5zhg - Revision history

OCA at 10:27, 27 March 2024

OCA — Wed, 27 Mar 2024 10:27:52 GMT

←Older revision		Revision as of 10:27, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='5zhg' size='340' side='right'caption='[[5zhg]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='5zhg' size='340' side='right'caption='[[5zhg]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zhg]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human_rotavirus_(group_c_~~/~~_strain_bristol)~~ Human rotavirus ~~(group c~~ / ~~strain bristol)~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZHG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5ZHG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zhg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_rotavirus_C/Bristol Human rotavirus C/Bristol]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZHG FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5zhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zhg OCA], [~~http~~://pdbe.org/5zhg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5zhg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5zhg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5zhg ProSAT]</span></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]] 1.799Å</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=5zhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zhg OCA], [https://pdbe.org/5zhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zhg RCSB], [https://www.ebi.ac.uk/pdbsum/5zhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zhg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/VP4_ROTHC VP4_ROTHC]] Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (By similarity). Outer capsid protein VP5: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm (By similarity). VP8 forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies (By similarity).	+	[https://www.uniprot.org/uniprot/VP4_ROTHC VP4_ROTHC] Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (By similarity). Outer capsid protein VP5: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm (By similarity). VP8 forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies (By similarity).
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Group/species C rotaviruses (RVCs) have been identified as important pathogens of acute gastroenteritis (AGE) in children, family-based outbreaks, as well as animal infections. However, little is known regarding their host-specific interaction, infection, and pathogenesis. In this study, we performed serial studies to characterize the function and structural features of a human G4P[lsqb]2[rsqb] RVC VP8* that is responsible for host receptor interaction. Glycan microarrays demonstrated that the human RVC VP8* recognizes type A histo-blood antigens (HBGAs), which was confirmed by synthetic glycan-/saliva-based binding assays, and hemagglutination of red blood cells, establishing a paradigm of RVC VP8-glycan interactions. Furthermore, high resolution crystal structure of the human RVC VP8 was solved, showing a typical galectin-like structure consisting of two beta-sheets but with significant differences to cogent proteins of RVAs. The VP8* in complex with a type A trisaccharide displays a novel ligand binding site that consists of a particular set of amino acid (aa) residues of the C-D, G-H, and K-L loops. RVC VP8* interacts with type A HBGAs through a unique mechanism compared with RVAs. Our findings shed light on the host-virus interaction and co-evolution of RVCs and will facilitate the development of specific antivirals and vaccines.IMPORTANCE Group/species C rotaviruses (RVCs), members of Reoviridae family, infect both humans and animals, but our knowledge about the host factors that control host susceptibility and specificity is rudimentary. In this work, we characterized the glycan binding specificity and structural basis of a human RVC that recognizes type A HBGAs. We found that human RVC VP8*, the RV host ligand binding domain that shares only approximately 15% homology to those of RVAs, recognizes type A HBGA at an as-yet-unknown glycan binding site through a distinct mechanism compared with RVAs. Our new advancements provide insights into RVC-cell attachment, the critical step of virus infection, which will in turn help the development of control and prevention strategies against RVs.	+
-		+
-	Human group C rotavirus VP8*s recognize type A histo-blood group antigens as ligands.,Sun X, Wang L, Qi J, Li D, Wang M, Cong X, Peng R, Chai W, Zhang Q, Wang H, Wen H, Gao GF, Tan M, Duan Z J Virol. 2018 Mar 28. pii: JVI.00442-18. doi: 10.1128/JVI.00442-18. PMID:29593033<ref>PMID:29593033</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5zhg" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human rotavirus C/Bristol]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Duan, Z]]	+	[[Category: Duan Z]]
-	[[Category: Sun, X]]	+	[[Category: Sun X]]
-	~~[[Category: Galactin-like]]~~	+
-	~~[[Category: Group c rotavirus]]~~	+
-	~~[[Category: Histo-blood group antigen]]~~	+
-	~~[[Category: Viral protein]]~~	+
-	[[Category: Vp8*]]	+

OCA at 21:19, 28 October 2020

OCA — Wed, 28 Oct 2020 21:19:35 GMT

←Older revision		Revision as of 21:19, 28 October 2020
Line 1:		Line 1:

	==Human group C rotavirus VP8*s recognize type A histo-blood group antigens as ligands==		==Human group C rotavirus VP8*s recognize type A histo-blood group antigens as ligands==
-	<StructureSection load='5zhg' size='340' side='right' caption='[[5zhg]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='5zhg' size='340' side='right'caption='[[5zhg]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zhg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rotavirus_(group_c_/_strain_bristol) Human rotavirus (group c / strain bristol)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZHG OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ZHG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zhg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rotavirus_(group_c_/_strain_bristol) Human rotavirus (group c / strain bristol)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZHG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZHG FirstGlance]. <br>
-	</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=5zhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zhg OCA], [http://pdbe.org/5zhg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zhg RCSB], [http://www.ebi.ac.uk/pdbsum/5zhg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zhg ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zhg OCA], [http://pdbe.org/5zhg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zhg RCSB], [http://www.ebi.ac.uk/pdbsum/5zhg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zhg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Duan, Z]]		[[Category: Duan, Z]]
	[[Category: Sun, X]]		[[Category: Sun, X]]

