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5xrt

From Proteopedia

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Current revision

Crystal structure of A/Minnesota/11/2010 (H3N2) influenza virus hemagglutinin

Structural highlights

5xrt is a 8 chain structure with sequence from Influenza A virus (A/swine/Indiana/A01260280/2013(H3N2)) and Influenza A virus (A/swine/Minnesota/A01134337/2010(H3N2)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.15Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

I0AXC3_9INFA Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[HAMAP-Rule:MF_04072][SAAS:SAAS01039073] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]

Publication Abstract from PubMed

The high rate of antigenic drift in seasonal influenza viruses necessitates frequent changes in vaccine composition. Recent seasonal H3 vaccines do not protect against swine-origin H3N2 variant (H3N2v) strains that recently have caused severe human infections. Here, we report a human VH1-69 gene-encoded monoclonal antibody (mAb) designated H3v-47 that exhibits potent cross-reactive neutralization activity against human and swine H3N2 viruses that circulated since 1989. The crystal structure and electron microscopy reconstruction of H3v-47 Fab with the H3N2v hemagglutinin (HA) identify a unique epitope spanning the vestigial esterase and receptor-binding subdomains that is distinct from that of any known neutralizing antibody for influenza A H3 viruses. MAb H3v-47 functions largely by blocking viral egress from infected cells. Interestingly, H3v-47 also engages Fcgamma receptor and mediates antibody dependent cellular cytotoxicity (ADCC). This newly identified conserved epitope can be used in design of novel immunogens for development of broadly protective H3 vaccines.

A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA.,Bangaru S, Zhang H, Gilchuk IM, Voss TG, Irving RP, Gilchuk P, Matta P, Zhu X, Lang S, Nieusma T, Richt JA, Albrecht RA, Vanderven HA, Bombardi R, Kent SJ, Ward AB, Wilson IA, Crowe JE Jr Nat Commun. 2018 Jul 10;9(1):2669. doi: 10.1038/s41467-018-04704-9. PMID:29991715^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bangaru S, Zhang H, Gilchuk IM, Voss TG, Irving RP, Gilchuk P, Matta P, Zhu X, Lang S, Nieusma T, Richt JA, Albrecht RA, Vanderven HA, Bombardi R, Kent SJ, Ward AB, Wilson IA, Crowe JE Jr. A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA. Nat Commun. 2018 Jul 10;9(1):2669. doi: 10.1038/s41467-018-04704-9. PMID:29991715 doi:http://dx.doi.org/10.1038/s41467-018-04704-9

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5xrt"

Categories: Large Structures | Wilson IA | Zhang H

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5xrt]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/swine/Indiana/A01260280/2013(H3N2)) Influenza A virus (A/swine/Indiana/A01260280/2013(H3N2))] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/swine/Minnesota/A01134337/2010(H3N2)) Influenza A virus (A/swine/Minnesota/A01134337/2010(H3N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XRT FirstGlance]. <br>
-</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=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15&#8491;</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=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=5xrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrt OCA], [https://pdbe.org/5xrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xrt RCSB], [https://www.ebi.ac.uk/pdbsum/5xrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrt ProSAT]</span></td></tr>
 </table>

5xrt

From Proteopedia

Current revision

Crystal structure of A/Minnesota/11/2010 (H3N2) influenza virus hemagglutinin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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