Elucidating the 3D Structure of a Surface Membrane Antigen from Trypanosoma cruzi as a Serodiagnostic Biomarker of Chagas Disease
Chagas disease (CD) is a vector-borne parasitosis, caused by the protozoan parasite Trypanosoma cruzi, that affects millions of people worldwide. Although endemic in South America, CD is emerging throughout the world due to climate change and increased immigratory flux of infected people to non-ende...
Uložené v:
| Vydané v: | Vaccines (Basel) Ročník 10; číslo 1; s. 71 |
|---|---|
| Hlavní autori: | , , , , , , , , , , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
| Vydavateľské údaje: |
Switzerland
MDPI AG
03.01.2022
MDPI |
| Predmet: | |
| ISSN: | 2076-393X, 2076-393X |
| On-line prístup: | Získať plný text |
| Tagy: |
Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
|
| Abstract | Chagas disease (CD) is a vector-borne parasitosis, caused by the protozoan parasite Trypanosoma cruzi, that affects millions of people worldwide. Although endemic in South America, CD is emerging throughout the world due to climate change and increased immigratory flux of infected people to non-endemic regions. Containing of the diffusion of CD is challenged by the asymptomatic nature of the disease in early infection stages and by the lack of a rapid and effective diagnostic test. With the aim of designing new serodiagnostic molecules to be implemented in a microarray-based diagnostic set-up for early screening of CD, herein, we report the recombinant production of the extracellular domain of a surface membrane antigen from T. cruzi (TcSMP) and confirm its ability to detect plasma antibodies from infected patients. Moreover, we describe its high-resolution (1.62 Å) crystal structure, to which in silico epitope predictions were applied in order to locate the most immunoreactive regions of TcSMP in order to guide the design of epitopes that may be used as an alternative to the full-length antigen for CD diagnosis. Two putative, linear epitopes, belonging to the same immunogenic region, were synthesized as free peptides, and their immunological properties were tested in vitro. Although both peptides were shown to adopt a structural conformation that allowed their recognition by polyclonal antibodies raised against the recombinant protein, they were not serodiagnostic for T. cruzi infections. Nevertheless, they represent good starting points for further iterative structure-based (re)design cycles. |
|---|---|
| AbstractList | Chagas disease (CD) is a vector-borne parasitosis, caused by the protozoan parasite
, that affects millions of people worldwide. Although endemic in South America, CD is emerging throughout the world due to climate change and increased immigratory flux of infected people to non-endemic regions. Containing of the diffusion of CD is challenged by the asymptomatic nature of the disease in early infection stages and by the lack of a rapid and effective diagnostic test. With the aim of designing new serodiagnostic molecules to be implemented in a microarray-based diagnostic set-up for early screening of CD, herein, we report the recombinant production of the extracellular domain of a surface membrane antigen from
(
SMP) and confirm its ability to detect plasma antibodies from infected patients. Moreover, we describe its high-resolution (1.62 Å) crystal structure, to which in silico epitope predictions were applied in order to locate the most immunoreactive regions of
SMP in order to guide the design of epitopes that may be used as an alternative to the full-length antigen for CD diagnosis. Two putative, linear epitopes, belonging to the same immunogenic region, were synthesized as free peptides, and their immunological properties were tested in vitro. Although both peptides were shown to adopt a structural conformation that allowed their recognition by polyclonal antibodies raised against the recombinant protein, they were not serodiagnostic for
infections. Nevertheless, they represent good starting points for further iterative structure-based (re)design cycles. Chagas disease (CD) is a vector-borne parasitosis, caused by the protozoan parasite Trypanosoma cruzi, that affects millions of people worldwide. Although endemic in South America, CD is emerging throughout the world due to climate change and increased immigratory flux of infected people to non-endemic regions. Containing of the diffusion of CD is challenged by the asymptomatic nature of the disease in early infection stages and by the lack of a rapid and effective diagnostic test. With the aim of designing new serodiagnostic molecules to be implemented in a microarray-based diagnostic set-up for early screening of CD, herein, we report the recombinant production of the extracellular domain of a surface membrane antigen from T. cruzi (TcSMP) and confirm its ability to detect plasma antibodies from infected patients. Moreover, we describe its high-resolution (1.62 Å) crystal structure, to which in silico epitope predictions were applied in order to locate the most immunoreactive regions of TcSMP in order to guide the design of epitopes that may be used as an alternative to the full-length antigen for CD diagnosis. Two putative, linear epitopes, belonging to the same immunogenic region, were synthesized as free peptides, and their immunological