
Z Han (pone.0271878.ref021) 2013; 171
CJ Bao (pone.0271878.ref036) 2011; 53
G. Houen (pone.0271878.ref019) 2015; 1348
PY Chou (pone.0271878.ref031) 1978; 47
JR Yoo (pone.0271878.ref007) 2016; 95
B Xu (pone.0271878.ref035) 2011; 7
E Davidson (pone.0271878.ref022) 2014; 143
J Zhang (pone.0271878.ref017) 2019; 14
J Arikawa (pone.0271878.ref041) 1992; 126
Y Liu (pone.0271878.ref037) 2012; 12
X Tang (pone.0271878.ref038) 2013; 207
RC Ladner (pone.0271878.ref020) 2007; 24
WX Xu (pone.0271878.ref029) 2017; 12
Estrada-Pena (pone.0271878.ref001) 2014; 108
J Garnier (pone.0271878.ref030) 1996; 266
L Yu (pone.0271878.ref040) 2013; 10
T Yoshikawa (pone.0271878.ref008) 2015; 212
S Kurihara (pone.0271878.ref002) 2016; 22
J Zhang (pone.0271878.ref027) 2019; 67
WX Xu (pone.0271878.ref024) 2016; 6
A Abula (pone.0271878.ref028) 2020; 40
H Hofmann (pone.0271878.ref010) 2013; 87
J Hinkula (pone.0271878.ref039) 2017; 91
DA Bente (pone.0271878.ref034) 2013; 100
A Abudurexiti (pone.0271878.ref005) 2019; 164
T Plegge (pone.0271878.ref032) 2016; 11
MA Fill (pone.0271878.ref004) 2017; 64
References_xml – volume: 33
  start-page: 5520
  issue: 42
  year: 2015
  ident: pone.0271878.ref033
  article-title: Rift Valley fever virus: A review of diagnosis and vaccination, and implications for emergence in Europe
  publication-title: Vaccine
  doi: 10.1016/j.vaccine.2015.08.020
– volume: 207
  start-page: 736
  issue: 5
  year: 2013
  ident: pone.0271878.ref038
  article-title: Human-to-human transmission of severe fever with thrombocytopenia syndrome bunyavirus through contact with infectious blood
  publication-title: J Infect Dis
  doi: 10.1093/infdis/jis748
– volume: 1348
  start-page: 1
  year: 2015
  ident: pone.0271878.ref019
  article-title: Peptide antibodies: Past, present, and future
  publication-title: Methods Mol Biol
  doi: 10.1007/978-1-4939-2999-3_1
– volume: 24
  start-page: 1
  year: 2007
  ident: pone.0271878.ref020
  article-title: Mapping the epitopes of antibodies
  publication-title: Biotechnol Genet Eng Rev
  doi: 10.1080/02648725.2007.10648092
– volume: 91
  start-page: e02076
  issue: 10
  year: 2017
  ident: pone.0271878.ref039
  article-title: Immunization with DNA plasmids coding for Crimean-Congo hemorrhagic fever virus capsid and envelope proteins and/or virus-like particles induces protection and survival in challenged mice
  publication-title: J Virol
  doi: 10.1128/JVI.02076-16
– volume: 212
  start-page: 889
  issue: 6
  year: 2015
  ident: pone.0271878.ref008
  article-title: Phylogenetic and geographic relationships of severe fever with thrombocytopenia syndrome virus in China, South Korea, and Japan
  publication-title: J Infect Dis
  doi: 10.1093/infdis/jiv144
– volume: 87
  start-page: 4384
  issue: 8
  year: 2013
  ident: pone.0271878.ref010
  article-title: Severe fever with thrombocytopenia virus glycoproteins are targeted by neutralizing antibodies and can use DC-SIGN as a receptor for pH-dependent entry into human and animal cell lines
  publication-title: J Virol
  doi: 10.1128/JVI.02628-12
– volume: 209
  start-page: 816
  issue: 6
  year: 2014
  ident: pone.0271878.ref003
  article-title: The first identification and retrospective study of severe fever with thrombocytopenia syndrome in Japan
  publication-title: J Infect Dis
  doi: 10.1093/infdis/jit603
– volume: 95
  start-page: 1351
  issue: 6
  year: 2016
  ident: pone.0271878.ref007
  article-title: Family cluster analysis of severe fever with thrombocytopenia syndrome virus infection in Korea
  publication-title: Am J Trop Med Hyg
  doi: 10.4269/ajtmh.16-0527
– volume: 47
  start-page: 109
  year: 2017
  ident: pone.0271878.ref009