OCA at 06:17, 6 June 2018

OCA — Wed, 06 Jun 2018 06:17:15 GMT

←Older revision		Revision as of 06:17, 6 June 2018
Line 3:		Line 3:
	<StructureSection load='5zhg' size='340' side='right' caption='[[5zhg]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='5zhg' size='340' side='right' caption='[[5zhg]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zhg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZHG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zhg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rotavirus_(group_c_/_strain_bristol) Human rotavirus (group c / strain bristol)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZHG FirstGlance]. <br>
	</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=5zhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zhg OCA], [http://pdbe.org/5zhg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zhg RCSB], [http://www.ebi.ac.uk/pdbsum/5zhg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zhg ProSAT]</span></td></tr>		</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=5zhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zhg OCA], [http://pdbe.org/5zhg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zhg RCSB], [http://www.ebi.ac.uk/pdbsum/5zhg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zhg ProSAT]</span></td></tr>
	</table>		</table>

OCA at 13:50, 11 April 2018

OCA — Wed, 11 Apr 2018 13:50:09 GMT

←Older revision		Revision as of 13:50, 11 April 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5zhg is ~~ON HOLD~~ ~~until Mar 13 2020~~	+	==Human group C rotavirus VP8*s recognize type A histo-blood group antigens as ligands==
		+	<StructureSection load='5zhg' size='340' side='right' caption='[[5zhg]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5zhg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZHG FirstGlance]. <br>
		+	</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=5zhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zhg OCA], [http://pdbe.org/5zhg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zhg RCSB], [http://www.ebi.ac.uk/pdbsum/5zhg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zhg ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VP4_ROTHC VP4_ROTHC]] Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (By similarity). Outer capsid protein VP5: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm (By similarity). VP8 forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Group/species C rotaviruses (RVCs) have been identified as important pathogens of acute gastroenteritis (AGE) in children, family-based outbreaks, as well as animal infections. However, little is known regarding their host-specific interaction, infection, and pathogenesis. In this study, we performed serial studies to characterize the function and structural features of a human G4P[lsqb]2[rsqb] RVC VP8* that is responsible for host receptor interaction. Glycan microarrays demonstrated that the human RVC VP8* recognizes type A histo-blood antigens (HBGAs), which was confirmed by synthetic glycan-/saliva-based binding assays, and hemagglutination of red blood cells, establishing a paradigm of RVC VP8-glycan interactions. Furthermore, high resolution crystal structure of the human RVC VP8 was solved, showing a typical galectin-like structure consisting of two beta-sheets but with significant differences to cogent proteins of RVAs. The VP8* in complex with a type A trisaccharide displays a novel ligand binding site that consists of a particular set of amino acid (aa) residues of the C-D, G-H, and K-L loops. RVC VP8* interacts with type A HBGAs through a unique mechanism compared with RVAs. Our findings shed light on the host-virus interaction and co-evolution of RVCs and will facilitate the development of specific antivirals and vaccines.IMPORTANCE Group/species C rotaviruses (RVCs), members of Reoviridae family, infect both humans and animals, but our knowledge about the host factors that control host susceptibility and specificity is rudimentary. In this work, we characterized the glycan binding specificity and structural basis of a human RVC that recognizes type A HBGAs. We found that human RVC VP8*, the RV host ligand binding domain that shares only approximately 15% homology to those of RVAs, recognizes type A HBGA at an as-yet-unknown glycan binding site through a distinct mechanism compared with RVAs. Our new advancements provide insights into RVC-cell attachment, the critical step of virus infection, which will in turn help the development of control and prevention strategies against RVs.

-	~~Authors: Xiaoman, S~~., ~~Zhaojun~~, D.	+	Human group C rotavirus VP8*s recognize type A histo-blood group antigens as ligands.,Sun X, Wang L, Qi J, Li D, Wang M, Cong X, Peng R, Chai W, Zhang Q, Wang H, Wen H, Gao GF, Tan M, Duan Z J Virol. 2018 Mar 28. pii: JVI.00442-18. doi: 10.1128/JVI.00442-18. PMID:29593033<ref>PMID:29593033</ref>

-	~~Description: Human group C rotavirus VP8*s recognize type A histo~~-~~blood group antigens as ligands~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: ~~Zhaojun~~, D]]	+	<div class="pdbe-citations 5zhg" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Xiaoman, S~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Duan, Z]]
		+	[[Category: Sun, X]]
		+	[[Category: Galactin-like]]
		+	[[Category: Group c rotavirus]]
		+	[[Category: Histo-blood group antigen]]
		+	[[Category: Viral protein]]
		+	[[Category: Vp8*]]

OCA at 05:08, 28 March 2018

OCA — Wed, 28 Mar 2018 05:08:52 GMT

←Older revision		Revision as of 05:08, 28 March 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5zhg is ON HOLD	+	The entry 5zhg is ON HOLD until Mar 13 2020

	Authors: Xiaoman, S., Zhaojun, D.		Authors: Xiaoman, S., Zhaojun, D.

OCA: Protected "5zhg" [edit=sysop:move=sysop]

OCA — Wed, 21 Mar 2018 06:00:16 GMT

Protected "5zhg" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:00, 21 March 2018

OCA: New page: '''Unreleased structure''' The entry 5zhg is ON HOLD Authors: Xiaoman, S., Zhaojun, D. Description: Human group C rotavirus VP8*s recognize type A histo-blood group antigens as ligands...

OCA — Wed, 21 Mar 2018 06:00:15 GMT

New page: '''Unreleased structure''' The entry 5zhg is ON HOLD Authors: Xiaoman, S., Zhaojun, D. Description: Human group C rotavirus VP8*s recognize type A histo-blood group antigens as ligands...

New page

'''Unreleased structure'''

The entry 5zhg is ON HOLD

Authors: Xiaoman, S., Zhaojun, D.

Description: Human group C rotavirus VP8*s recognize type A histo-blood group antigens as ligands
[[Category: Unreleased Structures]]
[[Category: Zhaojun, D]]
[[Category: Xiaoman, S]]