properties were tested in vitro. Although both peptides were shown to adopt a structural conformation that allowed their recognition by polyclonal antibodies raised against the recombinant protein, they were not serodiagnostic for T. cruzi infections. Nevertheless, they represent good starting points for further iterative structure-based (re)design cycles.Chagas disease (CD) is a vector-borne parasitosis, caused by the protozoan parasite Trypanosoma cruzi, that affects millions of people worldwide. Although endemic in South America, CD is emerging throughout the world due to climate change and increased immigratory flux of infected people to non-endemic regions. Containing of the diffusion of CD is challenged by the asymptomatic nature of the disease in early infection stages and by the lack of a rapid and effective diagnostic test. With the aim of designing new serodiagnostic molecules to be implemented in a microarray-based diagnostic set-up for early screening of CD, herein, we report the recombinant production of the extracellular domain of a surface membrane antigen from T. cruzi (TcSMP) and confirm its ability to detect plasma antibodies from infected patients. Moreover, we describe its high-resolution (1.62 Å) crystal structure, to which in silico epitope predictions were applied in order to locate the most immunoreactive regions of TcSMP in order to guide the design of epitopes that may be used as an alternative to the full-length antigen for CD diagnosis. Two putative, linear epitopes, belonging to the same immunogenic region, were synthesized as free peptides, and their immunological properties were tested in vitro. Although both peptides were shown to adopt a structural conformation that allowed their recognition by polyclonal antibodies raised against the recombinant protein, they were not serodiagnostic for T. cruzi infections. Nevertheless, they represent good starting points for further iterative structure-based (re)design cycles. Chagas disease (CD) is a vector-borne parasitosis, caused by the protozoan parasite Trypanosoma cruzi, that affects millions of people worldwide. Although endemic in South America, CD is emerging throughout the world due to climate change and increased immigratory flux of infected people to non-endemic regions. Containing of the diffusion of CD is challenged by the asymptomatic nature of the disease in early infection stages and by the lack of a rapid and effective diagnostic test. With the aim of designing new serodiagnostic molecules to be implemented in a microarray-based diagnostic set-up for early screening of CD, herein, we report the recombinant production of the extracellular domain of a surface membrane antigen from T. cruzi (TcSMP) and confirm its ability to detect plasma antibodies from infected patients. Moreover, we describe its high-resolution (1.62 Å) crystal structure, to which in silico epitope predictions were applied in order to locate the most immunoreactive regions of TcSMP in order to guide the design of epitopes that may be used as an alternative to the full-length antigen for CD diagnosis. Two putative, linear epitopes, belonging to the same immunogenic region, were synthesized as free peptides, and their immunological properties were tested in vitro. Although both peptides were shown to adopt a structural conformation that allowed their recognition by polyclonal antibodies raised against the recombinant protein, they were not serodiagnostic for T. cruzi infections. Nevertheless, they represent good starting points for further iterative structure-based (re)design cycles. |
| Author | Musicò, Angelo Grifantini, Renata De Benedetti, Stefano Rigo, Cinzia Frigerio, Roberto Zanchetta, Nadia Gourlay, Louise Jane Bombaci, Mauro Gori, Alessandro Bolognesi, Martino Cretich, Marina Mileto, Davide Abelli, Sandra Colombo, Giorgio Pontillo, Angela Grande, Romualdo Rizzo, Alberto Fassi, Enrico Mario Alessandro Di Pisa, Flavio Mancon, Alessandro |
| AuthorAffiliation | 2 Consiglio Nazionale delle Ricerche, Istituto di Scienze e Tecnologie Chimiche “Giulio Natta” (SCITEC), Via Mario Bianco 9, 20131 Milano, Italy; enrico.fassi@unimi.it (E.M.A.F.); angelo.musico94@gmail.com (A.M.); roberto.frigerio94@gmail.com (R.F.); alessandro.gori@cnr.it (A.G.); marina.cretich@cnr.it (M.C.); g.colombo@unipv.it (G.C.) 8 Dipartimento di Chimica, Università di Pavia, V.le Taramelli 12, 27100 Pavia, Italy 1 Department of Biosciences, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy; DiPisa.Flavio@hsr.it (F.D.P.); stefano.debenedetti@unimi.it (S.D.B.); martino.bolognesi@unimi.it (M.B.) 4 Istituto Nazionale Genetica Molecolare, Padiglione Romeo ed Enrica Invernizzi, IRCCS Ospedale Maggiore Policlinico, 20122 Milano, Italy; bombaci@ingm.org (M.B.); grifantini@ingm.org (R.G.) 5 PRIMM S.r.l., Via Fatebenefratelli 15, 20121 Milano, Italy; angela.pontillo@primm.it 7 UOC Microbiologia Clinica, Virologia e Diagnostica delle Bioemergenze, ASST FBF Sacco, Via G.B Gr |