  article-title: Migration, recombination, and reassortment are involved in the evolution of severe fever with thrombocytopenia syndrome bunyavirus
  publication-title: Infect Genet Evol
  doi: 10.1016/j.meegid.2016.11.015
– volume: 113
  start-page: 7154
  issue: 26
  year: 2016
  ident: pone.0271878.ref011
  article-title: Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1603827113
– volume: 5
  start-page: 50
  issue: 100
  year: 2014
  ident: pone.0271878.ref013
  article-title: Emerging Phleboviruses. Curr Opin Virol
– volume: 64
  start-page: 510
  issue: 4
  year: 2017
  ident: pone.0271878.ref004
  article-title: Novel clinical and pathologic findings in a Heartland virus-associated death
  publication-title: Clin Infect Dis
– volume: 7
  start-page: e1002369
  issue: 11
  year: 2011
  ident: pone.0271878.ref035
  article-title: Metagenomic analysis of fever, thrombocytopenia and leukopenia syndrome (FTLS) in Henan Province, China: discovery of a new bunyavirus
  publication-title: PLoS Pathog
  doi: 10.1371/journal.ppat.1002369
– volume: 2016
  start-page: 1
  year: 2016
  ident: pone.0271878.ref015
  article-title: An introduction to B-cell epitope mapping and In Silico epitope prediction
  publication-title: J Immunol Res
  doi: 10.1155/2016/6760830
– volume: 47
  start-page: 145
  issue: 6
  year: 1978
  ident: pone.0271878.ref031
  article-title: Prediction of the secondary structure of proteins from their amino acid sequence
  publication-title: Adv Enzymol Relat Areas Mol Biol
– volume: 11
  start-page: e0166013
  issue: 11
  year: 2016
  ident: pone.0271878.ref032
  article-title: Evidence that processing of the severe fever with thrombocytopenia syndrome virus Gn/Gc polyprotein is critical for viral infectivity and requires an internal Gc signal peptide
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0166013
– volume: 22
  start-page: 461
  issue: 7
  year: 2016
  ident: pone.0271878.ref002
  article-title: The world first two cases of severe fever with thrombocytopenia syndrome: An epidemiological study in Nagasaki, Japan.
  publication-title: J Infect Chemother
  doi: 10.1016/j.jiac.2016.04.001
– volume: 164
  start-page: 1949
  issue: 7
  year: 2019
  ident: pone.0271878.ref005
  article-title: Taxonomy of the order Bunyavirales: update 2019.
  publication-title: Arch Virol
  doi: 10.1007/s00705-019-04253-6
– volume: 171
  start-page: 54
  issue: 1
  year: 2013
  ident: pone.0271878.ref021
  article-title: Fine level epitope mapping and conservation analysis of two novel linear B-cell epitopes of the avian infectious bronchitis coronavirus nucleocapsid protein
  publication-title: Virus Res
  doi: 10.1016/j.virusres.2012.10.028
– volume: 53
  start-page: 1208
  issue: 12
  year: 2011
  ident: pone.0271878.ref036
  article-title: A family cluster of infections by a newly recognized bunyavirus in eastern China, 2007: further evidence of person-to-person transmission
  publication-title: Clin Infect Dis
  doi: 10.1093/cid/cir732
– volume: 143
  start-page: 13
  issue: 1
  year: 2014
  ident: pone.0271878.ref022
  article-title: A high-throughput shotgun mutagenesis approach to mapping B-cell antibody epitopes
  publication-title: Immunology
  doi: 10.1111/imm.12323
– volume: 126
  start-page: 271
  issue: 1–4
  year: 1992
  ident: pone.0271878.ref041
  article-title: Protective role of antigenic sites on the envelope protein of Hantaan virus defined by monoclonal antibodies
  publication-title: Arch Virol
  doi: 10.1007/BF01309700
– volume: 32
  start-page: 44
  issue: 001
  year: 2017
  ident: pone.0271878.ref012
  article-title: Entry of severe fever with thrombocytopenia syndrome virus.
