EMD-22551
Polyclonal immune complex of Fab binding the receptor binding site region of H5 HA from serum of subject 36 at day 28
EMD-22551
Single-particle20.0 Å
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Map released: 03/03/2021
Last modified: 03/03/2021
Sample Organism:
Homo sapiens
Sample: Polyclonal immune complex of Fab binding the receptor binding site region of H5 HA from serum of subject 36 at day 28
Deposition Authors: Ward A, Han J, Richey ST
Sample: Polyclonal immune complex of Fab binding the receptor binding site region of H5 HA from serum of subject 36 at day 28
Deposition Authors: Ward A, Han J, Richey ST
Polyclonal epitope mapping reveals temporal dynamics and diversity of human antibody responses to H5N1 vaccination.
Han J,
Schmitz AJ
,
Richey ST,
Dai YN,
Turner HL,
Mohammed BM,
Fremont DH
,
Ellebedy AH,
Ward AB
(2021) Cell Rep , 34 , 108682 - 108682
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(2021) Cell Rep , 34 , 108682 - 108682
Abstract:
Novel influenza A virus (IAV) strains elicit recall immune responses to conserved epitopes, making them favorable antigenic choices for universal influenza virus vaccines. Evaluating these immunogens requires a thorough understanding of the antigenic sites targeted by the polyclonal antibody (pAb) response, which single-particle electron microscopy (EM) can sensitively detect. In this study, we employ EM polyclonal epitope mapping (EMPEM) to extensively characterize the pAb response to hemagglutinin (HA) after H5N1 immunization in humans. Cross-reactive pAbs originating from memory B cells immediately bound the stem of HA and persisted for more than a year after vaccination. In contrast, de novo pAb responses to multiple sites on the head of HA, targeting previously determined key neutralizing sites on H5 HA, expanded after the second immunization and waned quickly. Thus, EMPEM provides a robust tool for comprehensively tracking the specificity and durability of immune responses elicited by novel universal influenza vaccine candidates.
Novel influenza A virus (IAV) strains elicit recall immune responses to conserved epitopes, making them favorable antigenic choices for universal influenza virus vaccines. Evaluating these immunogens requires a thorough understanding of the antigenic sites targeted by the polyclonal antibody (pAb) response, which single-particle electron microscopy (EM) can sensitively detect. In this study, we employ EM polyclonal epitope mapping (EMPEM) to extensively characterize the pAb response to hemagglutinin (HA) after H5N1 immunization in humans. Cross-reactive pAbs originating from memory B cells immediately bound the stem of HA and persisted for more than a year after vaccination. In contrast, de novo pAb responses to multiple sites on the head of HA, targeting previously determined key neutralizing sites on H5 HA, expanded after the second immunization and waned quickly. Thus, EMPEM provides a robust tool for comprehensively tracking the specificity and durability of immune responses elicited by novel universal influenza vaccine candidates.