The role of Mannose Binding Lectin in the immune response against Borrelia burgdorferi sensu lato

The causative agents of Lyme borreliosis, spirochetes belonging to the Borrelia burgdorferi sensu lato group, have developed several ways to protect themselves against killing by the host complement system. In addition, it has been shown that serum sensitive isolates are (partially) protected by the...

Full description

Saved in:

Bibliographic Details
Published in:	Scientific reports Vol. 9; no. 1; p. 1431
Main Authors:	Coumou, Jeroen, Wagemakers, Alex, Narasimhan, Sukanya, Schuijt, Tim J., Ersoz, Jasmin I., Oei, Anneke, de Boer, Onno J., Roelofs, Joris J. T. H., Fikrig, Erol, Hovius, Joppe W.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 05.02.2019 Nature Publishing Group
Subjects:	14/34 631/250/262 631/326/421 64/60 692/420/254 82 Borrelia burgdorferi Borreliosis Complement activation Humanities and Social Sciences Immune clearance Immune response Immunoglobulin G Immunoglobulins Infectious diseases Lectins Leukocyte migration Macrophages Mannose multidisciplinary Oligosaccharides Peritoneum Phagocytosis Salivary gland Science Science (multidisciplinary) Skin Spirochetes
ISSN:	2045-2322, 2045-2322
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Abstract	The causative agents of Lyme borreliosis, spirochetes belonging to the Borrelia burgdorferi sensu lato group, have developed several ways to protect themselves against killing by the host complement system. In addition, it has been shown that serum sensitive isolates are (partially) protected by the Ixodes Tick Salivary Lectin Pathway Inhibitor (TSLPI) protein; a salivary gland protein that inhibits the function of Mannose Binding Lectin (MBL). MBL is a C-type lectin that recognizes oligosaccharides on pathogens and activates the complement system via the lectin pathway. MBL deficiency has been linked to a more severe course of several infectious diseases and humans with detectable antibodies against B. burgdorferi are significantly more often MBL deficient compared to humans without antibodies against B. burgdorferi . Here we set out to investigate the role of MBL in the immune response against B. burgdorferi in more detail. We demonstrate that B. burgdorferi N40 needle-infected C57BL/6 MBL deficient mice harbored significantly higher B. burgdorferi numbers in skin tissue during the early course of infection. In line with these findings they also developed higher anti- B. burgdorferi IgG serum antibodies compared to WT controls. In contrast , B. burgdorferi loads in distant tissue such as heart, joints or bladder at later time points were similar for both mouse strains. These in vivo findings were corroborated using a B. burgdorferi N40-infected I. scapularis infestation model. We showed that MBL is capable of binding B. burgdorferi through its carbohydrate recognition domains, but in vitro complement killing assays, peritoneal macrophage and whole blood stimulations, phagocytosis assays and an in vivo migration experiment did not reveal the mechanism by which MBL facilitates early clearance of B. burgdorferi . To conclude, we show a protective role of MBL in the early stages of B. burgdorferi infection, yet the underlying mechanism warrants further investigation.
AbstractList	The causative agents of Lyme borreliosis, spirochetes belonging to the Borrelia burgdorferi sensu lato group, have developed several ways to protect themselves against killing by the host complement system. In addition, it has been shown that serum sensitive isolates are (partially) protected by the Ixodes Tick Salivary Lectin Pathway Inhibitor (TSLPI) protein; a salivary gland protein that inhibits the function of Mannose Binding Lectin (MBL). MBL is a C-type lectin that recognizes oligosaccharides on pathogens and activates the complement system via the lectin pathway. MBL deficiency has been linked to a more severe course of several infectious diseases and humans with detectable antibodies against B. burgdorferi are significantly more often MBL deficient compared to humans without antibodies against B. burgdorferi. Here we set out to investigate the role of MBL in the immune response against B. burgdorferi in more detail. We demonstrate that B. burgdorferi N40 needle-infected C57BL/6 MBL deficient mice harbored significantly higher B. burgdorferi numbers in skin tissue during the early course of infection. In line with these findings they also developed higher anti-B. burgdorferi IgG serum antibodies compared to WT controls. In contrast, B. burgdorferi loads in distant tissue such as heart, joints or bladder at later time points were similar for both mouse strains. These in vivo findings were corroborated using a B. burgdorferi N40-infected I. scapularis infestation model. We showed that MBL is capable of binding B. burgdorferi through its carbohydrate recognition domains, but in vitro complement killing assays, peritoneal macrophage and whole blood stimulations, phagocytosis assays and an in vivo migration experiment did not reveal the mechanism by which MBL facilitates early clearance of B. burgdorferi. To conclude, we show a protective role of MBL in the early stages of B. burgdorferi