  publication-title: Virologica Sinica
  doi: 10.1007/s12250-016-3858-6
– volume: 81
  start-page: 9
  issue: 1
  year: 2009
  ident: pone.0271878.ref023
  article-title: Minimal motif mapping of a known epitope on human zona pellucida protein-4 using a peptide biosynthesis strategy
  publication-title: J Reprod Immunol
  doi: 10.1016/j.jri.2009.04.004
– volume: 108
  start-page: 104
  year: 2014
  ident: pone.0271878.ref001
  article-title: The ecology of ticks and epidemiology of tick-borne viral diseases
  publication-title: Antiviral Res
  doi: 10.1016/j.antiviral.2014.05.016
– start-page: S0147957118300572
  year: 2018
  ident: pone.0271878.ref026
  article-title: Fine mapping epitope on glycoprotein-Gn from Crimean-Congo hemorrhagic fever virus
  publication-title: Comp Immunol Microbiol Infect Dis
– volume: 13
  start-page: e0204264
  issue: 9
  year: 2018
  ident: pone.0271878.ref025
  article-title: Mapping of B-cell epitopes on the N-terminal and C-terminal segment of nucleocapsid protein from Crimean-Congo hemorrhagic fever virus
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0204264
– volume: 14
  start-page: e0223978
  issue: 10
  year: 2019
  ident: pone.0271878.ref017
  article-title: Fine epitope mapping of glycoprotein Gn in Guertu virus
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0223978
– volume: 12
  start-page: 156
  issue: 2
  year: 2012
  ident: pone.0271878.ref037
  article-title: Person-to-person transmission of severe fever with thrombocytopenia syndrome virus
  publication-title: Vector Borne Zoonotic Dis
  doi: 10.1089/vbz.2011.0758
– volume: 100
  start-page: 159
  issue: 1
  year: 2013
  ident: pone.0271878.ref034
  article-title: Crimean-Congo hemorrhagic fever: history, epidemiology, pathogenesis, clinical syndrome and genetic diversity
  publication-title: Antiviral Res
  doi: 10.1016/j.antiviral.2013.07.006
– volume: 67
  start-page: 101371
  year: 2019
  ident: pone.0271878.ref027
  article-title: Fine mapping epitope on glycoprotein Gc from Crimean-Congo hemorrhagic fever virus
  publication-title: Comp Immunol Microbiol Infect Dis
  doi: 10.1016/j.cimid.2019.101371
– volume: 12
  start-page: e0186097
  issue: 10
  year: 2017
  ident: pone.0271878.ref029
  article-title: A simpler and more cost-effective peptide biosynthetic method using the truncated GST as carrier for epitope mapping
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0186097
– volume: 266
  start-page: 540
  year: 1996
  ident: pone.0271878.ref030
  article-title: GOR method for predicting protein secondary structure from amino acid sequence
  publication-title: Methods Enzymol
  doi: 10.1016/S0076-6879(96)66034-0
– volume: 6
  start-page: 34686
  year: 2016
  ident: pone.0271878.ref024
  article-title: Epitomics: IgG-epitome decoding of E6, E7 and L1 proteins from oncogenic human papillomavirus type 58
  publication-title: Sci Rep
  doi: 10.1038/srep34686
– volume: 10
  start-page: 301
  issue: 1
  year: 2013
  ident: pone.0271878.ref040
  article-title: A recombinant pseudotyped lentivirus expressing the envelope glycoprotein of Hantaan virus induced protective immunity in mice
  publication-title: Virol J
  doi: 10.1186/1743-422X-10-301
– volume: 40
  start-page: 178
