8GV7
Crystal structure of PN-SIA28 in complex with influenza hemagglutinin H18 A/flat-faced bat/Peru/033/2010
Summary for 8GV7
Entry DOI | 10.2210/pdb8gv7/pdb |
Descriptor | Hemagglutinin H18-HA1, Hemagglutinin H18-HA2, PN-SIA28 heavy chain, ... (9 entities in total) |
Functional Keywords | influenza, hemagglutinin, antibody, broadly neutralizing, viral protein, viral protein-immune system complex, viral protein/immune system |
Biological source | Influenza A virus (A/flat-faced bat/Peru/033/2010(H18N11)) More |
Total number of polymer chains | 4 |
Total formula weight | 83790.09 |
Authors | |
Primary citation | Chen, Y.,Wang, F.,Yin, L.,Jiang, H.,Lu, X.,Bi, Y.,Zhang, W.,Shi, Y.,Burioni, R.,Tong, Z.,Song, H.,Qi, J.,Gao, G.F. Structural basis for a human broadly neutralizing influenza A hemagglutinin stem-specific antibody including H17/18 subtypes. Nat Commun, 13:7603-7603, 2022 Cited by PubMed Abstract: Influenza infection continues are a persistent threat to public health. The identification and characterization of human broadly neutralizing antibodies can facilitate the development of antibody drugs and the design of universal influenza vaccines. Here, we present structural information for the human antibody PN-SIA28's heterosubtypic binding of hemagglutinin (HA) from circulating and emerging potential influenza A viruses (IAVs). Aside from group 1 and 2 conventional IAV HAs, PN-SIA28 also inhibits membrane fusion mediated by bat-origin H17 and H18 HAs. Crystallographic analyses of Fab alone or in complex with H1, H14, and H18 HA proteins reveal that PN-SIA28 binds to a highly conserved epitope in the fusion domain of different HAs, with the same CDRHs but different CDRLs for different HAs tested, distinguishing it from other structurally characterized anti-stem antibodies. The binding characteristics of PN-SIA28 provides information to support the design of increasingly potent engineered antibodies, antiviral drugs, and/or universal influenza vaccines. PubMed: 36494358DOI: 10.1038/s41467-022-35236-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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