| AuthorAffiliation_xml | – name: 4 Istituto Nazionale Genetica Molecolare, Padiglione Romeo ed Enrica Invernizzi, IRCCS Ospedale Maggiore Policlinico, 20122 Milano, Italy; bombaci@ingm.org (M.B.); grifantini@ingm.org (R.G.) – name: 8 Dipartimento di Chimica, Università di Pavia, V.le Taramelli 12, 27100 Pavia, Italy – name: 5 PRIMM S.r.l., Via Fatebenefratelli 15, 20121 Milano, Italy; angela.pontillo@primm.it – name: 1 Department of Biosciences, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy; DiPisa.Flavio@hsr.it (F.D.P.); stefano.debenedetti@unimi.it (S.D.B.); martino.bolognesi@unimi.it (M.B.) – name: 2 Consiglio Nazionale delle Ricerche, Istituto di Scienze e Tecnologie Chimiche “Giulio Natta” (SCITEC), Via Mario Bianco 9, 20131 Milano, Italy; enrico.fassi@unimi.it (E.M.A.F.); angelo.musico94@gmail.com (A.M.); roberto.frigerio94@gmail.com (R.F.); alessandro.gori@cnr.it (A.G.); marina.cretich@cnr.it (M.C.); g.colombo@unipv.it (G.C.) – name: 9 Centro di Ricerca Pediatrica Romeo ed Enrica Invernizzi, Università degli Studi di Milano, 20133 Milano, Italy – name: 7 UOC Microbiologia Clinica, Virologia e Diagnostica delle Bioemergenze, ASST FBF Sacco, Via G.B Grassi, 74, 20157 Milano, Italy; grande.romualdo@asst-fbf-sacco.it (R.G.); nadia.zanchetta@asst-fbf-sacco.it (N.Z.); davide.mileto@unimi.it (D.M.); alessandro.mancon@unimi.it (A.M.); alberto.rizzo@asst-fbf-sacco.it (A.R.) – name: 3 Dipartimento di Scienze Farmaceutiche, Università degli Studi di Milano, Via L. Mangiagalli 25, 20133 Milano, Italy – name: 6 PRIMM S.r.l., Via dell’Artigianato 2, Dosson di Casier, 31030 Treviso, Italy; rigocinzia4@gmail.com (C.R.); sa.esse.sa@gmail.com (S.A.) |
| Author_xml | – sequence: 1 givenname: Flavio surname: Di Pisa fullname: Di Pisa, Flavio – sequence: 2 givenname: Stefano orcidid: 0000-0002-7787-9645 surname: De Benedetti fullname: De Benedetti, Stefano – sequence: 3 givenname: Enrico Mario Alessandro orcidid: 0000-0001-6282-4273 surname: Fassi fullname: Fassi, Enrico Mario Alessandro – sequence: 4 givenname: Mauro orcidid: 0000-0002-9887-4165 surname: Bombaci fullname: Bombaci, Mauro – sequence: 5 givenname: Renata surname: Grifantini fullname: Grifantini, Renata – sequence: 6 givenname: Angelo surname: Musicò fullname: Musicò, Angelo – sequence: 7 givenname: Roberto surname: Frigerio fullname: Frigerio, Roberto – sequence: 8 givenname: Angela surname: Pontillo fullname: Pontillo, Angela – sequence: 9 givenname: Cinzia surname: Rigo fullname: Rigo, Cinzia – sequence: 10 givenname: Sandra surname: Abelli fullname: Abelli, Sandra – sequence: 11 givenname: Romualdo surname: Grande fullname: Grande, Romualdo – sequence: 12 givenname: Nadia surname: Zanchetta fullname: Zanchetta, Nadia – sequence: 13 givenname: Davide surname: Mileto fullname: Mileto, Davide – sequence: 14 givenname: Alessandro surname: Mancon fullname: Mancon, Alessandro – sequence: 15 givenname: Alberto orcidid: 0000-0001-5999-006X surname: Rizzo fullname: Rizzo, Alberto – sequence: 16 givenname: Alessandro orcidid: 0000-0003-1640-7238 surname: Gori fullname: Gori, Alessandro – sequence: 17 givenname: Marina orcidid: 0000-0001-8251-5275 surname: Cretich fullname: Cretich, Marina – sequence: 18 givenname: Giorgio orcidid: 0000-0002-1318-668X surname: Colombo fullname: Colombo, Giorgio – sequence: 19 givenname: Martino orcidid: 0000-0002-9253-5170 surname: Bolognesi fullname: Bolognesi, Martino – sequence: 20 givenname: Louise Jane orcidid: 0000-0002-6369-2230 surname: Gourlay fullname: Gourlay, Louise Jane |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35062732$$D View this record in MEDLINE/PubMed |
| BookMark | eNpdks1v1DAQxS1UREvpnROyxIXLgj-SOLkglW2BSkUcWiRu1sQZZ71k7a2dVCq3_ud12FK1tSzZ8vv5-Wk8r8meDx4JecvZRykb9ukajHEeE2csT8VfkAPBVLWQjfy992i_T45SWrM8Gi7rSr0i-7JklVBSHJDb02EyroPR-Z6OK6TyhF6McTLjFJEGS4FeTNGCQfoDN20Ej_TYj65HT20MG3oZb7bgQwoboCZOfx2FNF_CGDoHfVZGZ-gXl_X4B-NsuVxBn6ETlxASviEvLQwJj-7XQ_Lr6-nl8vvi_Oe3s-Xx-cIUhRwXZYEIQlQVB1FCAYqV2HDRCGgsqIKBrAyUEuoSmJLKQlN3JbaFAGCNVY08JGc73y7AWm-jy4FudACn_x2E2GuIOeuAWoqyAKyUsCY_a3hb1lZh21kGBmzLstfnndd2ajfYGfRjhOGJ6VPFu5Xuw7WuVc1rNRt8uDeI4WrCNOqNSwaHIdc3TEmLSghRC1arjL5_hq7DFH0u1UxxqRTjVabePU70EOX_T2eA7QATQ0oR7QPCmZ77ST_vJ3kHBVPAbw |
| Cites_doi | 10.3390/vaccines9040322 10.1016/j.bpj.2010.01.014 10.1016/j.str.2012.10.005 10.1038/nprot.2008.91 10.1107/S0907444909042073 10.1021/acs.jpclett.0c02341 10.1038/nrmicro2893 10.1371/journal.pone.0007074 10.1002/pro.3053 10.1063/1.464397 10.1107/S0907444909047374 10.1016/j.jacc.2013.05.046 10.3390/molecules22030426 10.1590/S0036-46652002000100006 10.1107/S0907444905036693 10.1016/j.cpc.2012.09.022 10.3389/fpubh.2019.00166 10.1016/j.tibtech.2017.06.018 10.1021/acsinfecdis.8b00014 10.1016/S1473-3099(01)00065-2 10.1021/ac900658c 10.1002/bip.360320508 10.1021/acsinfecdis.5b00118 10.1016/j.chembiol.2013.07.010 10.1107/S0907444912001308 10.1111/cea.12929 10.1016/0021-9991(77)90098-5 10.1016/S1473-3099(20)30844-6 10.1001/jama.298.18.2171 10.1021/cb300487u 10.1093/bioinformatics/btz536 10.1371/journal.pntd.0007694 10.1006/jmbi.2000.4315 10.1371/journal.pntd.0000931 10.1074/mcp.M112.018713 10.1016/j.pt.2006.09.011 10.1107/S0907444909042589 10.1063/1.445869 10.1021/acs.bioconjchem.6b00426 10.1002/pmic.201200202 10.1021/acs.jcim.9b00588 10.1016/j.cplett.2003.12.039 10.1002/(SICI)1098-2825(1996)10:6<407::AID-JCLA16>3.0.CO;2-0 10.1002/jcc.20291 10.1172/JCI33945 10.1371/journal.pntd.0004216 10.1021/acs.jmedchem.8b02021 10.1038/srep20613 10.1016/j.bbagen.2017.09.012 10.1016/S0140-6736(10)60061-X 10.1107/S0907444904019158 10.1107/S0907444911007281 10.1021/acs.jctc.5b00255 10.1107/S0907444994003112 10.1016/S0002-9440(10)65052-3 10.1002/(SICI)1521-3773(19990115)38:1/2<236::AID-ANIE236>3.0.CO;2-M |