  issue: 03
  year: 2020
  ident: pone.0271878.ref028
  article-title: Expression and antibody preparation of recombinant truncated glycoprotein of Guertu virus
  publication-title: Chin J Microbiol Immunol
– volume: 71
  start-page: 1743
  issue: 5
  year: 1974
  ident: pone.0271878.ref018
  article-title: Replication and transcription of eukaryotic DNA in Escherichia coli
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.71.5.1743
– volume: 44
  start-page: 2172
  issue: 9
  year: 2017
  ident: pone.0271878.ref014
  article-title: Progresses on B cell epitope mapping, microbio china
– volume: 142
  start-page: 526
  issue: 4
  year: 2014
  ident: pone.0271878.ref016
  article-title: Current approaches to fine mapping of antigen-antibody interactions
  publication-title: Immunology
  doi: 10.1111/imm.12284
– volume: 7
  start-page: 95
  issue: 1
  year: 2018
  ident: pone.0271878.ref006
  article-title: A novel tick-borne phlebovirus, closely related to severe fever with thrombocytopenia syndrome virus and Heartland virus, might be a potential pathogen
  publication-title: Emerg Microbes Infect
  doi: 10.1038/s41426-018-0093-2
SSID ssj0053866
Score 2.4013762
Snippet Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae , poses a potential health threat to humans and animals....
Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae, poses a potential health threat to humans and animals. The...
Guertu virus (GTV), a newly discovered member of the genus Banyangvirus in the family Phenuiviridae , poses a potential health threat to humans and animals....
SourceID plos
doaj
pubmedcentral
proquest
gale
crossref
SourceType Open Website
Open Access Repository
Aggregation Database
Enrichment Source
Index Database
StartPage e0271878
SubjectTerms Amino acid sequence
Amino acids
Antibodies
Antigenic determinants
Antigens
Arachnids
B cells
Biology and Life Sciences
Biosynthesis
Bunyaviruses
Cell interactions
Epitope mapping
Fever
Genetic aspects
Glycoproteins
Health risks
Homology
Immune response
Immune system
Immunoglobulin G
Immunological research
Immunology
Laboratories
Lymphocytes B
Mapping
Medical research
Medicine and Health Sciences
Methods
Nucleotide sequence
Peptide mapping
Peptides
Polyclonal antibodies
Proteins
Research and Analysis Methods
RNA polymerase
Sheep
Similarity
Structural analysis
Structure
Three dimensional analysis
Thrombocytopenia
Vaccines
Viral proteins
Viruses
SummonAdditionalLinks – databaseName: DOAJ Directory of Open Access Journals
  dbid: DOA
  link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELbQigMXRHmoCwUCQgIOaeN3ciyIbZFQQTyq3iLHsdtIJYk2m_5-ZhJvtJGQyoFrZrxKvnl4rPV8Q8gbwVPnVCJim-EIMy2zOEsNJEPIhj71QrGBUuj8iz47Sy8usm87o77wTthIDzwCdySVFzTzLFPSw2afpkqVUHZzKpg1JnGYfaHq2R6mxhwMUaxUaJTjmh4Fuxy2Te0O4SBGUxyrtrMRDXz9U1ZetNdNNys55xcmd3ag1QNyP5SO0fH4ynvkjqsfkr0QnF30LjBIv39ETldQO0a_DXIvXEaNj6DKiwBCZN6sbORaCOMWlgTJiY0GuoaqxicnvVtv-uimWvfdY_Jr9ennx9M4jEyIrVLZJvaFcywzqtCq5CXEovGSJ16UZWILyhwrdOpK5xLhoS5x3FgjBTUcotB5YQr-hCxqAGmfRLC3F14WnvvUCdzTaGmxU1V7K6ljdkn4Fr_cBj5xHGtxnQ9_kmk4V4y45Ih6HlBfknha1Y58Grfof0DTTLrIhj08AB_Jg4_kt_nIkrxEw-Zja-kU0_mxplhOSS6X5PWggYwYNV65uTR91-Wfv57_g9KP7zOlt0HJNwCHNaHNAb4JmbZmmgczTYhrOxPvoxtuUely7DnO4MjMKKzcuubfxa8mMf4oXqOrXdMHHSiYJejomUvPAJ5L6upqoB2HSh_MJJ7-D4s8I_cY9pEkOmbqgCw26949J3ftzabq1i-GWP4DSq5NMg
