6iec: Difference between revisions
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==Structure of RVFV Gn and human monoclonal antibody R17== | |||
<StructureSection load='6iec' size='340' side='right'caption='[[6iec]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6iec]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IEC FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6iec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iec OCA], [http://pdbe.org/6iec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iec RCSB], [http://www.ebi.ac.uk/pdbsum/6iec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iec ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rift Valley fever virus (RVFV) is a mosquito-borne pathogen that causes substantial morbidity and mortality in livestock and humans. To date, there are no licensed human vaccines or therapeutics available. Here, we report the isolation of monoclonal antibodies from a convalescent patient, targeting the RVFV envelope proteins Gn and Gc. The Gn-specific monoclonal antibodies exhibited much higher neutralizing activities in vitro and protection efficacies in mice against RVFV infection, compared to the Gc-specific monoclonal antibodies. The Gn monoclonal antibodies were found to interfere with soluble Gn binding to cells and prevent infection by blocking the attachment of virions to host cells. Structural analysis of Gn complexed with four Gn-specific monoclonal antibodies resulted in the definition of three antigenic patches (A, B and C) on Gn domain I. Both patches A and B are major neutralizing epitopes. Our results highlight the potential of antibody-based therapeutics and provide a structure-based rationale for designing vaccines against RVFV. | |||
Neutralization mechanism of human monoclonal antibodies against Rift Valley fever virus.,Wang Q, Ma T, Wu Y, Chen Z, Zeng H, Tong Z, Gao F, Qi J, Zhao Z, Chai Y, Yang H, Wong G, Bi Y, Wu L, Shi R, Yang M, Song J, Jiang H, An Z, Wang J, Yilma TD, Shi Y, Liu WJ, Liang M, Qin C, Gao GF, Yan J Nat Microbiol. 2019 Apr 1. pii: 10.1038/s41564-019-0411-z. doi:, 10.1038/s41564-019-0411-z. PMID:30936489<ref>PMID:30936489</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6iec" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Gao, F]] | [[Category: Gao, F]] | ||
[[Category: Wang, Q | [[Category: Gao, G F]] | ||
[[Category: Qi, J X]] | |||
[[Category: Wang, Q H]] | |||
[[Category: Wu, Y]] | [[Category: Wu, Y]] | ||
[[Category: Antibody]] | |||
[[Category: Rvfv]] | |||
[[Category: Structural protein]] | |||
[[Category: Structural protein-immune system complex]] | |||
Revision as of 10:22, 10 April 2019
Structure of RVFV Gn and human monoclonal antibody R17Structure of RVFV Gn and human monoclonal antibody R17
Structural highlights
Publication Abstract from PubMedRift Valley fever virus (RVFV) is a mosquito-borne pathogen that causes substantial morbidity and mortality in livestock and humans. To date, there are no licensed human vaccines or therapeutics available. Here, we report the isolation of monoclonal antibodies from a convalescent patient, targeting the RVFV envelope proteins Gn and Gc. The Gn-specific monoclonal antibodies exhibited much higher neutralizing activities in vitro and protection efficacies in mice against RVFV infection, compared to the Gc-specific monoclonal antibodies. The Gn monoclonal antibodies were found to interfere with soluble Gn binding to cells and prevent infection by blocking the attachment of virions to host cells. Structural analysis of Gn complexed with four Gn-specific monoclonal antibodies resulted in the definition of three antigenic patches (A, B and C) on Gn domain I. Both patches A and B are major neutralizing epitopes. Our results highlight the potential of antibody-based therapeutics and provide a structure-based rationale for designing vaccines against RVFV. Neutralization mechanism of human monoclonal antibodies against Rift Valley fever virus.,Wang Q, Ma T, Wu Y, Chen Z, Zeng H, Tong Z, Gao F, Qi J, Zhao Z, Chai Y, Yang H, Wong G, Bi Y, Wu L, Shi R, Yang M, Song J, Jiang H, An Z, Wang J, Yilma TD, Shi Y, Liu WJ, Liang M, Qin C, Gao GF, Yan J Nat Microbiol. 2019 Apr 1. pii: 10.1038/s41564-019-0411-z. doi:, 10.1038/s41564-019-0411-z. PMID:30936489[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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