| ContentType | Journal Article |
| Copyright | 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2022 by the authors. 2022 |
| Copyright_xml | – notice: 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: 2022 by the authors. 2022 |
| DBID | AAYXX CITATION NPM 3V. 7T7 7XB 8FD 8FE 8FH 8FK 8G5 ABUWG AEUYN AFKRA AZQEC BBNVY BENPR BHPHI C1K CCPQU COVID DWQXO FR3 GNUQQ GUQSH HCIFZ LK8 M2O M7P MBDVC P64 PHGZM PHGZT PIMPY PKEHL PQEST PQGLB PQQKQ PQUKI PRINS Q9U 7X8 5PM DOA |
| DOI | 10.3390/vaccines10010071 |
| DatabaseName | CrossRef PubMed ProQuest Central (Corporate) Industrial and Applied Microbiology Abstracts (Microbiology A) ProQuest Central (purchase pre-March 2016) Technology Research Database ProQuest SciTech Collection ProQuest Natural Science Collection ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Research Library ProQuest Central (Alumni) One Sustainability ProQuest Central UK/Ireland ProQuest Central Essentials - QC Biological Science Collection ProQuest Central Natural Science Collection Environmental Sciences and Pollution Management ProQuest One Community College Coronavirus Research Database ProQuest Central Korea Engineering Research Database ProQuest Central Student ProQuest Research Library SciTech Premium Collection Biological Sciences Research Library Biological Science Database Research Library (Corporate) Biotechnology and BioEngineering Abstracts ProQuest Central Premium ProQuest One Academic (New) Publicly Available Content Database ProQuest One Academic Middle East (New) ProQuest One Academic Eastern Edition (DO NOT USE) One Applied & Life Sciences ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China ProQuest Central Basic MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
| DatabaseTitle | CrossRef PubMed Publicly Available Content Database Research Library Prep ProQuest Central Student Technology Research Database ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College Research Library (Alumni Edition) ProQuest Natural Science Collection ProQuest Central China Environmental Sciences and Pollution Management ProQuest Central ProQuest One Applied & Life Sciences ProQuest One Sustainability Natural Science Collection ProQuest Central Korea Biological Science Collection ProQuest Research Library Industrial and Applied Microbiology Abstracts (Microbiology A) ProQuest Central (New) ProQuest Biological Science Collection ProQuest Central Basic ProQuest One Academic Eastern Edition Coronavirus Research Database Biological Science Database ProQuest SciTech Collection Biotechnology and BioEngineering Abstracts ProQuest One Academic UKI Edition Engineering Research Database ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic |
| DatabaseTitleList | PubMed MEDLINE - Academic Publicly Available Content Database CrossRef |
| Database_xml | – sequence: 1 dbid: DOA name: Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: PIMPY name: Publicly Available Content Database url: http://search.proquest.com/publiccontent sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Pharmacy, Therapeutics, & Pharmacology |
| EISSN | 2076-393X |
| ExternalDocumentID | oai_doaj_org_article_3254ae672fc54ec1b58f7ebdf0acafb0 PMC8781870 35062732 10_3390_vaccines10010071 |
| Genre | Journal Article |
| GeographicLocations | United Kingdom--UK United States--US |
| GeographicLocations_xml | – name: United Kingdom--UK – name: United States--US |
| GrantInformation_xml | – fundername: Regione Lombardia grantid: 229472 – fundername: INEXT grantid: 5912 |
| GroupedDBID | 53G 5VS 8FE 8FH 8G5 AADQD AAHBH AAYXX ABUWG ADBBV AEUYN AFFHD AFKRA AFZYC ALMA_UNASSIGNED_HOLDINGS AOIJS AZQEC BBNVY BCNDV BENPR BHPHI BPHCQ CCPQU CITATION DIK DWQXO GNUQQ GROUPED_DOAJ GUQSH HCIFZ HYE IAO IHR ITC KQ8 LK8 M2O M48 M7P MODMG M~E OK1 PGMZT PHGZM PHGZT PIMPY PQGLB PQQKQ PROAC RNS RPM 3V. NPM 7T7 7XB 8FD 8FK C1K COVID FR3 MBDVC P64 PKEHL PQEST PQUKI PRINS Q9U 7X8 5PM |
| ID | FETCH-LOGICAL-c443t-54eea22661a25a4a705e91292a9fa740a36ca53a85a0737fa98d5eb42aa09f793 |
| IEDL.DBID | BENPR |
| ISICitedReferencesCount | 0 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000758418900001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 2076-393X |
| IngestDate | Fri Oct 03 12:27:22 EDT 2025 Tue Nov 04 02:00:50 EST 2025 Sun Nov 09 10:52:10 EST 2025 Fri Jul 25 11:58:58 EDT 2025 Thu Jan 02 22:55:58 EST 2025 Sat Nov 29 07:14:52 EST 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Keywords | in silico epitope mapping structural vaccinology Chagas disease neglected tropical disease peptide microarray immunodiagnostics Trypanosoma cruzi |
| Language | English |
| License | Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c443t-54eea22661a25a4a705e91292a9fa740a36ca53a85a0737fa98d5eb42aa09f793 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Current affiliation: Department of Food, Environmental and Nutritional Sciences, Università degli Studi di Milano, Via Celoria 2, 20133, Milano, Italy. Current affiliation: Biocrystallography Unit, Division of Immunology, Transplantation, and Infectious Diseases, IRCCS Scientific Institute San Raffaele, 20132 Milano, Italy. |
| ORCID | 0000-0002-7787-9645 0000-0001-8251-5275 0000-0002-9253-5170 0000-0001-6282-4273 0000-0002-6369-2230 0000-0002-9887-4165 0000-0001-5999-006X 0000-0003-1640-7238 0000-0002-1318-668X |