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: Biological Science Database
  dbid: M7P
  link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9QwELZg4cAFKA91aQGDkIBD2jh2nOSECmJbJFQqHlVvluPYS6SSpMmmv5-ZrLM0EgIkrplxoszL42TmG0JeCJ5aK0MRmAxHmCVxFmSphmAI0dClTshogBQ6_ZgcH6dnZ9mJ_-DW-bLKMSYOgbqoDX4j38eOywwODBF701wEODUK_676ERrXyQ1ESeBD6d7JGInBl6X07XI8YfteO3tNXdk9OI6xFIerXdmOBtT-TWyeNed1N0k8p2WTV_ahxZ3_fYO75LbPQOnB2mS2yDVb3SNb3sc7-soDUb--T44WkILSHxohHJa0dhSSRQqaQADP0lDbQDRoYImnHBo6oD6UFV457G276ull2fbdA_Jt8f7ru6PAT14IjJTZKnC5tVGmZZ7Ighfg0trFPHSiKEKTs8hGeZLawtpQOEhvLNdGx4JpDs5sndA5f0hmFUh5m1BIEXIX54671ArcGllhsOE1cSZmNjJzwkcFKONhyXE6xrka_rUlcDxZy0Wh2pRX25wEm1XNGpbjL_xvUbcbXgTVHi7U7VJ5H1WxdIJlLspk7CCvTMF6CjjhcSYio3Vo5-QpWoZad6huQoM6SBhmZTGP5-T5wIHAGhVW7ix133Xqw6fTf2D68nnC9NIzuRrEYbTvloB3QsCuCefuhBPCg5mQt9GOR6l06pcZwsrRUH9PfrYh402xGq-yde95IO-OgSeZ-MREwFNKVX4f0MvhwABqEo_-_PAdcivCRpMwCSK5S2artrePyU1zuSq79sng5j8BwLtcjg
  priority: 102
  providerName: ProQuest
Title Fine mapping of the antigenic epitopes of the Gc protein of Guertu virus
URI https://www.proquest.com/docview/2694902621
https://www.proquest.com/docview/2694961051
https://pubmed.ncbi.nlm.nih.gov/PMC9321374
https://doaj.org/article/56f419f2965f4568866d0963142caa0e
http://dx.doi.org/10.1371/journal.pone.0271878
Volume 17
WOSCitedRecordID wos000860587700006&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVAON
  databaseName: DOAJ Directory of Open Access Journals
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: DOA
  dateStart: 20060101
  isFulltext: true
  titleUrlDefault: https://www.doaj.org/
  providerName: Directory of Open Access Journals
– providerCode: PRVHPJ
  databaseName: ROAD: Directory of Open Access Scholarly Resources
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: M~E
  dateStart: 20060101
  isFulltext: true
  titleUrlDefault: https://road.issn.org
  providerName: ISSN International Centre
– providerCode: PRVPQU
  databaseName: Agricultural Science Database
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: M0K
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/agriculturejournals
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Biological Science Database
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: M7P
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: http://search.proquest.com/biologicalscijournals
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Engineering Database
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: M7S
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: http://search.proquest.com
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Environmental Science Database
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: PATMY
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: http://search.proquest.com/environmentalscience
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Health & Medical Collection
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: 7X7
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/healthcomplete
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Materials Science Database
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: KB.
