PLOS Pathogens · 10 authors, 9 centres
This summary was generated by AI from a single paper. It has not been reviewed by a clinician and is not clinical advice. Verify against the source before acting on it.
This preclinical study analyzed a human monoclonal antibody, LAH31, that targets a unique epitope on influenza virus hemagglutinin only exposed after the virus enters its postfusion state. The antibody provides cross-group protection by binding this non-native epitope via its mutated light chain and mediating Fc-dependent clearance of infected cells.
This study performed an in-depth structural and functional analysis of the human monoclonal antibody LAH31, which targets a stem-helix kinked loop epitope on influenza virus hemagglutinin (HA) that is occluded in the native prefusion state but exposed after conversion to the postfusion state. Structural analysis and molecular modeling revealed that LAH31's cross-group breadth relies on somatically mutated light chain CDRs, distinct from other IGHV1-69-type antibodies. While LAH31 was inaccessible to prefusion HA on cell surfaces, it bound to HA on infected cells, mediating Fc-dependent clearance mechanisms like ADCC. The study demonstrates that postfusion HA can be a target for broadly protective antibodies, suggesting implications for next-generation universal vaccine design by focusing on conserved, non-native epitopes.
