2giy

From Proteopedia

(Difference between revisions)

Revision as of 23:02, 24 December 2014

Crystal Structure of the C-terminal domain of the HSV-1 gE ectodomain

Structural highlights

2giy is a 2 chain structure with sequence from Human herpesvirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2gjy
Gene:	GE, US8 (Human herpesvirus 1)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[VGLE_HHV11] In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells (By similarity). In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips.^[1] ^[2] The heterodimer gE/gI serves as a receptor for the Fc part of host IgG. Dissociation of gE/gI from IgG occurs at acidic pH. May thus be involved in anti-HSV antibodies bipolar bridging, followed by intracellular endocytosis and degradation, thereby interfering with host IgG-mediated immune responses.^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Herpes simplex virus type-1 expresses a heterodimeric Fc receptor, gE-gI, on the surfaces of virions and infected cells that binds the Fc region of host immunoglobulin G and is implicated in the cell-to-cell spread of virus. gE-gI binds immunoglobulin G at the basic pH of the cell surface and releases it at the acidic pH of lysosomes, consistent with a role in facilitating the degradation of antiviral antibodies. Here we identify the C-terminal domain of the gE ectodomain (CgE) as the minimal Fc-binding domain and present a 1.78-angstroms CgE structure. A 5-angstroms gE-gI/Fc crystal structure, which was independently verified by a theoretical prediction method, reveals that CgE binds Fc at the C(H)2-C(H)3 interface, the binding site for several mammalian and bacterial Fc-binding proteins. The structure identifies interface histidines that may confer pH-dependent binding and regions of CgE implicated in cell-to-cell spread of virus. The ternary organization of the gE-gI/Fc complex is compatible with antibody bipolar bridging, which can interfere with the antiviral immune response.

Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.,Sprague ER, Wang C, Baker D, Bjorkman PJ PLoS Biol. 2006 Jun;4(6):e148. Epub 2006 May 2. PMID:16646632^[5]

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

References

↑ Johnson DC, Frame MC, Ligas MW, Cross AM, Stow ND. Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI. J Virol. 1988 Apr;62(4):1347-54. PMID:2831396
↑ Sprague ER, Martin WL, Bjorkman PJ. pH dependence and stoichiometry of binding to the Fc region of IgG by the herpes simplex virus Fc receptor gE-gI. J Biol Chem. 2004 Apr 2;279(14):14184-93. Epub 2004 Jan 20. PMID:14734541 doi:10.1074/jbc.M313281200
↑ Johnson DC, Frame MC, Ligas MW, Cross AM, Stow ND. Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI. J Virol. 1988 Apr;62(4):1347-54. PMID:2831396
↑ Sprague ER, Martin WL, Bjorkman PJ. pH dependence and stoichiometry of binding to the Fc region of IgG by the herpes simplex virus Fc receptor gE-gI. J Biol Chem. 2004 Apr 2;279(14):14184-93. Epub 2004 Jan 20. PMID:14734541 doi:10.1074/jbc.M313281200
↑ Sprague ER, Wang C, Baker D, Bjorkman PJ. Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging. PLoS Biol. 2006 Jun;4(6):e148. Epub 2006 May 2. PMID:16646632 doi:10.1371/journal.pbio.0040148

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2giy"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2giy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GIY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GIY FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gjy|2gjy]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gjy|2gjy]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GE, US8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10298 Human herpesvirus 1])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GE, US8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10298 Human herpesvirus 1])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2giy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2giy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2giy RCSB], [http://www.ebi.ac.uk/pdbsum/2giy PDBsum]</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=2giy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2giy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2giy RCSB], [http://www.ebi.ac.uk/pdbsum/2giy PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/VGLE_HHV11 VGLE_HHV11]] In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells (By similarity). In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips.<ref>PMID:2831396</ref> <ref>PMID:14734541</ref>   The heterodimer gE/gI serves as a receptor for the Fc part of host IgG. Dissociation of gE/gI from IgG occurs at acidic pH. May thus be involved in anti-HSV antibodies bipolar bridging, followed by intracellular endocytosis and degradation, thereby interfering with host IgG-mediated immune responses.<ref>PMID:2831396</ref> <ref>PMID:14734541</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 </StructureSection>
 [[Category: Human herpesvirus 1]]
-[[Category: Baker, D.]]
+[[Category: Baker, D]]
-[[Category: Bjorkman, P J.]]
+[[Category: Bjorkman, P J]]
-[[Category: Sprague, E R.]]
+[[Category: Sprague, E R]]
-[[Category: Wang, C.]]
+[[Category: Wang, C]]
 [[Category: Ig v domain]]
 [[Category: Viral fc receptor]]
 [[Category: Viral protein]]

2giy

From Proteopedia

Revision as of 23:02, 24 December 2014

Crystal Structure of the C-terminal domain of the HSV-1 gE ectodomain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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