infection, yet the underlying mechanism warrants further investigation.The causative agents of Lyme borreliosis, spirochetes belonging to the Borrelia burgdorferi sensu lato group, have developed several ways to protect themselves against killing by the host complement system. In addition, it has been shown that serum sensitive isolates are (partially) protected by the Ixodes Tick Salivary Lectin Pathway Inhibitor (TSLPI) protein; a salivary gland protein that inhibits the function of Mannose Binding Lectin (MBL). MBL is a C-type lectin that recognizes oligosaccharides on pathogens and activates the complement system via the lectin pathway. MBL deficiency has been linked to a more severe course of several infectious diseases and humans with detectable antibodies against B. burgdorferi are significantly more often MBL deficient compared to humans without antibodies against B. burgdorferi. Here we set out to investigate the role of MBL in the immune response against B. burgdorferi in more detail. We demonstrate that B. burgdorferi N40 needle-infected C57BL/6 MBL deficient mice harbored significantly higher B. burgdorferi numbers in skin tissue during the early course of infection. In line with these findings they also developed higher anti-B. burgdorferi IgG serum antibodies compared to WT controls. In contrast, B. burgdorferi loads in distant tissue such as heart, joints or bladder at later time points were similar for both mouse strains. These in vivo findings were corroborated using a B. burgdorferi N40-infected I. scapularis infestation model. We showed that MBL is capable of binding B. burgdorferi through its carbohydrate recognition domains, but in vitro complement killing assays, peritoneal macrophage and whole blood stimulations, phagocytosis assays and an in vivo migration experiment did not reveal the mechanism by which MBL facilitates early clearance of B. burgdorferi. To conclude, we show a protective role of MBL in the early stages of B. burgdorferi infection, yet the underlying mechanism warrants further investigation. The causative agents of Lyme borreliosis, spirochetes belonging to the Borrelia burgdorferi sensu lato group, have developed several ways to protect themselves against killing by the host complement system. In addition, it has been shown that serum sensitive isolates are (partially) protected by the Ixodes Tick Salivary Lectin Pathway Inhibitor (TSLPI) protein; a salivary gland protein that inhibits the function of Mannose Binding Lectin (MBL). MBL is a C-type lectin that recognizes oligosaccharides on pathogens and activates the complement system via the lectin pathway. MBL deficiency has been linked to a more severe course of several infectious diseases and humans with detectable antibodies against B. burgdorferi are significantly more often MBL deficient compared to humans without antibodies against B. burgdorferi. Here we set out to investigate the role of MBL in the immune response against B. burgdorferi in more detail. We demonstrate that B. burgdorferi N40 needle-infected C57BL/6 MBL deficient mice harbored significantly higher B. burgdorferi numbers in skin tissue during the early course of infection. In line with these findings they also developed higher anti-B. burgdorferi IgG serum antibodies compared to WT controls. In contrast, B. burgdorferi loads in distant tissue such as heart, joints or bladder at later time points were similar for both mouse strains. These in vivo findings were corroborated using a B. burgdorferi N40-infected I. scapularis infestation model. We showed that MBL is capable of binding B. burgdorferi through its carbohydrate recognition domains, but in vitro complement killing assays, peritoneal macrophage and whole blood stimulations, phagocytosis assays and an in vivo migration experiment did not reveal the mechanism by which MBL facilitates early clearance of B. burgdorferi. To conclude, we show a protective role of MBL in the early stages of B. burgdorferi infection, yet the underlying mechanism warrants further investigation. The causative agents of Lyme borreliosis, spirochetes belonging to the Borrelia burgdorferi sensu lato group, have developed several ways to protect themselves against killing by the host complement system. In addition, it has been shown that serum sensitive isolates are (partially) protected by the Ixodes Tick Salivary Lectin Pathway Inhibitor (TSLPI) protein; a salivary gland protein that inhibits the function of Mannose Binding Lectin (MBL). MBL is a C-type lectin that recognizes oligosaccharides on pathogens and activates the complement system via the lectin pathway. MBL deficiency has been linked to a more severe course of several infectious diseases and humans with detectable antibodies against B. burgdorferi are significantly more often MBL deficient compared to humans without antibodies against B. burgdorferi . Here we set out to investigate the role of MBL in the immune response against B. burgdorferi in more detail. We demonstrate that B. burgdorferi N40 needle-infected C57BL/6 MBL deficient mice harbored significantly higher B. burgdorferi numbers in skin tissue during the early course of infection. In line with these