| OpenAccessLink | https://www.proquest.com/docview/2621377016?pq-origsite=%requestingapplication% |
| PMID | 35062732 |
| PQID | 2621377016 |
| PQPubID | 2032320 |
| ParticipantIDs | doaj_primary_oai_doaj_org_article_3254ae672fc54ec1b58f7ebdf0acafb0 pubmedcentral_primary_oai_pubmedcentral_nih_gov_8781870 proquest_miscellaneous_2622282087 proquest_journals_2621377016 pubmed_primary_35062732 crossref_primary_10_3390_vaccines10010071 |
| PublicationCentury | 2000 |
| PublicationDate | 20220103 |
| PublicationDateYYYYMMDD | 2022-01-03 |
| PublicationDate_xml | – month: 1 year: 2022 text: 20220103 day: 3 |
| PublicationDecade | 2020 |
| PublicationPlace | Switzerland |
| PublicationPlace_xml | – name: Switzerland – name: Basel |
| PublicationTitle | Vaccines (Basel) |
| PublicationTitleAlternate | Vaccines (Basel) |
| PublicationYear | 2022 |
| Publisher | MDPI AG MDPI |
| Publisher_xml | – name: MDPI AG – name: MDPI |
| References | Nervall (ref_42) 2004; 384 Jorgensen (ref_40) 1983; 79 ref_13 Scarabelli (ref_48) 2010; 98 ref_53 ref_19 ref_17 Ramaswamy (ref_31) 2016; 25 Sievers (ref_57) 2017; 47 Maier (ref_39) 2015; 11 Linciano (ref_15) 2019; 62 Gourlay (ref_22) 2013; 20 Lassaux (ref_56) 2013; 21 (ref_10) 2002; 44 ref_23 Montefiori (ref_50) 2019; 59 Sola (ref_58) 2018; 4 Gourlay (ref_20) 2017; 35 Dormitzer (ref_21) 2012; 10 Chen (ref_35) 2010; 66 ref_29 Nunes (ref_7) 2013; 62 Kabsch (ref_27) 2010; 66 Stuart (ref_5) 2008; 118 ref_26 Gori (ref_59) 2016; 2 Spyrakis (ref_14) 2017; 1861 Umezawa (ref_16) 1996; 10 Langer (ref_34) 2008; 3 Cretich (ref_37) 2009; 81 Evans (ref_28) 2005; 62 Schofield (ref_1) 2006; 22 Torrico (ref_11) 2021; 21 Walker (ref_43) 2013; 184 Lindahl (ref_47) 2005; 26 Daura (ref_46) 1999; 38 Afonine (ref_33) 2012; 68 Gori (ref_24) 2016; 27 Zingaretti (ref_36) 2012; 11 McNicholas (ref_54) 2011; 67 Krishnarjuna (ref_25) 2016; 6 Prata (ref_6) 2001; 1 Holm (ref_55) 2019; 35 Moraes (ref_12) 2019; 24 Rassi (ref_8) 2010; 375 Krogh (ref_52) 2001; 305 Loncharich (ref_41) 1992; 32 Serapian (ref_51) 2020; 11 Darden (ref_44) 1993; 98 Cretich (ref_38) 2012; 12 Lidani (ref_4) 2019; 7 Vagin (ref_30) 2009; 66 ref_3 ref_2 Peri (ref_49) 2012; 8 Bern (ref_18) 2007; 298 Emsley (ref_32) 2004; 60 Vago (ref_9) 2000; 156 Ryckaert (ref_45) 1977; 23 |
| References_xml | – ident: ref_23 doi: 10.3390/vaccines9040322 – volume: 98 start-page: 1966 year: 2010 ident: ref_48 article-title: Predicting Interaction Sites from the Energetics of Isolated Proteins: A New Approach to Epitope Mapping publication-title: Biophys. J. doi: 10.1016/j.bpj.2010.01.014 – volume: 21 start-page: 167 year: 2013 ident: ref_56 article-title: A Structure-Based Strategy for Epitope Discovery in Burkholderia pseudomallei OppA Antigen publication-title: Structure doi: 10.1016/j.str.2012.10.005 – volume: 3 start-page: 1171 year: 2008 ident: ref_34 article-title: Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 publication-title: Nat. Protoc. doi: 10.1038/nprot.2008.91 – volume: 66 start-page: 12 year: 2010 ident: ref_35 article-title: MolProbity: All-atom structure validation for macromolecular crystallography publication-title: Acta Cryst. D Biol. Crystallogr. doi: 10.1107/S0907444909042073 – volume: 11 start-page: 8084 year: 2020 ident: ref_51 article-title: The Answer Lies in the Energy: How Simple Atomistic Molecular Dynamics Simulations May Hold the Key to Epitope Prediction on the Fully Glycosylated SARS-CoV-2 Spike Protein publication-title: J. Phys. Chem. Lett. doi: 10.1021/acs.jpclett.0c02341 – volume: 10 start-page: 807 year: 2012 ident: ref_21 article-title: Structural vaccinology starts to deliver publication-title: Nat. Rev. Genet. doi: 10.1038/nrmicro2893 – ident: ref_53 doi: 10.1371/journal.pone.0007074 – volume: 25 start-page: 2297 year: 2016 ident: ref_31 article-title: Structural characterization reveals a novel bilobed architecture for the ectodomains of insect stage expressed Trypanosoma brucei PSSA-2 and Trypanosoma congolense ISA publication-title: Protein Sci. A Publ. Protein Soc. doi: 10.1002/pro.3053 – volume: 98 start-page: 10089 year: 1993 ident: ref_44 article-title: Particle mesh Ewald: An N log(N) method for Ewald sums in large systems publication-title: J. Chem. Phys. doi: 10.1063/1.464397 – volume: 66 start-page: 133 year: 2010 ident: ref_27 article-title: Integration, scaling, space-group assignment and post-refinement publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. doi: 10.1107/S0907444909047374 – volume: 62 start-page: 767 year: 2013 ident: ref_7 article-title: Chagas Disease: An Overview of Clinical and Epidemiological Aspects publication-title: J. Am. Coll. Cardiol. doi: 10.1016/j.jacc.2013.05.046 – ident: ref_13 doi: 10.3390/molecules22030426 – volume: 44 start-page: 29 year: 2002 ident: ref_10 article-title: Long term evaluation of etiological treatment of chagas disease with benznidazole publication-title: Rev. Inst. Med. Trop. São Paulo doi: 10.1590/S0036-46652002000100006 – volume: 62 start-page: 72 year: 2005 ident: ref_28 article-title: Scaling and assessment of data quality publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. doi: 10.1107/S0907444905036693 – volume: 184 start-page: 374 year: 2013 ident: ref_43 article-title: SPFP: Speed