6e7h: Difference between revisions

Latest revision as of 07:54, 17 October 2024

Crystal structure of H5 hemagglutinin mutant Y161A from A/Viet Nam/1203/2004 H5N1 influenza virus in complex with 3'-GcLN

Structural highlights

6e7h is a 6 chain structure with sequence from Influenza A virus (A/Viet Nam/1203/2004(H5N1)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.3Å
Ligands:	BMA, GAL, NAG, NGC
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

A species barrier for the influenza A virus is the differential expression of sialic acid, which can either be alpha2,3-linked for avians or alpha2,6-linked for human viruses. The influenza A virus hosts also express other species-specific sialic acid derivatives. One major modification at C-5 is N-glycolyl (NeuGc), instead of N-acetyl (NeuAc). N-glycolyl is mammalian specific and expressed in pigs and horses, but not in humans, ferrets, seals, or dogs. Hemagglutinin (HA) adaptation to either N-acetyl or N-glycolyl is analyzed on a sialoside microarray containing both alpha2,3- and alpha2,6-linkage modifications on biologically relevant N-glycans. Binding studies reveal that avian, human, and equine HAs bind either N-glycolyl or N-acetyl. Structural data on N-glycolyl binding HA proteins of both H5 and H7 origin describe this specificity. Neuraminidases can cleave N-glycolyl efficiently, and tissue-binding studies reveal strict species specificity. The exclusive manner in which influenza A viruses differentiate between N-glycolyl and N-acetyl is indicative of selection.

N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses.,Broszeit F, Tzarum N, Zhu X, Nemanichvili N, Eggink D, Leenders T, Li Z, Liu L, Wolfert MA, Papanikolaou A, Martinez-Romero C, Gagarinov IA, Yu W, Garcia-Sastre A, Wennekes T, Okamatsu M, Verheije MH, Wilson IA, Boons GJ, de Vries RP Cell Rep. 2019 Jun 11;27(11):3284-3294.e6. doi: 10.1016/j.celrep.2019.05.048. PMID:31189111^[1]

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

References

↑ Broszeit F, Tzarum N, Zhu X, Nemanichvili N, Eggink D, Leenders T, Li Z, Liu L, Wolfert MA, Papanikolaou A, Martinez-Romero C, Gagarinov IA, Yu W, Garcia-Sastre A, Wennekes T, Okamatsu M, Verheije MH, Wilson IA, Boons GJ, de Vries RP. N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses. Cell Rep. 2019 Jun 11;27(11):3284-3294.e6. doi: 10.1016/j.celrep.2019.05.048. PMID:31189111 doi:https://dx.doi.org/10.1016/j.celrep.2019.05.048

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OCA

[1] Broszeit F, Tzarum N, Zhu X, Nemanichvili N, Eggink D, Leenders T, Li Z, Liu L, Wolfert MA, Papanikolaou A, Martinez-Romero C, Gagarinov IA, Yu W, Garcia-Sastre A, Wennekes T, Okamatsu M, Verheije MH, Wilson IA, Boons GJ, de Vries RP. N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses. Cell Rep. 2019 Jun 11;27(11):3284-3294.e6. doi: 10.1016/j.celrep.2019.05.048. PMID:31189111 doi:https://dx.doi.org/10.1016/j.celrep.2019.05.048

[1]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6e7h is ON HOLD
+==Crystal structure of H5 hemagglutinin mutant Y161A from A/Viet Nam/1203/2004 H5N1 influenza virus in complex with 3'-GcLN==
+<StructureSection load='6e7h' size='340' side='right'caption='[[6e7h]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6e7h]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Viet_Nam/1203/2004(H5N1)) Influenza A virus (A/Viet Nam/1203/2004(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E7H FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NGC:3,5-DIDEOXY-5-[(HYDROXYACETYL)AMINO]-D-GLYCERO-ALPHA-D-GALACTO-NON-2-ULOPYRANOSONIC+ACID'>NGC</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=6e7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e7h OCA], [https://pdbe.org/6e7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e7h RCSB], [https://www.ebi.ac.uk/pdbsum/6e7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e7h ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A species barrier for the influenza A virus is the differential expression of sialic acid, which can either be alpha2,3-linked for avians or alpha2,6-linked for human viruses. The influenza A virus hosts also express other species-specific sialic acid derivatives. One major modification at C-5 is N-glycolyl (NeuGc), instead of N-acetyl (NeuAc). N-glycolyl is mammalian specific and expressed in pigs and horses, but not in humans, ferrets, seals, or dogs. Hemagglutinin (HA) adaptation to either N-acetyl or N-glycolyl is analyzed on a sialoside microarray containing both alpha2,3- and alpha2,6-linkage modifications on biologically relevant N-glycans. Binding studies reveal that avian, human, and equine HAs bind either N-glycolyl or N-acetyl. Structural data on N-glycolyl binding HA proteins of both H5 and H7 origin describe this specificity. Neuraminidases can cleave N-glycolyl efficiently, and tissue-binding studies reveal strict species specificity. The exclusive manner in which influenza A viruses differentiate between N-glycolyl and N-acetyl is indicative of selection.
-Authors:
+N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses.,Broszeit F, Tzarum N, Zhu X, Nemanichvili N, Eggink D, Leenders T, Li Z, Liu L, Wolfert MA, Papanikolaou A, Martinez-Romero C, Gagarinov IA, Yu W, Garcia-Sastre A, Wennekes T, Okamatsu M, Verheije MH, Wilson IA, Boons GJ, de Vries RP Cell Rep. 2019 Jun 11;27(11):3284-3294.e6. doi: 10.1016/j.celrep.2019.05.048. PMID:31189111<ref>PMID:31189111</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6e7h" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Tzarum N]]
+[[Category: Wilson IA]]

6e7h: Difference between revisions

Latest revision as of 07:54, 17 October 2024

Crystal structure of H5 hemagglutinin mutant Y161A from A/Viet Nam/1203/2004 H5N1 influenza virus in complex with 3'-GcLN

Structural highlights

Publication Abstract from PubMed

See Also

References

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