findings they also developed higher anti- B. burgdorferi IgG serum antibodies compared to WT controls. In contrast , B. burgdorferi loads in distant tissue such as heart, joints or bladder at later time points were similar for both mouse strains. These in vivo findings were corroborated using a B. burgdorferi N40-infected I. scapularis infestation model. We showed that MBL is capable of binding B. burgdorferi through its carbohydrate recognition domains, but in vitro complement killing assays, peritoneal macrophage and whole blood stimulations, phagocytosis assays and an in vivo migration experiment did not reveal the mechanism by which MBL facilitates early clearance of B. burgdorferi . To conclude, we show a protective role of MBL in the early stages of B. burgdorferi infection, yet the underlying mechanism warrants further investigation.
ArticleNumber	1431
Author	Schuijt, Tim J. Wagemakers, Alex Oei, Anneke Ersoz, Jasmin I. Fikrig, Erol Roelofs, Joris J. T. H. de Boer, Onno J. Hovius, Joppe W. Coumou, Jeroen Narasimhan, Sukanya
Author_xml	– sequence: 1 givenname: Jeroen surname: Coumou fullname: Coumou, Jeroen email: lyme@amc.uva.nl organization: Amsterdam UMC, University of Amsterdam, Center for Experimental and Molecular Medicine – sequence: 2 givenname: Alex orcidid: 0000-0001-9632-7830 surname: Wagemakers fullname: Wagemakers, Alex organization: Amsterdam UMC, University of Amsterdam, Center for Experimental and Molecular Medicine – sequence: 3 givenname: Sukanya surname: Narasimhan fullname: Narasimhan, Sukanya organization: Department of Internal Medicine, Yale University School of Medicine – sequence: 4 givenname: Tim J. surname: Schuijt fullname: Schuijt, Tim J. organization: Amsterdam UMC, University of Amsterdam, Center for Experimental and Molecular Medicine – sequence: 5 givenname: Jasmin I. surname: Ersoz fullname: Ersoz, Jasmin I. organization: Amsterdam UMC, University of Amsterdam, Center for Experimental and Molecular Medicine – sequence: 6 givenname: Anneke surname: Oei fullname: Oei, Anneke organization: Amsterdam UMC, University of Amsterdam, Department of Medical Microbiology – sequence: 7 givenname: Onno J. surname: de Boer fullname: de Boer, Onno J. organization: Amsterdam UMC, University of Amsterdam, Department of Pathology, Amsterdam Cardiovascular Sciences, Amsterdam Infection & Immunity – sequence: 8 givenname: Joris J. T. H. surname: Roelofs fullname: Roelofs, Joris J. T. H. organization: Amsterdam UMC, University of Amsterdam, Department of Pathology, Amsterdam Cardiovascular Sciences, Amsterdam Infection & Immunity – sequence: 9 givenname: Erol surname: Fikrig fullname: Fikrig, Erol organization: Department of Internal Medicine, Yale University School of Medicine – sequence: 10 givenname: Joppe W. surname: Hovius fullname: Hovius, Joppe W. organization: Amsterdam UMC, University of Amsterdam, Center for Experimental and Molecular Medicine
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/30723261$$D View this record in MEDLINE/PubMed
BookMark	eNp9kU9vFSEUxYmpsX_sF3BhSNy4GQXuMAMbE19jq8kzbuqa8Jg7U5oZeMJME7-9tK_VZxePkEByf-fkwDklRyEGJOQNZx84A_Ux11xqVTGuKmi1EJV6QU4Eq2UlQIijvfsxOc_5lpUlha65fkWOgbVl0vATYq9vkKY4Io09_W5DiBnpyofOh4Gu0c0-0LLnQvlpWkKBMW9jKJQdrA95pquYEo7e0s2Shi6mHpOnGUNe6Gjn-Jq87O2Y8fzxPCM_L79cX3yt1j-uvl18XleullJVCiQ4rfjGOiUa6N1GcYXS8RZrzQV2su40YgEUOAmiBtnZFrl0XSegqeGMfNr5bpfNhJ3DMCc7mm3yk02_TbTe_D8J_sYM8c400EALuhi8fzRI8deCeTaTzw7H0QaMSzZCCM0UKM0K-u4ZehuXFMrzjOBtIyRTrC3U2_1Ef6M8_X4B1A5wKeacsDfOz3b28T6gHw1n5r5rs-valK7NQ9dGFal4Jn1yPyiCnSgXOAyY_sU-oPoD1A27rw
CitedBy_id	crossref_primary_10_3389_fcimb_2022_809052 crossref_primary_10_1016_j_tim_2021_06_011 crossref_primary_10_1016_j_tim_2022_08_002 crossref_primary_10_1038_s41598_020_73517_y crossref_primary_10_1016_j_ebiom_2023_104825 crossref_primary_10_1186_s13071_020_04442_2 crossref_primary_10_1371_journal_ppat_1012032 crossref_primary_10_1038_s41579_020_0400_5 crossref_primary_10_1038_s41598_020_76268_y crossref_primary_10_1016_j_tim_2020_05_004 crossref_primary_10_1111_cas_15991 crossref_primary_10_3389_fimmu_2020_583845 crossref_primary_10_3390_pathogens13110976 crossref_primary_10_1016_j_it_2021_05_005 crossref_primary_10_1093_cid_ciz872 crossref_primary_10_1088_2050_6120_ac4e72 crossref_primary_10_17816_EID532724 crossref_primary_10_1371_journal_ppat_1009030 crossref_primary_10_3389_fcimb_2023_1253670
Cites_doi	10.1016/S0140-6736(11)60103-7 10.1016/j.molimm.2009.11.028 10.1038/ni.1923 10.1016/j.chom.2011.06.010 10.4049/jimmunol.164.5.2610 10.1038/nrmicro2714 10.1086/590006 10.1016/j.pt.2012.12.001 10.4049/jimmunol.175.4.2534 10.1128/IAI.00949-09 10.1126/science.7043737 10.1089/vbz.2015.1901 10.1056/NEJM200107123450207 10.1371/journal.ppat.1000447 10.1084/jem.170.4.1427 10.1128/IAI.68.2.688-693.2000 10.1084/jem.20071164 10.1016/j.molimm.2014.06.005 10.1371/journal.ppat.1004278 10.1038/gt.2014.87 10.4049/jimmunol.170.6.3214 10.1093/clinids/17.4.708 10.1007/BF01967434 10.1586/eri.11.136 10.1128/IAI.00232-08 10.4049/jimmunol.175.5.3299 10.1016/j.pt.2007.07.001 10.1016/S0171-2985(00)80094-7 10.1084/jem.20032207 10.1016/j.jim.2009.11.003 10.1002/pmic.200500187 10.1016/j.molimm.2014.07.007 10.1093/hmg/ddl193 10.4049/jimmunol.1402128 10.1128/iai.65.4.1228-1236.1997
