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| | ==The crystal structure of hemagglutinin form A/chicken/New York/14677-13/1998== | | ==The crystal structure of hemagglutinin form A/chicken/New York/14677-13/1998== |
| - | <StructureSection load='4wsr' size='340' side='right' caption='[[4wsr]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4wsr' size='340' side='right'caption='[[4wsr]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wsr]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WSR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WSR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wsr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/chicken/New_York/14677-13/1998(H6N2)) Influenza A virus (A/chicken/New York/14677-13/1998(H6N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WSR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wss|4wss]], [[4wst|4wst]], [[4wsu|4wsu]], [[4wsv|4wsv]], [[4wsw|4wsw]], [[4wsx|4wsx]]</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=4wsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wsr OCA], [https://pdbe.org/4wsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wsr RCSB], [https://www.ebi.ac.uk/pdbsum/4wsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wsr ProSAT]</span></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=4wsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wsr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wsr RCSB], [http://www.ebi.ac.uk/pdbsum/4wsr PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q0A3A5_9INFA Q0A3A5_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 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][SAAS:SAAS00145386] | + | [https://www.uniprot.org/uniprot/Q0A3A5_9INFA Q0A3A5_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 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][SAAS:SAAS00145386] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4wsr" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carney, P J]] | + | [[Category: Large Structures]] |
| - | [[Category: Chang, J C]] | + | [[Category: Carney PJ]] |
| - | [[Category: Stevens, J]] | + | [[Category: Chang JC]] |
| - | [[Category: Villanueva, J M]] | + | [[Category: Stevens J]] |
| - | [[Category: Yang, H]] | + | [[Category: Villanueva JM]] |
| - | [[Category: H6]] | + | [[Category: Yang H]] |
| - | [[Category: Hemagglutinin]]
| + | |
| - | [[Category: Influenza virus]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
Q0A3A5_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 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][SAAS:SAAS00145386]
Publication Abstract from PubMed
During 2013, three new avian influenza A virus subtypes, A(H7N9), A(H6N1) and A(H10N8), resulted in human infections. While the A(H7N9) virus resulted in a significant epidemic in China across 19 provinces and municipalities, both A(H6N1) and A(H10N8) viruses resulted in only a few human infections. This study focuses on the major surface glycoprotein hemagglutinin from both of these novel human viruses. The detailed structural and glycan microarray analyses presented here highlight that both A(H6N1) and A(H10N8) virus hemagglutinins retain a strong avian receptor binding preference, and thus currently pose a low risk for sustained human infections. IMPORTANCE: Human infections with zoonotic influenza virus subtypes continue to be a great public health concern. We report detailed structural analysis and glycan microarray data for recombinant hemagglutinins from A(H6N1) and A(H10N8) viruses, isolated from human infections in 2013, and compare them with hemagglutinins of avian origin. This is the first structural report of an H6 HA, and our results should further the understanding of these viruses, and provide useful information to aid continuous surveillance of these zoonotic influenza viruses.
Structure and receptor binding preferences of recombinant hemagglutinins from avian and human H6 and H10 influenza A virus subtypes.,Yang H, Carney PJ, Chang JC, Villanueva JM, Stevens J J Virol. 2015 Feb 11. pii: JVI.03456-14. PMID:25673707[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang H, Carney PJ, Chang JC, Villanueva JM, Stevens J. Structure and receptor binding preferences of recombinant hemagglutinins from avian and human H6 and H10 influenza A virus subtypes. J Virol. 2015 Feb 11. pii: JVI.03456-14. PMID:25673707 doi:http://dx.doi.org/10.1128/JVI.03456-14
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