5wnb | pdb_00005wnb

Structure of antibody 3D3 bound to the linear epitope of RSV G

spinqualitylabelsall models 5wnb, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wnb is a 6 chain structure with sequence from Homo sapiens and Human respiratory syncytial virus A2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: ACY, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monoclonal Antibodies 3D structures

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