ContentType	Journal Article
Copyright	The Author(s) 2019 This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Copyright_xml	– notice: The Author(s) 2019 – notice: This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
DBID	C6C AAYXX CITATION NPM 3V. 7X7 7XB 88A 88E 88I 8FE 8FH 8FI 8FJ 8FK ABUWG AEUYN AFKRA AZQEC BBNVY BENPR BHPHI CCPQU DWQXO FYUFA GHDGH GNUQQ HCIFZ K9. LK8 M0S M1P M2P M7P PHGZM PHGZT PIMPY PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS Q9U 7X8 5PM
DOI	10.1038/s41598-018-37922-8
DatabaseName	Springer Nature OA Free Journals CrossRef PubMed ProQuest Central (Corporate) ProQuest Health & Medical Collection ProQuest Central (purchase pre-March 2016) Biology Database (Alumni Edition) Medical Database (Alumni Edition) Science Database (Alumni Edition) ProQuest SciTech Collection ProQuest Natural Science Collection ProQuest Hospital Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) One Sustainability ProQuest Central UK/Ireland ProQuest Central Essentials - QC Biological Science Collection ProQuest Central Database Suite (ProQuest) Natural Science Collection ProQuest One ProQuest Central Korea Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student SciTech Collection (ProQuest) ProQuest Health & Medical Complete (Alumni) Biological Sciences ProQuest Health & Medical Collection PML(ProQuest Medical Library) Science Database Biological Science Database ProQuest Central Premium ProQuest One Academic (New) ProQuest Publicly Available Content ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing 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)
DatabaseTitle	CrossRef PubMed Publicly Available Content Database ProQuest Central Student ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Central China ProQuest Biology Journals (Alumni Edition) ProQuest Central ProQuest One Applied & Life Sciences ProQuest One Sustainability ProQuest Health & Medical Research Collection Health Research Premium Collection Health and Medicine Complete (Alumni Edition) Natural Science Collection ProQuest Central Korea Health & Medical Research Collection Biological Science Collection ProQuest Central (New) ProQuest Medical Library (Alumni) ProQuest Science Journals (Alumni Edition) ProQuest Biological Science Collection ProQuest Central Basic ProQuest Science Journals ProQuest One Academic Eastern Edition ProQuest Hospital Collection Health Research Premium Collection (Alumni) Biological Science Database ProQuest SciTech Collection ProQuest Hospital Collection (Alumni) ProQuest Health & Medical Complete ProQuest Medical Library ProQuest One Academic UKI Edition ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic
DatabaseTitleList	MEDLINE - Academic PubMed CrossRef Publicly Available Content Database
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: PIMPY name: ProQuest Publicly Available Content url: http://search.proquest.com/publiccontent sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Biology
EISSN	2045-2322
ExternalDocumentID	PMC6363739 30723261 10_1038_s41598_018_37922_8
Genre	Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural
GrantInformation_xml	– fundername: NIAID NIH HHS grantid: P01 AI138949 – fundername: Howard Hughes Medical Institute
GroupedDBID	0R~ 3V. 4.4 53G 5VS 7X7 88A 88E 88I 8FE 8FH 8FI 8FJ AAFWJ AAJSJ AAKDD ABDBF ABUWG ACGFS ACSMW ACUHS ADBBV ADRAZ AENEX AEUYN AFKRA AJTQC ALIPV ALMA_UNASSIGNED_HOLDINGS AOIJS AZQEC BAWUL BBNVY BCNDV BENPR BHPHI BPHCQ BVXVI C6C CCPQU DIK DWQXO EBD EBLON EBS EJD ESX FYUFA GNUQQ GROUPED_DOAJ GX1 HCIFZ HH5 HMCUK HYE KQ8 LK8 M0L M1P M2P M48 M7P M~E NAO OK1 PIMPY PQQKQ PROAC PSQYO RNT RNTTT RPM SNYQT UKHRP AASML AAYXX AFFHD AFPKN CITATION PHGZM PHGZT PJZUB PPXIY PQGLB NPM 7XB 8FK K9. PKEHL PQEST PQUKI PRINS Q9U 7X8 5PM
ID	FETCH-LOGICAL-c4558-8353c981bac8263fcb818e5c17e4912ed54d9ee81b83c532435da7e15cdd23643
IEDL.DBID	M2P
ISSN	2045-2322
IngestDate	Tue Nov 04 02:03:08 EST 2025 Sun Nov 09 11:34:12 EST 2025 Tue Oct 07 07:44:10 EDT 2025 Thu Jan 02 22:58:36 EST 2025 Sat Nov 29 02:11:46 EST 2025 Tue Nov 18 22:32:20 EST 2025 Fri Feb 21 02:38:44 EST 2025
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	1
Language	English
License	Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c4558-8353c981bac8263fcb818e5c17e4912ed54d9ee81b83c532435da7e15cdd23643
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ORCID	0000-0001-9632-7830
OpenAccessLink	https://www.proquest.com/docview/2176250807?pq-origsite=%requestingapplication%
PMID	30723261
PQID	2176250807
PQPubID	2041939
ParticipantIDs	pubmedcentral_primary_oai_pubmedcentral_nih_gov_6363739 proquest_miscellaneous_2229083890 proquest_journals_2176250807 pubmed_primary_30723261 crossref_citationtrail_10_1038_s41598_018_37922_8 crossref_primary_10_1038_s41598_018_37922_8 springer_journals_10_1038_s41598_018_37922_8
PublicationCentury	2000
PublicationDate	20190205
PublicationDateYYYYMMDD	2019-02-05
PublicationDate_xml	– month: 2 year: 2019 text: 20190205 day: 5
PublicationDecade	2010
PublicationPlace	London
PublicationPlace_xml	– name: London – name: England
PublicationTitle	Scientific reports
PublicationTitleAbbrev	Sci Rep
PublicationTitleAlternate	Sci Rep