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: http://search.proquest.com/materialsscijournals
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Nursing & Allied Health Database
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: 7RV
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/nahs
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest advanced technologies & aerospace journals
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: P5Z
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/hightechjournals
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Central
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: BENPR
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: https://www.proquest.com/central
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Public Health Database
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: 8C1
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/publichealth
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Publicly Available Content Database
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: PIMPY
  dateStart: 20061201
  isFulltext: true
  titleUrlDefault: http://search.proquest.com/publiccontent
  providerName: ProQuest
– providerCode: PRVATS
  databaseName: Public Library of Science (PLoS) Journals Open Access
  customDbUrl:
  eissn: 1932-6203
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0053866
  issn: 1932-6203
  databaseCode: FPL
  dateStart: 20060101
  isFulltext: true
  titleUrlDefault: http://www.plos.org/publications/
  providerName: Public Library of Science
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3db9MwELdYxwMvwPjQCqMEhAQ8pMRxYieP67Ru07YSdVANXiLHsUelkVZNs7-fO9ctBDEBL_eQu4uS8519l_h-JuRNxBKteRD5KsUjzESc-mkiYTKE2dAkJuKhhRSanInRKLm8TLOfheJvf_CZoB-cTfvzWaX7UETRRCRbZDtknOMWrmF2tp55IXY5d-1xt2m2lh-L0r-Zizvz61ndSjTb2yR_WXeGD_73iR-S-y7D9PZXLrFD7ujqEdlxMVx77xzQ9PvH5HgIKab3XSJEw5U3Mx4kgx5YGgE6p8rTc4j2Oag4zpHyLKrDtMIrR41eLBvvZrpo6ifk8_Dw08Gx705W8BXn6dI3hdZhKnkheMlKCFlpYhaYqCwDVdBQh4VIdKl1EBlIXzSTSsYRlQyCVZtIFuwp6VTwdrvEgxSgMHFhmEl0hEsfLRU2tAqjYqpD1SVsbfBcOdhxPP3iOrf_0gSUHyu75Giu3JmrS_yN1nwFu_EX-QGO5UYWQbPtBRiX3MVgHnMT0dSEKY8N5I0JeEsJFRyjUaikDHSXvERPyFcdqJvQz_cFxawrZnGXvLYSCJxR4c6cK9nUdX7ycfIPQhfjltBbJ2RmYA4lXTcEvBMCcrUk91qSEP6qxd5Fv11bpc6xNTmFyjqkoLn25T-zX23YeFPcbVfpWeNkIK-OQUa0YqBl4Danmn6z6ORQEMAwRc9uf67n5F6ITSSB8EO-RzrLRaNfkLvqZjmtFz2yJcYTpJfC0gRockB7ZHtwOMrGPfvVpGcDH-jpoA_0PDhFKjJLL4Bm8VfQyE7Osy8_AICOV4E
linkProvider Public Library of Science
