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| | ==Influenza A virus H5 hemagglutinin globular head== | | ==Influenza A virus H5 hemagglutinin globular head== |
| - | <StructureSection load='5dut' size='340' side='right' caption='[[5dut]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='5dut' size='340' side='right'caption='[[5dut]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dut]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DUT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dut]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Anhui/1/2005(H5N1)) Influenza A virus (A/Anhui/1/2005(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DUT 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]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dum|5dum]], [[5dup|5dup]], [[5dur|5dur]]</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='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=5dut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dut OCA], [http://pdbe.org/5dut PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dut RCSB], [http://www.ebi.ac.uk/pdbsum/5dut PDBsum]</span></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=5dut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dut OCA], [https://pdbe.org/5dut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dut RCSB], [https://www.ebi.ac.uk/pdbsum/5dut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dut ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q1WDM0_9INFA Q1WDM0_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS013829_004_327643] | + | [https://www.uniprot.org/uniprot/Q1WDM0_9INFA Q1WDM0_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS013829_004_327643] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5dut" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5dut" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Sun, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Wang, G]] | + | [[Category: Sun J]] |
| - | [[Category: Wang, X]] | + | [[Category: Wang G]] |
| - | [[Category: Zhang, L]] | + | [[Category: Wang X]] |
| - | [[Category: Zhou, P]] | + | [[Category: Zhang L]] |
| - | [[Category: Zuo, T]] | + | [[Category: Zhou P]] |
| - | [[Category: Globular head]]
| + | [[Category: Zuo T]] |
| - | [[Category: H5]]
| + | |
| - | [[Category: Hemagglutinin]]
| + | |
| - | [[Category: Influenza virus]]
| + | |
| - | [[Category: Viral protein]]
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| Structural highlights
Function
Q1WDM0_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS013829_004_327643]
Publication Abstract from PubMed
Understanding the mechanism of protective antibody recognition against highly pathogenic avian influenza A virus H5N1 in humans is critical for the development of effective therapies and vaccines. Here we report the crystal structure of three H5-specific human monoclonal antibodies bound to the globular head of hemagglutinin (HA) with distinct epitope specificities, neutralization potencies and breadth. A structural and functional analysis of these epitopes combined with those reported elsewhere identifies four major vulnerable sites on the globular head of H5N1 HA. Chimeric and vulnerable site-specific mutant pseudoviruses are generated to delineate broad neutralization specificities of convalescent sera from two individuals who recovered from the infection with H5N1 virus. Our results show that the four vulnerable sites on the globular head rather than the stem region are the major neutralizing targets, suggesting that during natural H5N1 infection neutralizing antibodies against the globular head work in concert to provide protective antibody-mediated immunity.
Comprehensive analysis of antibody recognition in convalescent humans from highly pathogenic avian influenza H5N1 infection.,Zuo T, Sun J, Wang G, Jiang L, Zuo Y, Li D, Shi X, Liu X, Fan S, Ren H, Hu H, Sun L, Zhou B, Liang M, Zhou P, Wang X, Zhang L Nat Commun. 2015 Dec 4;6:8855. doi: 10.1038/ncomms9855. PMID:26635249[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zuo T, Sun J, Wang G, Jiang L, Zuo Y, Li D, Shi X, Liu X, Fan S, Ren H, Hu H, Sun L, Zhou B, Liang M, Zhou P, Wang X, Zhang L. Comprehensive analysis of antibody recognition in convalescent humans from highly pathogenic avian influenza H5N1 infection. Nat Commun. 2015 Dec 4;6:8855. doi: 10.1038/ncomms9855. PMID:26635249 doi:http://dx.doi.org/10.1038/ncomms9855
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