PublicationYear	2019
Publisher	Nature Publishing Group UK Nature Publishing Group
Publisher_xml	– name: Nature Publishing Group UK – name: Nature Publishing Group
References	Verdu (CR16) 2006; 15 Schroder (CR25) 2005; 175 Pietikainen, Meri, Blom, Meri (CR10) 2010; 47 Hovius, van Dam, Fikrig (CR5) 2007; 23 CR19 Wagemakers (CR26) 2014; 21 Kuiper, van Dam, Moll van Charante, Nauta, Dankert (CR30) 1993; 12 Keizer, Wouters, Schlapbach, Kuijpers (CR17) 2014; 61 Shi (CR20) 2004; 199 de Taeye, Kreuk, van Dam, Hovius, Schuijt (CR6) 2013; 29 van Dam (CR3) 1993; 17 van Dam (CR11) 1997; 65 Wagemakers (CR13) 2016; 16 Brooks (CR8) 2005; 175 Burgdorfer (CR1) 1982; 216 Kraiczy (CR23) 2000; 201 Schaible (CR27) 1989; 170 Pausa (CR9) 2003; 170 Narasimhan (CR31) 2014; 10 Stanek, Wormser, Gray, Strle (CR4) 2012; 379 Hansen, Thiel, Willis, Holmskov, Jensenius (CR21) 2000; 164 Genster (CR22) 2014; 61 Neth (CR32) 2000; 68 Ip, Takahashi, Moore, Stuart, Ezekowitz (CR14) 2008; 205 Nowalk, Nolder, Clifton, Carroll (CR33) 2006; 6 Hovius (CR24) 2009; 5 Lachmann (CR29) 2010; 352 Schuijt (CR34) 2008; 76 Schuijt (CR12) 2011; 10 van der Windt, van ‘t Veer, Florquin, van der Poll (CR35) 2010; 78 Eisen (CR15) 2008; 47 Radolf, Caimano, Stevenson, Hu (CR28) 2012; 10 Steere (CR2) 2001; 345 Ricklin, Hajishengallis, Yang, Lambris (CR7) 2010; 11 Takahashi (CR18) 2011; 9 L Shi (37922_CR20) 2004; 199 AP van Dam (37922_CR3) 1993; 17 GJ van der Windt (37922_CR35) 2010; 78 NW Schroder (37922_CR25) 2005; 175 PJ Lachmann (37922_CR29) 2010; 352 UE Schaible (37922_CR27) 1989; 170 H Kuiper (37922_CR30) 1993; 12 S Hansen (37922_CR21) 2000; 164 CS Brooks (37922_CR8) 2005; 175 WK Ip (37922_CR14) 2008; 205 K Takahashi (37922_CR18) 2011; 9 P Verdu (37922_CR16) 2006; 15 W Burgdorfer (37922_CR1) 1982; 216 SW de Taeye (37922_CR6) 2013; 29 37922_CR19 JW Hovius (37922_CR5) 2007; 23 N Genster (37922_CR22) 2014; 61 S Narasimhan (37922_CR31) 2014; 10 DP Eisen (37922_CR15) 2008; 47 O Neth (37922_CR32) 2000; 68 A Wagemakers (37922_CR13) 2016; 16 D Ricklin (37922_CR7) 2010; 11 AP van Dam (37922_CR11) 1997; 65 AC Steere (37922_CR2) 2001; 345 A Wagemakers (37922_CR26) 2014; 21 JW Hovius (37922_CR24) 2009; 5 MP Keizer (37922_CR17) 2014; 61 J Pietikainen (37922_CR10) 2010; 47 AJ Nowalk (37922_CR33) 2006; 6 P Kraiczy (37922_CR23) 2000; 201 G Stanek (37922_CR4) 2012; 379 TJ Schuijt (37922_CR34) 2008; 76 M Pausa (37922_CR9) 2003; 170 TJ Schuijt (37922_CR12) 2011; 10 JD Radolf (37922_CR28) 2012; 10
References_xml	– volume: 379 start-page: 461 year: 2012 end-page: 473 ident: CR4 article-title: Lyme borreliosis publication-title: Lancet doi: 10.1016/S0140-6736(11)60103-7 – volume: 47 start-page: 1299 year: 2010 end-page: 1305 ident: CR10 article-title: Binding of the complement inhibitor C4b-binding protein to Lyme disease Borreliae publication-title: Mol Immunol doi: 10.1016/j.molimm.2009.11.028 – volume: 65 start-page: 1228 year: 1997 end-page: 1236 ident: CR11 article-title: Complement-mediated serum sensitivity among spirochetes that cause Lyme disease publication-title: Infection and immunity – volume: 11 start-page: 785 year: 2010 end-page: 797 ident: CR7 article-title: Complement: a key system for immune surveillance and homeostasis publication-title: Nat Immunol doi: 10.1038/ni.1923 – volume: 10 start-page: 136 year: 2011 end-page: 146 ident: CR12 article-title: A tick mannose-binding lectin inhibitor interferes with the vertebrate complement cascade to enhance transmission of the lyme disease agent publication-title: Cell host & microbe doi: 10.1016/j.chom.2011.06.010 – volume: 164 start-page: 2610 year: 2000 end-page: 2618 ident: CR21 article-title: Purification and characterization of two mannan-binding lectins from mouse serum publication-title: J Immunol doi: 10.4049/jimmunol.164.5.2610 – volume: 10 start-page: 87 year: 2012 end-page: 99 ident: CR28 article-title: Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes publication-title: Nat Rev Microbiol doi: 10.1038/nrmicro2714 – volume: 47 start-page: 510 year: 2008 end-page: 516 ident: CR15 article-title: Low serum mannose-binding lectin level increases the risk of death due to pneumococcal infection publication-title: Clin Infect Dis doi: 10.1086/590006 – volume: 29 start-page: 119 year: 2013 end-page: 128 ident: CR6 article-title: Complement evasion by Borrelia burgdorferi: it takes three to tango publication-title: Trends Parasitol doi: 10.1016/j.pt.2012.12.001 – volume: 175 start-page: 2534 year: 2005 end-page: 2540 ident: CR25 article-title: Heterozygous Arg753Gln polymorphism of human TLR-2 impairs immune activation by Borrelia burgdorferi and protects from late stage Lyme disease publication-title: J Immunol doi: 10.4049/jimmunol.175.4.2534 – volume: 78 start-page: 115 year: 2010 end-page: 124 ident: CR35 article-title: CD44 deficiency is associated with enhanced Escherichia coli-induced proinflammatory cytokine and chemokine release by peritoneal macrophages publication-title: Infect Immun doi: 10.1128/IAI.00949-09 – volume: 216 start-page: 1317 year: 1982 end-page: 1319 ident: CR1 article-title: Lyme disease-a tick-borne spirochetosis? publication-title: Science doi: 10.1126/science.7043737 – volume: 16 start-page: 223 year: 2016 