6v4o: Difference between revisions
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==== | ==Structure of human 2E01 Fab in complex with influenza virus neuraminidase from B/Phuket/3073/2013== | ||
<StructureSection load='6v4o' size='340' side='right'caption='[[6v4o]]' scene=''> | <StructureSection load='6v4o' size='340' side='right'caption='[[6v4o]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6v4o]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_B_virus Influenza B virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V4O FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6v4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v4o OCA], [https://pdbe.org/6v4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v4o RCSB], [https://www.ebi.ac.uk/pdbsum/6v4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v4o ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1S5RAG6_9INFB A0A1S5RAG6_9INFB] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.[RuleBase:RU361252] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Influenza B virus (IBV) infections can cause severe disease in children and the elderly. Commonly used antivirals have lower clinical effectiveness against IBV compared to influenza A viruses (IAV). Neuraminidase (NA), the second major surface protein on the influenza virus, is emerging as a target of broadly protective antibodies that recognize the NA active site of IAVs. However, similarly broadly protective antibodies against IBV NA have not been identified. Here, we isolated and characterized human monoclonal antibodies (mAbs) that target IBV NA from an IBV-infected patient. Two mAbs displayed broad and potent capacity to inhibit IBV NA enzymatic activity, neutralize the virus in vitro, and protect against lethal IBV infection in mice in prophylactic and therapeutic settings. These mAbs inserted long CDR-H3 loops into the NA active site, engaging residues highly conserved among IBV NAs. These mAbs provide a blueprint for the development of improved vaccines and therapeutics against IBVs. | |||
Human Antibodies Targeting Influenza B Virus Neuraminidase Active Site Are Broadly Protective.,Madsen A, Dai YN, McMahon M, Schmitz AJ, Turner JS, Tan J, Lei T, Alsoussi WB, Strohmeier S, Amor M, Mohammed BM, Mudd PA, Simon V, Cox RJ, Fremont DH, Krammer F, Ellebedy AH Immunity. 2020 Sep 22. pii: S1074-7613(20)30372-1. doi:, 10.1016/j.immuni.2020.08.015. PMID:32976769<ref>PMID:32976769</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6v4o" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[Neuraminidase 3D structures|Neuraminidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Influenza B virus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Dai YN]] | ||
[[Category: Fremont DH]] | |||
Latest revision as of 13:34, 23 October 2024
Structure of human 2E01 Fab in complex with influenza virus neuraminidase from B/Phuket/3073/2013Structure of human 2E01 Fab in complex with influenza virus neuraminidase from B/Phuket/3073/2013
Structural highlights
FunctionA0A1S5RAG6_9INFB Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.[RuleBase:RU361252] Publication Abstract from PubMedInfluenza B virus (IBV) infections can cause severe disease in children and the elderly. Commonly used antivirals have lower clinical effectiveness against IBV compared to influenza A viruses (IAV). Neuraminidase (NA), the second major surface protein on the influenza virus, is emerging as a target of broadly protective antibodies that recognize the NA active site of IAVs. However, similarly broadly protective antibodies against IBV NA have not been identified. Here, we isolated and characterized human monoclonal antibodies (mAbs) that target IBV NA from an IBV-infected patient. Two mAbs displayed broad and potent capacity to inhibit IBV NA enzymatic activity, neutralize the virus in vitro, and protect against lethal IBV infection in mice in prophylactic and therapeutic settings. These mAbs inserted long CDR-H3 loops into the NA active site, engaging residues highly conserved among IBV NAs. These mAbs provide a blueprint for the development of improved vaccines and therapeutics against IBVs. Human Antibodies Targeting Influenza B Virus Neuraminidase Active Site Are Broadly Protective.,Madsen A, Dai YN, McMahon M, Schmitz AJ, Turner JS, Tan J, Lei T, Alsoussi WB, Strohmeier S, Amor M, Mohammed BM, Mudd PA, Simon V, Cox RJ, Fremont DH, Krammer F, Ellebedy AH Immunity. 2020 Sep 22. pii: S1074-7613(20)30372-1. doi:, 10.1016/j.immuni.2020.08.015. PMID:32976769[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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