linkToHtml http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Nb9QwELXKggQXoHyoC4UGBAIOaWPHcZIDQuVj21WXBZWy6i04jr2sVJKw2RTxp_iNzGSdpZEQcOmBazxOFPv5eSbxvCHkEfcjrYXHXRVjCbMwiN04kkCGwIYmMlywRlJoMgrH4-j4OH6_Rn60uTB4rLLlxIaos0LhN_IdzLiMIWBg9EX51cWqUfh3tS2hsYTFgf7-DUK26vnwNczvY8YGb45e7bu2qoCrhIgXrkm1ZrEUaSgyPwO4ShP4nuFZ5qmUMs3SMNKZ1h43sHVrXyoZcCp9AKo2XKY-3PcCuQg8TvEIWXg4aZkfuEMIm57nh3THomG7LHK9DeEfjbCY25ntr6kSsNoLeuVJUXUc3e4xzTP73uDa_zZi18lV62E7u8slsU7WdH6DrFsOq5ynVmj72U2yPwAX2_kiUaJi6hTGAWfYAaShQOlMOboEtiuhi23ZU06jajHL8cpereeL2jmdzevqFvl4Lm90m_RymNUN4oALlJogNb6JNMetn2YKE3pDowKqmeoTv53wRFnZdaz-cZI0_xJDCL-W45IgTBILkz5xV73KpezIX-xfIpZWtiga3lwo5tPEclASCMNpbFgsAgN-cwRozSCC9SlnSkpP98kWIjFZZuCuqC_ZDSl6nYEf9MnDxgKFQ3I8mTSVdVUlw3eTfzD6cNgxemKNTAHDoaTNBoF3QkGyjuVmxxLoT3WaN3DdtKNSJb9gDz3bhfH75gerZrwpnjbMdVFbG4grArAJO2uwM8Ddlnz2uVFnh4AIponf-fPDt8jl_aO3o2Q0HB_cJVcYJtV4ocvEJukt5rW-Ry6p08Wsmt9vKMYhn857hf4EFZO9OQ
linkToPdf http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9QwELbKghAXoDzUhUINAgGHdBM7cZIDQqVl21WrUvGoeguOYy8rlSRsNkX8NX4dM1knNBICLj1wtcdZZTzzeWbj-YaQJz6PtBau76gYW5iFQezEkQQwBDQ0kfEFayiFjg_Cw8Po5CQ-WiE_2loYvFbZYmID1Fmh8D_yEVZcxpAwMG9k7LWIo53xq_Krgx2k8Etr205jaSL7-vs3SN-ql5Md2OunjI3ffNjec2yHAUcJES8ck2rNYinSUGQ8A9OVJuCu8bPMVanHNEvDSGdau76BY1xzqWTge5KD0Wrjy5TDcy-RyyEOYJX6dne9BHBECFuqx0NvZC1jsyxyvQmpoBdhY7dzR2HTMaA7FwblaVH1gt7-lc1zZ-D4xv-svZvkuo286dbSVVbJis5vkVWLbRV9bgm4X9wme2MIvekXidQVU1oYCkEyBQtE4tKZoroEFCxhiZ3ZVbRhu5jlOLJb6_mipmezeV3dIR8v5I3ukkEOO7xGKIRGqQlSw02kfQwJvExhoW9oVOBppoaEt5ufKEvHjl1BTpPmG2MIadlSLwmaTGJNZkicblW5pCP5i_xrtKtOFsnEm4FiPk0sNiWBML4XGxaLwEA8HYHlZpDZcs9nSkpXD8kGWmWyrMztIDHZCj2MRgMeDMnjRgIJRXI0rqmsqyqZvD3-B6H373pCz6yQKUAdStoqEXgnJCrrSa73JAEWVW96DX2o1UqV_HIBWNk6ye-nH3XT-FC8hZjrorYykG8EIBP2_LGn4P5MPvvcsLZDogTb5N_7849vkKvgmMnB5HD_PrnGsNbGDR0m1slgMa_1A3JFnS1m1fxhgzaUfLpoB_0JhgrFlA
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Fine+mapping+of+the+antigenic+epitopes+of+the+Gc+protein+of+Guertu+virus&rft.jtitle=PloS+one&rft.au=Meilipaiti+Yusufu&rft.au=Contributed+equally+to+this+work+with%3A+Meilipaiti+Yusufu&rft.au=Ayipairi+Abula+Ayipairi+Abula&rft.au=Ayipairi+Abula+Boyong+Jiang&rft.date=2022-07-26&rft.pub=Public+Library+of+Science&rft.eissn=1932-6203&rft.volume=17&rft.issue=7&rft_id=info:doi/10.1371%2Fjournal.pone.0271878&rft.externalDocID=2694902621
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1932-6203&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1932-6203&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1932-6203&client=summon