end-page: 228 ident: CR13 article-title: An Ixodes ricinus Tick Salivary Lectin Pathway Inhibitor Protects Borrelia burgdorferi sensu lato from HumanComplement publication-title: Vector borne and zoonotic diseases doi: 10.1089/vbz.2015.1901 – volume: 345 start-page: 115 year: 2001 end-page: 125 ident: CR2 article-title: Lyme disease publication-title: N Engl J Med doi: 10.1056/NEJM200107123450207 – volume: 5 start-page: e1000447 year: 2009 ident: CR24 article-title: The urokinase receptor (uPAR) facilitates clearance of Borrelia burgdorferi publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1000447 – volume: 170 start-page: 1427 year: 1989 end-page: 1432 ident: CR27 article-title: The severe combined immunodeficiency (scid) mouse. A laboratory model for the analysis of Lyme arthritis and carditis publication-title: J Exp Med doi: 10.1084/jem.170.4.1427 – volume: 68 start-page: 688 year: 2000 end-page: 693 ident: CR32 article-title: Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition publication-title: Infect Immun doi: 10.1128/IAI.68.2.688-693.2000 – volume: 205 start-page: 169 year: 2008 end-page: 181 ident: CR14 article-title: Mannose-binding lectin enhances Toll-like receptors 2 and 6 signaling from the phagosome publication-title: J Exp Med doi: 10.1084/jem.20071164 – ident: CR19 – volume: 61 start-page: 174 year: 2014 end-page: 184 ident: CR17 article-title: Restoration of MBL-deficiency: redefining the safety, efficacy and viability of MBL-substitution therapy publication-title: Mol Immunol doi: 10.1016/j.molimm.2014.06.005 – volume: 10 start-page: e1004278 year: 2014 ident: CR31 article-title: A Tick Gut Protein with Fibronectin III Domains Aids Borrelia burgdorferi Congregation to the Gut during Transmission publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1004278 – volume: 21 start-page: 1051 year: 2014 end-page: 1057 ident: CR26 article-title: Rapid outer-surface protein C DNA tattoo vaccination protects against Borrelia afzelii infection publication-title: Gene Ther doi: 10.1038/gt.2014.87 – volume: 170 start-page: 3214 year: 2003 end-page: 3222 ident: CR9 article-title: Serum-resistant strains of Borrelia burgdorferi evade complement-mediated killing by expressing a CD59-like complement inhibitory molecule publication-title: J Immunol doi: 10.4049/jimmunol.170.6.3214 – volume: 17 start-page: 708 year: 1993 end-page: 717 ident: CR3 article-title: Different genospecies of Borrelia burgdorferi are associated with distinct clinical manifestations of Lyme borreliosis publication-title: Clin Infect Dis doi: 10.1093/clinids/17.4.708 – volume: 12 start-page: 413 year: 1993 end-page: 418 ident: CR30 article-title: One year follow-up study to assess the prevalence and incidence of Lyme borreliosis among Dutch forestry workers publication-title: Eur J Clin Microbiol Infect Dis doi: 10.1007/BF01967434 – volume: 9 start-page: 1179 year: 2011 end-page: 1190 ident: CR18 article-title: Mannose-binding lectin and the balance between immune protection and complication publication-title: Expert Rev Anti Infect Ther doi: 10.1586/eri.11.136 – volume: 76 start-page: 2888 year: 2008 end-page: 2894 ident: CR34 article-title: The tick salivary protein Salp15 inhibits the killing of serum-sensitive Borrelia burgdorferi sensu lato isolates publication-title: Infect Immun doi: 10.1128/IAI.00232-08 – volume: 175 start-page: 3299 year: 2005 end-page: 3308 ident: CR8 article-title: Complement regulator-acquiring surface protein 1 imparts resistance to human serum in Borrelia burgdorferi publication-title: J Immunol doi: 10.4049/jimmunol.175.5.3299 – volume: 23 start-page: 434 year: 2007 end-page: 438 ident: CR5 article-title: Tick-host-pathogen interactions in Lyme borreliosis publication-title: Trends Parasitol doi: 10.1016/j.pt.2007.07.001 – volume: 201 start-page: 406 year: 2000 end-page: 419 ident: CR23 article-title: Comparison of two laboratory methods for the determination of serum resistance in Borrelia burgdorferi isolates publication-title: Immunobiology doi: 10.1016/S0171-2985(00)80094-7 – volume: 199 start-page: 1379 year: 2004 end-page: 1390 ident: CR20 article-title: Mannose-binding lectin-deficient mice are susceptible to infection with Staphylococcus aureus publication-title: J Exp Med doi: 10.1084/jem.20032207 – volume: 352 start-page: 195 year: 2010 end-page: 197 ident: CR29 article-title: Preparing serum for functional complement assays publication-title: J Immunol Methods doi: 10.1016/j.jim.2009.11.003 – volume: 6 start-page: 2121 year: 2006 end-page: 2134 ident: CR33 article-title: Comparative proteome analysis of subcellular fractions from Borrelia burgdorferi by NEPHGE and IPG publication-title: Proteomics doi: 10.1002/pmic.200500187 – volume: 61 start-page: 59 year: 2014 end-page: 68 ident: CR22 article-title: Lessons learned from mice deficient in lectin complement pathway molecules publication-title: Mol Immunol doi: 10.1016/j.molimm.2014.07.007 – volume: 15 start-page: 2650 year: 2006 end-page: 2658 ident: CR16 article-title: Evolutionary insights into the high worldwide prevalence of MBL2 deficiency alleles publication-title: Hum Mol Genet doi: 10.1093/hmg/ddl193 – volume: 379 start-page: 