without compromise—A mixed precision model for GPU accelerated molecular dynamics simulations publication-title: Comput. Phys. Commun. doi: 10.1016/j.cpc.2012.09.022 – volume: 7 start-page: 166 year: 2019 ident: ref_4 article-title: Chagas Disease: From Discovery to a Worldwide Health Problem publication-title: Front. Public Health doi: 10.3389/fpubh.2019.00166 – volume: 35 start-page: 1208 year: 2017 ident: ref_20 article-title: Structure and Computation in Immunoreagent Design: From Diagnostics to Vaccines publication-title: Trends Biotechnol. doi: 10.1016/j.tibtech.2017.06.018 – volume: 4 start-page: 998 year: 2018 ident: ref_58 article-title: Enhancing Antibody Serodiagnosis Using a Controlled Peptide Coimmobilization Strategy publication-title: ACS Infect. Dis. doi: 10.1021/acsinfecdis.8b00014 – volume: 1 start-page: 92 year: 2001 ident: ref_6 article-title: Clinical and epidemiological aspects of Chagas disease publication-title: Lancet Infect. Dis. doi: 10.1016/S1473-3099(01)00065-2 – volume: 81 start-page: 5197 year: 2009 ident: ref_37 article-title: High Sensitivity Protein Assays on Microarray Silicon Slides publication-title: Anal. Chem. doi: 10.1021/ac900658c – volume: 32 start-page: 523 year: 1992 ident: ref_41 article-title: Langevin dynamics of peptides: The frictional dependence of isomerization rates ofN-acetylalanyl-N?-methylamide publication-title: Biopolymers doi: 10.1002/bip.360320508 – volume: 2 start-page: 221 year: 2016 ident: ref_59 article-title: Flexible vs Rigid Epitope Conformations for Diagnostic- and Vaccine-Oriented Applications: Novel Insights from the Burkholderia pseudomallei BPSL2765 Pal3 Epitope publication-title: ACS Infect. Dis. doi: 10.1021/acsinfecdis.5b00118 – volume: 20 start-page: 1147 year: 2013 ident: ref_22 article-title: Exploiting the Burkholderia pseudomallei Acute Phase Antigen BPSL2765 for Structure-Based Epitope Discovery/Design in Structural Vaccinology publication-title: Chem. Biol. doi: 10.1016/j.chembiol.2013.07.010 – volume: 68 start-page: 352 year: 2012 ident: ref_33 article-title: Towards automated crystallographic structure refinement with phenix.refine publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. doi: 10.1107/S0907444912001308 – volume: 47 start-page: 1057 year: 2017 ident: ref_57 article-title: Performance of a polymer coated silicon microarray for simultaneous detection of food allergen-specific IgE and IgG4 publication-title: Clin. Exp. Allergy doi: 10.1111/cea.12929 – volume: 23 start-page: 327 year: 1977 ident: ref_45 article-title: Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes publication-title: J. Comput. Phys. doi: 10.1016/0021-9991(77)90098-5 – volume: 21 start-page: 1129 year: 2021 ident: ref_11 article-title: New regimens of benznidazole monotherapy and in combination with fosravuconazole for treatment of Chagas disease (BENDITA): A phase 2, double-blind, randomised trial publication-title: Lancet Infect. Dis. doi: 10.1016/S1473-3099(20)30844-6 – volume: 298 start-page: 2171 year: 2007 ident: ref_18 article-title: Evaluation and Treatment of Chagas Disease in the United States publication-title: JAMA J. Am. Med. Assoc. doi: 10.1001/jama.298.18.2171 – volume: 8 start-page: 397 year: 2012 ident: ref_49 article-title: Rational Epitope Design for Protein Targeting publication-title: ACS Chem. Biol. doi: 10.1021/cb300487u – volume: 35 start-page: 5326 year: 2019 ident: ref_55 article-title: Benchmarking fold detection by DaliLite v.5 publication-title: Bioinformation doi: 10.1093/bioinformatics/btz536 – ident: ref_17 doi: 10.1371/journal.pntd.0007694 – volume: 305 start-page: 567 year: 2001 ident: ref_52 article-title: Predicting transmembrane protein topology with a hidden markov model: Application to complete genomes publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.4315 – ident: ref_19 doi: 10.1371/journal.pntd.0000931 – volume: 24 start-page: 346 year: 2019 ident: ref_12 article-title: Accelerating Drug Discovery Efforts for Trypanosomatidic Infections Using an Integrated Transnational Academic Drug Discovery Platform publication-title: SLAS Discov. Adv. Life Sci. R&D – volume: 11 start-page: 1885 year: 2012 ident: ref_36 article-title: Identification of New Autoantigens by Protein Array Indicates a Role for IL4 Neutralization in Autoimmune Hepatitis publication-title: Mol. Cell. Proteom. doi: 10.1074/mcp.M112.018713 – ident: ref_3 – volume: 22 start-page: 583 year: 2006 ident: ref_1 article-title: The future of Chagas disease control publication-title: Trends Parasitol. doi: 10.1016/j.pt.2006.09.011 – volume: 66 start-page: 22 year: 2009 ident: ref_30 article-title: Molecular replacement withMOLREP publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. doi: 10.1107/S0907444909042589 – volume: 79 start-page: 926 year: 1983 ident: ref_40 article-title: Comparison of simple potential functions for simulating liquid water publication-title: J. Chem. Phys. doi: 10.1063/1.445869 – volume: 27 start-page: 2669 year: 2016 ident: ref_24 article-title: Screening Complex Biological Samples with Peptide Microarrays: The Favorable Impact of Probe Orientation via Chemoselective Immobilization Strategies on Clickable Polymeric Coatings publication-title: Bioconjugate Chem. doi: 10.1021/acs.bioconjchem.6b00426 – volume: 12 start-page: 