5W08
A/Texas/50/2012(H3N2) Influenza hemagglutinin in complex with K03.12 Fab
Summary for 5W08
| Entry DOI | 10.2210/pdb5w08/pdb |
| Related | 5W0D |
| Descriptor | Hemagglutinin HA1, K03.12 antibody heavy chain, K03.12 antibody light chain, ... (8 entities in total) |
| Functional Keywords | fab influenza neutralizing antibody, viral protein-immune system complex, viral protein/immune system |
| Biological source | Influenza A virus (A/Texas/50/2012(H3N2)) More |
| Total number of polymer chains | 18 |
| Total formula weight | 498029.27 |
| Authors | McCarthy, K.R.,Harrison, S.C. (deposition date: 2017-05-30, release date: 2018-02-14, Last modification date: 2024-11-13) |
| Primary citation | McCarthy, K.R.,Watanabe, A.,Kuraoka, M.,Do, K.T.,McGee, C.E.,Sempowski, G.D.,Kepler, T.B.,Schmidt, A.G.,Kelsoe, G.,Harrison, S.C. Memory B Cells that Cross-React with Group 1 and Group 2 Influenza A Viruses Are Abundant in Adult Human Repertoires. Immunity, 48:174-184.e9, 2018 Cited by PubMed Abstract: Human B cell antigen-receptor (BCR) repertoires reflect repeated exposures to evolving influenza viruses; new exposures update the previously generated B cell memory (Bmem) population. Despite structural similarity of hemagglutinins (HAs) from the two groups of influenza A viruses, cross-reacting antibodies (Abs) are uncommon. We analyzed Bmem compartments in three unrelated, adult donors and found frequent cross-group BCRs, both HA-head directed and non-head directed. Members of a clonal lineage from one donor had a BCR structure similar to that of a previously described Ab, encoded by different gene segments. Comparison showed that both Abs contacted the HA receptor-binding site through long heavy-chain third complementarity determining regions. Affinities of the clonal-lineage BCRs for historical influenza-virus HAs from both group 1 and group 2 viruses suggested that serial responses to seasonal influenza exposures had elicited the lineage and driven affinity maturation. We propose that appropriate immunization regimens might elicit a comparably broad response. PubMed: 29343437DOI: 10.1016/j.immuni.2017.12.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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