461 year: 2012 ident: 37922_CR4 publication-title: Lancet doi: 10.1016/S0140-6736(11)60103-7 – volume: 47 start-page: 1299 year: 2010 ident: 37922_CR10 publication-title: Mol Immunol doi: 10.1016/j.molimm.2009.11.028 – volume: 21 start-page: 1051 year: 2014 ident: 37922_CR26 publication-title: Gene Ther doi: 10.1038/gt.2014.87 – volume: 23 start-page: 434 year: 2007 ident: 37922_CR5 publication-title: Trends Parasitol doi: 10.1016/j.pt.2007.07.001 – volume: 15 start-page: 2650 year: 2006 ident: 37922_CR16 publication-title: Hum Mol Genet doi: 10.1093/hmg/ddl193 – volume: 170 start-page: 3214 year: 2003 ident: 37922_CR9 publication-title: J Immunol doi: 10.4049/jimmunol.170.6.3214 – volume: 12 start-page: 413 year: 1993 ident: 37922_CR30 publication-title: Eur J Clin Microbiol Infect Dis doi: 10.1007/BF01967434 – volume: 216 start-page: 1317 year: 1982 ident: 37922_CR1 publication-title: Science doi: 10.1126/science.7043737 – volume: 199 start-page: 1379 year: 2004 ident: 37922_CR20 publication-title: J Exp Med doi: 10.1084/jem.20032207 – volume: 61 start-page: 174 year: 2014 ident: 37922_CR17 publication-title: Mol Immunol doi: 10.1016/j.molimm.2014.06.005 – volume: 9 start-page: 1179 year: 2011 ident: 37922_CR18 publication-title: Expert Rev Anti Infect Ther doi: 10.1586/eri.11.136 – ident: 37922_CR19 doi: 10.4049/jimmunol.1402128 – volume: 29 start-page: 119 year: 2013 ident: 37922_CR6 publication-title: Trends Parasitol doi: 10.1016/j.pt.2012.12.001 – volume: 175 start-page: 3299 year: 2005 ident: 37922_CR8 publication-title: J Immunol doi: 10.4049/jimmunol.175.5.3299 – volume: 201 start-page: 406 year: 2000 ident: 37922_CR23 publication-title: Immunobiology doi: 10.1016/S0171-2985(00)80094-7 – volume: 10 start-page: e1004278 year: 2014 ident: 37922_CR31 publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1004278 – volume: 47 start-page: 510 year: 2008 ident: 37922_CR15 publication-title: Clin Infect Dis doi: 10.1086/590006 – volume: 205 start-page: 169 year: 2008 ident: 37922_CR14 publication-title: J Exp Med doi: 10.1084/jem.20071164 – volume: 16 start-page: 223 year: 2016 ident: 37922_CR13 publication-title: Vector borne and zoonotic diseases doi: 10.1089/vbz.2015.1901 – volume: 68 start-page: 688 year: 2000 ident: 37922_CR32 publication-title: Infect Immun doi: 10.1128/IAI.68.2.688-693.2000 – volume: 10 start-page: 136 year: 2011 ident: 37922_CR12 publication-title: Cell host & microbe doi: 10.1016/j.chom.2011.06.010 – volume: 5 start-page: e1000447 year: 2009 ident: 37922_CR24 publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1000447 – volume: 10 start-page: 87 year: 2012 ident: 37922_CR28 publication-title: Nat Rev Microbiol doi: 10.1038/nrmicro2714 – volume: 345 start-page: 115 year: 2001 ident: 37922_CR2 publication-title: N Engl J Med doi: 10.1056/NEJM200107123450207 – volume: 6 start-page: 2121 year: 2006 ident: 37922_CR33 publication-title: Proteomics doi: 10.1002/pmic.200500187 – volume: 11 start-page: 785 year: 2010 ident: 37922_CR7 publication-title: Nat Immunol doi: 10.1038/ni.1923 – volume: 76 start-page: 2888 year: 2008 ident: 37922_CR34 publication-title: Infect Immun doi: 10.1128/IAI.00232-08 – volume: 170 start-page: 1427 year: 1989 ident: 37922_CR27 publication-title: J Exp Med doi: 10.1084/jem.170.4.1427 – volume: 175 start-page: 2534 year: 2005 ident: 37922_CR25 publication-title: J Immunol doi: 10.4049/jimmunol.175.4.2534 – volume: 61 start-page: 59 year: 2014 ident: 37922_CR22 publication-title: Mol Immunol doi: 10.1016/j.molimm.2014.07.007 – volume: 78 start-page: 115 year: 2010 ident: 37922_CR35 publication-title: Infect Immun doi: 10.1128/IAI.00949-09 – volume: 164 start-page: 2610 year: 2000 ident: 37922_CR21 publication-title: J Immunol doi: 10.4049/jimmunol.164.5.2610 – volume: 17 start-page: 708 year: 1993 ident: 37922_CR3 publication-title: Clin Infect Dis doi: 10.1093/clinids/17.4.708 – volume: 65 start-page: 1228 year: 1997 ident: 37922_CR11 publication-title: Infection and immunity doi: 10.1128/iai.65.4.1228-1236.1997 – volume: 352 start-page: 195 year: 2010 ident: 37922_CR29 publication-title: J Immunol Methods doi: 10.1016/j.jim.2009.11.003
SSID	ssj0000529419
Score	2.3673182
Snippet	The causative agents of Lyme borreliosis, spirochetes belonging to the Borrelia burgdorferi sensu lato group, have developed several ways to protect themselves... The causative agents of Lyme borreliosis, spirochetes belonging to the Borrelia burgdorferi sensu lato group, have developed several ways to protect themselves...
SourceID	pubmedcentral proquest pubmed crossref springer
SourceType	Open Access Repository Aggregation Database Index Database Enrichment Source Publisher
StartPage	1431
SubjectTerms	14/34 631/250/262 631/326/421 64/60 692/420/254 82 Borrelia burgdorferi Borreliosis Complement activation Humanities and Social Sciences Immune clearance Immune response Immunoglobulin G Immunoglobulins Infectious diseases Lectins Leukocyte migration Macrophages Mannose multidisciplinary Oligosaccharides Peritoneum Phagocytosis Salivary gland Science Science (multidisciplinary) Skin Spirochetes
Title	The role of Mannose Binding Lectin in the immune response against Borrelia burgdorferi sensu lato
