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4w8n

From Proteopedia

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Current revision

The crystal structure of hemagglutinin from a swine influenza virus (A/swine/Missouri/2124514/2006)

Structural highlights

4w8n is a 6 chain structure with sequence from Influenza A virus (A/swine/Missouri/2124514/2006(H2N3)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A9YN66_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

After their disappearance from the human population in 1968, influenza H2 viruses have continued to circulate in the natural avian reservoir. The isolation of this virus subtype from multiple bird species as well as swine highlights the need to better understand the potential of these viruses to spread and cause disease in humans. Here we analyzed the virulence, transmissibility and receptor-binding preference of two avian influenza H2 viruses (H2N2 and H2N3) and compared them to a swine H2N3 (A/swine/Missouri/2124514/2006 [swMO]), and a human H2N2 (A/England/10/1967 [Eng/67]) virus using the ferret model as a mammalian host. Both avian H2 viruses possessed the capacity to spread efficiently between cohoused ferrets, and the swine (swMO) and human (Eng/67) viruses transmitted to naive ferrets by respiratory droplets. Further characterization of the swMO hemagglutinin (HA) by x-ray crystallography and glycan microarray array identified receptor-specific adaptive mutations. As influenza virus quasispecies dynamics during transmission have not been well characterized, we sequenced nasal washes collected during transmission studies to better understand experimental adaptation of H2 HA. The avian H2 viruses isolated from ferret nasal washes contained mutations in the HA1, including a Gln226Leu substitution, which is a mutation associated with alpha2,6 sialic acid (human-like) binding preference. These results suggest that the molecular structure of HA in viruses of the H2 subtype continue to have the potential to adapt to a mammalian host and become transmissible, after acquiring additional genetic markers.

Assessment of transmission, pathogenesis and adaptation of H2 subtype influenza viruses in ferrets.,Pappas C, Yang H, Carney PJ, Pearce MB, Katz JM, Stevens J, Tumpey TM Virology. 2015 Feb 4;477C:61-71. doi: 10.1016/j.virol.2015.01.002. PMID:25659818^[1]

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

References

↑ Pappas C, Yang H, Carney PJ, Pearce MB, Katz JM, Stevens J, Tumpey TM. Assessment of transmission, pathogenesis and adaptation of H2 subtype influenza viruses in ferrets. Virology. 2015 Feb 4;477C:61-71. doi: 10.1016/j.virol.2015.01.002. PMID:25659818 doi:http://dx.doi.org/10.1016/j.virol.2015.01.002

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/4w8n"

Categories: Large Structures | Carney PJ | Stevens J | Tumpey TM | Yang H

@@ Line 1: / Line 1: @@
 ==The crystal structure of hemagglutinin from a swine influenza virus (A/swine/Missouri/2124514/2006)==
-<StructureSection load='4w8n' size='340' side='right' caption='[[4w8n]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='4w8n' size='340' side='right'caption='[[4w8n]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4w8n]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W8N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4w8n]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/swine/Missouri/2124514/2006(H2N3)) Influenza A virus (A/swine/Missouri/2124514/2006(H2N3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W8N 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>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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]] 2.9&#8491;</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=4w8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w8n RCSB], [http://www.ebi.ac.uk/pdbsum/4w8n PDBsum]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=4w8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8n OCA], [https://pdbe.org/4w8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w8n RCSB], [https://www.ebi.ac.uk/pdbsum/4w8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w8n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A9YN66_9INFA A9YN66_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/A9YN66_9INFA A9YN66_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;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4w8n" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Carney, P J]]
+[[Category: Large Structures]]
-[[Category: Stevens, J]]
+[[Category: Carney PJ]]
-[[Category: Tumpey, T M]]
+[[Category: Stevens J]]
-[[Category: Yang, H]]
+[[Category: Tumpey TM]]
-[[Category: Hemagglutinin]]
+[[Category: Yang H]]
-[[Category: Influenza virus]]
-[[Category: Viral protein]]

4w8n

From Proteopedia

Current revision

The crystal structure of hemagglutinin from a swine influenza virus (A/swine/Missouri/2124514/2006)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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