|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5wna' size='340' side='right'caption='[[5wna]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='5wna' size='340' side='right'caption='[[5wna]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wna]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrsva Hrsva] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WNA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WNA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wna]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_respiratory_syncytial_virus_A2 Human respiratory syncytial virus A2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WNA 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=5wna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wna OCA], [http://pdbe.org/5wna PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wna RCSB], [http://www.ebi.ac.uk/pdbsum/5wna PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wna 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]] 2.4Å</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=5wna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wna OCA], [https://pdbe.org/5wna PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wna RCSB], [https://www.ebi.ac.uk/pdbsum/5wna PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wna ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLYC_HRSVA GLYC_HRSVA]] Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors. | + | [https://www.uniprot.org/uniprot/GLYC_HRSVA GLYC_HRSVA] Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 17: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5wna" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5wna" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hrsva]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Human respiratory syncytial virus A2]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: DuBois, R M]] | + | [[Category: DuBois RM]] |
| - | [[Category: Fedechkin, S O]] | + | [[Category: Fedechkin SO]] |
| - | [[Category: George, N L]] | + | [[Category: George NL]] |
| - | [[Category: Kauvar, L M]] | + | [[Category: Kauvar LM]] |
| - | [[Category: Wolff, J T]] | + | [[Category: Wolff JT]] |
| - | [[Category: Antibody]]
| + | |
| - | [[Category: G glycoprotein]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Rsv]]
| + | |
| - | [[Category: Viral attachment protein]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Viral protein-immune system complex]]
| + | |
| Structural highlights
Function
GLYC_HRSVA Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors.
Publication Abstract from PubMed
Respiratory syncytial virus (RSV) is a top cause of severe lower respiratory tract disease and mortality in young children and the elderly. The viral envelope G glycoprotein contributes to pathogenesis through its roles in host cell attachment and modulation of host immunity. Although the G glycoprotein is a target of protective RSV-neutralizing antibodies, its development as a vaccine antigen has been hindered by its heterogeneous glycosylation and sequence variability outside a conserved central domain (CCD). We describe the cocrystal structures of two high-affinity broadly neutralizing human monoclonal antibodies bound to the RSV G CCD. The antibodies bind to neighboring conformational epitopes, which we named antigenic sites gamma1 and gamma2, that span a highly conserved surface, illuminating an important region of vulnerability. We further show that isolated RSV G CCD activates the chemokine receptor CX3CR1 and that antibodies block this activity. These studies provide a template for rational vaccine design targeting this key contributor to RSV disease.
Structures of respiratory syncytial virus G antigen bound to broadly neutralizing antibodies.,Fedechkin SO, George NL, Wolff JT, Kauvar LM, DuBois RM Sci Immunol. 2018 Mar 9;3(21). pii: 3/21/eaar3534. doi:, 10.1126/sciimmunol.aar3534. Epub 2018 Mar 9. PMID:29523582[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fedechkin SO, George NL, Wolff JT, Kauvar LM, DuBois RM. Structures of respiratory syncytial virus G antigen bound to broadly neutralizing antibodies. Sci Immunol. 2018 Mar 9;3(21). pii: 3/21/eaar3534. doi:, 10.1126/sciimmunol.aar3534. Epub 2018 Mar 9. PMID:29523582 doi:http://dx.doi.org/10.1126/sciimmunol.aar3534
|