2963 year: 2012 ident: ref_38 article-title: Interferometric silicon biochips for label and label-free DNA and protein microarrays publication-title: Proteomics doi: 10.1002/pmic.201200202 – volume: 59 start-page: 3927 year: 2019 ident: ref_50 article-title: Impact of Mutations on NPAC Structural Dynamics: Mechanistic Insights from MD Simulations publication-title: J. Chem. Inf. Model. doi: 10.1021/acs.jcim.9b00588 – volume: 384 start-page: 288 year: 2004 ident: ref_42 article-title: Molecular dynamics simulations of water and biomolecules with a Monte Carlo constant pressure algorithm publication-title: Chem. Phys. Lett. doi: 10.1016/j.cplett.2003.12.039 – volume: 10 start-page: 407 year: 1996 ident: ref_16 article-title: Changes in isotype composition and antigen recognition of anti-Trypanosoma cruzi antibodies from acute to chronic Chagas disease publication-title: J. Clin. Lab. Anal. doi: 10.1002/(SICI)1098-2825(1996)10:6<407::AID-JCLA16>3.0.CO;2-0 – volume: 26 start-page: 1701 year: 2005 ident: ref_47 article-title: GROMACS: Fast, flexible, and free publication-title: J. Comput. Chem. doi: 10.1002/jcc.20291 – volume: 118 start-page: 1301 year: 2008 ident: ref_5 article-title: Kinetoplastids: Related protozoan pathogens, different diseases publication-title: J. Clin. Investig. doi: 10.1172/JCI33945 – ident: ref_26 doi: 10.1371/journal.pntd.0004216 – volume: 62 start-page: 3989 year: 2019 ident: ref_15 article-title: Enhancement of Benzothiazoles as Pteridine Reductase-1 Inhibitors for the Treatment of Trypanosomatidic Infections publication-title: J. Med. Chem. doi: 10.1021/acs.jmedchem.8b02021 – volume: 6 start-page: 20613 year: 2016 ident: ref_25 article-title: Strain-transcending immune response generated by chimeras of the malaria vaccine candidate merozoite surface protein 2 publication-title: Sci. Rep. doi: 10.1038/srep20613 – ident: ref_2 – volume: 1861 start-page: 3215 year: 2017 ident: ref_14 article-title: Comparative mapping of on-targets and off-targets for the discovery of anti-trypanosomatid folate pathway inhibitors publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbagen.2017.09.012 – volume: 375 start-page: 1388 year: 2010 ident: ref_8 article-title: Chagas disease publication-title: Lancet doi: 10.1016/S0140-6736(10)60061-X – volume: 60 start-page: 2126 year: 2004 ident: ref_32 article-title: Coot: Model-building tools for molecular graphics publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444904019158 – volume: 67 start-page: 386 year: 2011 ident: ref_54 article-title: Presenting your structures: The CCP4mgmolecular-graphics software publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. doi: 10.1107/S0907444911007281 – volume: 11 start-page: 3696 year: 2015 ident: ref_39 article-title: ff14SB: Improving the accuracy of protein side chain and backbone parameters from ff99SB publication-title: J. Chem. Theory Comput. doi: 10.1021/acs.jctc.5b00255 – ident: ref_29 doi: 10.1107/S0907444994003112 – volume: 156 start-page: 1805 year: 2000 ident: ref_9 article-title: Genetic Characterization of Trypanosoma cruzi Directly from Tissues of Patients with Chronic Chagas Disease publication-title: Am. J. Pathol. doi: 10.1016/S0002-9440(10)65052-3 – volume: 38 start-page: 236 year: 1999 ident: ref_46 article-title: Peptide folding: When simulation meets experiment publication-title: Angew. Chem. Int. Ed. doi: 10.1002/(SICI)1521-3773(19990115)38:1/2<236::AID-ANIE236>3.0.CO;2-M |
| SSID | ssj0000913867 |
| Score | 2.180326 |
| Snippet | Chagas disease (CD) is a vector-borne parasitosis, caused by the protozoan parasite Trypanosoma cruzi, that affects millions of people worldwide. Although... Chagas disease (CD) is a vector-borne parasitosis, caused by the protozoan parasite , that affects millions of people worldwide. Although endemic in South... |
| SourceID | doaj pubmedcentral proquest pubmed crossref |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database |
| StartPage | 71 |
| SubjectTerms | Antibodies Antigens Asymptomatic Biomarkers Chagas disease Climate change Cloning Crystal structure Crystallization Diagnostic systems Epitopes Immunogenicity Immunology in silico epitope mapping Infections Membranes neglected tropical disease Parasites Parasitic diseases Pathogens peptide microarray Peptides Polyclonal antibodies Proteins structural vaccinology Trypanosoma cruzi Vector-borne diseases |
| SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1La9wwEBYl9NBL6btu06JCCRRi4tXDko950kvDQraQmxnLUmKa2MVeBza3_POOpM1mNxR66dWSbEnztmY-EfI1d8JVzP-5z3Odor02KdTapqbItQCp3USacNmEOj3V5-fFdO2qL58TFuGB48btcYxgwOaKOSOFNZMKxytb1S4DA64K0Tp6PWvBVNDBxYTrXMVzSY5x_d4NGH9SPXjMIW9XN-xQgOv_m4_5OFVyzfacvCDPl04j3Y-TfUme2PYV2ZlG1OnFLp09FFENu3SHTh_wqBevyd3x1WgaX8bQXlD09yg_omcBNnbsLe0cBXo29g6MpT_sNUbPraX77dzDdFJffUJn_QJ1Rjd010BNP942FAY_yKLyjZl6-GF60GB7_8v2_pWHl3CBnY7i8c8b8vPkeHb4PV3evJAaIfg8xZ22wLztBiZBgMqkLdAzYFA4UCIDnhuQHLQEVBHKQaFraSvBALLCoci_JVtt19r3hGbacuBC1R41yAiMoIzCBVVSFVrmuk7It3s6lL8jwEaJgYmnWfmYZgk58IRa9fPQ2OEBMky5ZJjyXwyTkO17MpdLeR1KljMPvYj-b0K-rJpR0vzxCW57N4Y-DAPUTKuEvItcsZoJlx7umbOEqA1-2ZjqZkvbXAY0b63QZ1LZh_-xto_kGfPlGSFNbptsIS_ZT-SpuZk3Q_85iMgfkZUcAA priority: 102 providerName: Directory of Open Access Journals |