URI	https://link.springer.com/article/10.1038/s41598-018-37922-8 https://www.ncbi.nlm.nih.gov/pubmed/30723261 https://www.proquest.com/docview/2176250807 https://www.proquest.com/docview/2229083890 https://pubmed.ncbi.nlm.nih.gov/PMC6363739
Volume	9
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVAON databaseName: DOAJ Open Access Full Text customDbUrl: eissn: 2045-2322 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000529419 issn: 2045-2322 databaseCode: DOA dateStart: 20110101 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: 2045-2322 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000529419 issn: 2045-2322 databaseCode: M~E dateStart: 20110101 isFulltext: true titleUrlDefault: https://road.issn.org providerName: ISSN International Centre – providerCode: PRVPQU databaseName: Biological Science Database customDbUrl: eissn: 2045-2322 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000529419 issn: 2045-2322 databaseCode: M7P dateStart: 20110101 isFulltext: true titleUrlDefault: http://search.proquest.com/biologicalscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 2045-2322 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000529419 issn: 2045-2322 databaseCode: BENPR dateStart: 20110101 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Health & Medical Collection customDbUrl: eissn: 2045-2322 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000529419 issn: 2045-2322 databaseCode: 7X7 dateStart: 20110101 isFulltext: true titleUrlDefault: https://search.proquest.com/healthcomplete providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Publicly Available Content customDbUrl: eissn: 2045-2322 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000529419 issn: 2045-2322 databaseCode: PIMPY dateStart: 20110101 isFulltext: true titleUrlDefault: http://search.proquest.com/publiccontent providerName: ProQuest – providerCode: PRVPQU databaseName: Science Database customDbUrl: eissn: 2045-2322 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000529419 issn: 2045-2322 databaseCode: M2P dateStart: 20110101 isFulltext: true titleUrlDefault: https://search.proquest.com/sciencejournals providerName: ProQuest
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1bi9QwFD64Owq-eL9U1yGCb1q2aZpJ8iSO7KKwOxRRGJ9Km6RrYWjX6a7gv_ectDPLuLgvQslLTmnDueRLzg3gTZI5ZZ1J40p6F1NqZWxq1EfjpRYeMXRVh64lJ2qx0MulyccLt34Mq9zYxGCoXWfpjvwQoTNCdcQ36v35z5i6RpF3dWyhsQcTRDacQrpO03x7x0JerIybMVcmEfqwx_2Kcsq4Rs0yeA7Tu_vRNZB5PVbyL4dp2IeO7__vCh7AvRGBsg-DyDyEW759BHeGnpS_H0OJgsMo5pB1NaMWyl3v2bwJyS_shMxjy_BB3Mgayi1B4iHM1rPyrGwQbbI5dfxYNSUjF47r1jVKOeuppwZb4Rn_CXw7Pvr68VM89mGIbSaljhGkCWsQ35YWDyOithXu8l5arnxmeOqdzJzxHgm0sBIRmpCuVJ5L6xzVpxdPYb_tWv8cWFolDm1EUqd2lvnUVWhRhOCycklV8cpEwDfcKOxYpJx6ZayK4CwXuhg4WCAHi8DBQkfwdvvO-VCi40bqgw13ilFd--KKNRG83k6jopH3pGx9d4k0VBlfI75LIng2yMT2c2goEZnOeARqR1q2BFTEe3embX6EYt4zMRNK4MLfbeTq6rf-vYoXN6_iJdxFYGdCdLk8gP2L9aV_Bbftr4umX09hTy1VGPUUJvOjRf5lGu4ipkF9aFQ4TvLPp_n3P1LEH_E
linkProvider	ProQuest
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V3JbtRAEC2FAIIL-2II0EhwAiu22z3uPiBEgChRhlEOQcrNcS8GSyM7jCeg_BTfSFV7iYaI3HJA8s3lpe1XVc-uDeBVlNrMWJWEWjgbUmllqErUR-WE5A45tC791JJpNpvJw0O1vwa_h1oYSqscbKI31LYx9I98E6kzUnXkN9n74x8hTY2i6OowQqODxZ47_YWfbO273U_4fl8nyfbng487YT9VIDSpEDJEysGNQrZWGKTWvDQafZYTJs5cquLEWZFa5RwKSG4E8g0ubJG5WBhrqds6x_NegaspdRajVMFkf_ynQ1GzNFZ9bU7E5WaL_pFq2GKJmqzwu0-u-r9zpPZ8buZfAVrv97Zv_29P7A7c6hk2-9CpxF1Yc_U9uN7N3Dy9DwUqBqOcStaUjEZEN61jW5Uv7mFTMv81ww15MauodgaFuzRix4pvRYVsmm3RRJN5VTAKUdlmUaIWs5ZmhrB5sWwewNdLWd9DWK-b2j0GlujIog2MysRMUpdYjRaT81hoG2kdaxVAPLz93PRN2GkWyDz3yQBc5h1ickRM7hGTywDejMccdy1ILpTeGNCQ9-aozc-gEMDLcTcaEooOFbVrTlCGOv9L5K9RAI86DI6XQ0eAzHsSB5CtoHMUoCblq3vq6rtvVj7hE55xXPjbAcdnt_XvVTy5eBUv4MbOwZdpPt2d7T2Fm0hilc-kFxuwvlycuGdwzfxcVu3iuVdQBkeXje8_voV0aQ
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9NAEB6VFBAX3rSGAosEJ7Bie73x7gEhSomIGqIcQConY--uqaXIbuOUqn-tv44Zv6pQ0VsPSLl5Y2edb2Y-ex4fwGsvNJE2KnBTYY1LrZWuytAelRWSW-TQaVarlkyj2UweHKj5Bpx3vTBUVtn5xNpRm1LTO_IhUmek6shvomHWlkXM98Yfjo5dUpCiTGsnp9FAZN-eneLjW_V-sof_9ZsgGH_-9umL2yoMuDoUQrpIP7hWyNwSjTSbZzrF-GWF9iMbKj-wRoRGWYsLJNcCuQcXJomsL7QxNHmd43lvwCZS8jAYwOZ88nX-o3_DQzm00Fdtp47H5bDCaEkdbb5Eu1b4FCjXo-Elinu5UvOvdG0dBcf3_uf7dx_uttybfWyM5QFs2OIh3GrUOM8eQYImw6jakpUZI_HosrJsN6_bftiUAkPB8IOMmeXUVYOLmwJjy5JfSY48m-2S1skiTxglr0y5zNC-WUVqImyRrMrH8P1a9vcEBkVZ2G1gQeoZ9I5eFuhRaAOToi_l3Bep8dLUT5UDfoeEWLfj2UklZBHXZQJcxg16YkRPXKMnlg687b9z1AwnuXL1ToeMuHVUVXwBCwde9YfRxVDeKClseYJrSBNAIrP1HNhq8NhfDkMEcvKR70C0htR-AY0vXz9S5If1GPMRH_GI48bfdZi--Fn_3sXTq3fxEm4jrOPpZLb_DO4gu1V1ib3YgcFqeWKfw039e5VXyxettTL4ed0A_wNWZ36y
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=The+role+of+Mannose+Binding+Lectin+in+the+immune+response+against+Borrelia+burgdorferi+sensu+lato&rft.jtitle=Scientific+reports&rft.au=Coumou+Jeroen&rft.au=Wagemakers+Alex&rft.au=Narasimhan+Sukanya&rft.au=Schuijt+Tim+J&rft.date=2019-02-05&rft.pub=Nature+Publishing+Group&rft.eissn=2045-2322&rft.volume=9&rft.issue=1&rft_id=info:doi/10.1038%2Fs41598-018-37922-8&rft.externalDBID=HAS_PDF_LINK
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2045-2322&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2045-2322&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2045-2322&client=summon