| Title | Elucidating the 3D Structure of a Surface Membrane Antigen from Trypanosoma cruzi as a Serodiagnostic Biomarker of Chagas Disease |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/35062732 https://www.proquest.com/docview/2621377016 https://www.proquest.com/docview/2622282087 https://pubmed.ncbi.nlm.nih.gov/PMC8781870 https://doaj.org/article/3254ae672fc54ec1b58f7ebdf0acafb0 |
| Volume | 10 |
| WOSCitedRecordID | wos000758418900001&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: Directory of Open Access Journals customDbUrl: eissn: 2076-393X dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000913867 issn: 2076-393X databaseCode: DOA dateStart: 20130101 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: 2076-393X dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000913867 issn: 2076-393X databaseCode: M~E dateStart: 20130101 isFulltext: true titleUrlDefault: https://road.issn.org providerName: ISSN International Centre – providerCode: PRVPQU databaseName: Biological Science Database customDbUrl: eissn: 2076-393X dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000913867 issn: 2076-393X databaseCode: M7P dateStart: 20130301 isFulltext: true titleUrlDefault: http://search.proquest.com/biologicalscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 2076-393X dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000913867 issn: 2076-393X databaseCode: BENPR dateStart: 20130301 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: Publicly Available Content Database customDbUrl: eissn: 2076-393X dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000913867 issn: 2076-393X databaseCode: PIMPY dateStart: 20130301 isFulltext: true titleUrlDefault: http://search.proquest.com/publiccontent providerName: ProQuest – providerCode: PRVPQU databaseName: Research Library customDbUrl: eissn: 2076-393X dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000913867 issn: 2076-393X databaseCode: M2O dateStart: 20130301 isFulltext: true titleUrlDefault: https://search.proquest.com/pqrl providerName: ProQuest |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3Nb9MwFLdYx4EL34zAqIyEJiEtWuZ82DmhdesEh5aIFamcohfH6SJYMpJ2Ujkg8Z_zXpK2dEJcuPgQO8lL3vPz-_LPjL0JMi9LBEXug0DZuF5rG1JlbB0GygNfZce-bg6bkOOxmk7DqAu41V1Z5UonNoo6LTXFyI9EIAgcDy2Ud9ffbTo1irKr3REaO2yXkMq8HtsdDMfRp3WUhVAvVSDb_KSL_v3RDWjKWNeEPUTr69Z61MD2_83WvF0y-ccadP7gf6l_yO531ic_acXlEbtjisfsIGrhq5eHfLLZjVUf8gMebYCtl0_Yr-G3hc5pP0Qx42g4cveMXzT4s4vK8DLjwC8WVQba8JG5Qje8MPykmBPeJ6dtLHxSLVH5lHV5BVxXix85h5puMqjF25I_fDEf5NhffTUVPfL0EmY46KzNIz1ln8-Hk9P3dneEg609z53bvmcMCDICQPjggXR8E6KJISDMQHoOuIEG3wXlA-oamUGoUt8kngBwwgx1xzPWK8rCPGfcUcYF15MpwQ9pD10xLfGDEl-Gyg9UarG3K0bG1y1SR4weDjE9vs10iw2I0-txhLHdXCirWdxN2dhF3xlMIEWm8TP0cYKSK02SZg5oyBLHYvsrXsfdxK_jDaMt9nrdjVOW8jD428tFM0agp-soabG9VqzWlLg-4Ua7wmJyS-C2SN3uKfLLBhZcSTS-pPPi32S9ZPcE7eBoKun2WQ-lxLxid_XNPK-rPtuRU9XvZlG_CVBgOxIfqZURtT-H2B99GEVffgOJszAT |
| linkProvider | ProQuest |
| linkToHtml | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9QwELaqggQX3o9AASNBJaRGTZ04dg4Itd1WrdquVuoi9ZZOHHu7giYl2S1abvwhfiMzye6WrRC3HrjGTuI4n2fGnplvGHsXu8hlgk7u41j7qK-ND7m2vkliHYHUbkOaptiE6nb1yUnSW2K_ZrkwFFY5k4mNoM5LQ2fk6yIWRI6HFsqni28-VY0i7-qshEYLiwM7-Y5btvrjfgf_73shdnf623v-tKqAb6IoHPkyshYE6SUQEiJQgbQJaj0BiQMVBRDGBmQIWgLCXzlIdC5tFgmAIHGKyJdQ5N9CM0LoJlSwNz_TIY5NHavWGxqGSbB-CYb84zUxHZE2X9B-TZGAv1m21wM0_9B4u_f_t7l6wO5NbWu-2S6Gh2zJFo_Yaq8l556s8f5Vrlm9xld574q2e_KY_dz5OjZDyvYoBhzNYh52-HHDrjuuLC8dB348rhwYy4_seYY63vLNYkRsppySdHi_mqBoLevyHLipxj-GHGq6yaKOagMa8cV8a4jt1Rdb0SO3z2CAnTqtl-wJ-3wj0_OULRdlYZ8zHmgbQhipnMiVTIQbTaPwgzKpEi1jnXvswww46UXLQ5Li_o1All4Hmce2CFnzfsQg3lwoq0E6FUhpKGQENlbCGfwMs5HhulQ2y10ABlwWeGxlhq10Ktbq9ApYHns7b0aBRF4mnPZy3PQRuI8PtPLYsxbG85GEklixQ-ExtQDwhaEuthTDs4b0XCs0LVXw4t_DesPu7PWPDtPD_e7BS3ZXUK5KEzO4wpYRMfYVu20uR8O6et2sXM5Obxr-vwFNRIQS |
| linkToPdf | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9NAEF5VLUJceD8MBRYJKiHVqrv2etcHhJomEVUhimiRejPj9TqNoHaxk6Jw42_x65ixnYRUiFsPXLPrZL355rE7M98w9jLMgiwRdHMfhtpFe21cSLV1TRTqAKTOdqWpm02owUCfnETDNfZrXgtDaZVznVgr6rQwdEe-I0JB5HiUm5W1aRHDbv_t-TeXOkhRpHXeTqOByKGdfcfjW_XmoIv_9Ssh-r3j_Xdu22HANUHgT1wZWAuCbBQICQEoT9oILaCAKAMVeOCHBqQPWgKKgsog0qm0SSAAvChTRMSE6n9DoZOB0rXR6Q2GHxc3PMS4qUPVxEZ9P_J2LsBQtLwi3iOy7Su2sG4Z8Dc_93K65h_2r3_rf9652-xm63XzvUZM7rA1m99lW8OGtnu2zY-XVWjVNt_iwyWh9-we-9n7OjVjqgPJRxwdZu53-VHNuzstLS8yDvxoWmZgLP9gzxK0_pbv5RPiOeVUvsOPyxkq3aIqzoCbcvpjzKGihyxarybVEX-Yd8Y4Xn6xJX3l_imMcFK3iZ_dZ5-uZHsesPW8yO0jxj1tffADlRLtkgnwCGoUvlAiVaRlqFOHvZ6DKD5vGEpiPNkR4OLLgHNYh1C2mEfc4vUHRTmKW1UV-0IGYEMlMoOvYXYTlFhlkzTzwECWeA7bnOMsbhVeFS9B5rAXi2FUVRR_wm0vpvUcgSd8TyuHPWwgvViJL4kv2xcOUytgX1nq6kg-Pq3p0LVCp1N5j_-9rOfsOqI-fn8wOHzCbggqYqmTCTfZOgLGPmXXzMVkXJXPWjHm7PNV4_83fWWOIg |
| 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=Elucidating+the+3D+Structure+of+a+Surface+Membrane+Antigen+from+Trypanosoma+cruzi+as+a+Serodiagnostic+Biomarker+of+Chagas+Disease&rft.jtitle=Vaccines+%28Basel%29&rft.au=Di+Pisa%2C+Flavio&rft.au=De+Benedetti%2C+Stefano&rft.au=Fassi%2C+Enrico+Mario+Alessandro&rft.au=Bombaci%2C+Mauro&rft.date=2022-01-03&rft.issn=2076-393X&rft.eissn=2076-393X&rft.volume=10&rft.issue=1&rft.spage=71&rft_id=info:doi/10.3390%2Fvaccines10010071&rft.externalDBID=n%2Fa&rft.externalDocID=10_3390_vaccines10010071 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2076-393X&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2076-393X&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2076-393X&client=summon |