Year: 2020
Type: review
Abstract: Influenza virus constantly acquires genetic mutations/reassortment in the major surface protein, hemagglutinin (HA), resulting in the generation of strains with antigenic variations. There are, however, HA epitopes that are conserved across influenza viruses and are targeted by broadly protective antibodies. A goal for the next-generation influenza vaccines is to stimulate B-cell responses against such conserved epitopes in order to provide broad protection against divergent influenza viruses. Broadly protective B cells, however, are not easily activated by HA antigens with native structure, because the virus has multiple strategies to escape from the humoral immune responses directed to the conserved epitopes. One such strategy is to hide the conserved epitopes from the B-cell surveillance by steric hindrance. Technical advancement in the analysis of the human B-cell antigen receptor (BCR) repertoire has dissected the BCRs to HA epitopes that are hidden in the native structure but are targeted by broadly protective antibodies. We describe here the characterization and function of broadly protective antibodies and strategies that enable B cells to seek these hidden epitopes, with potential implications for the development of universal influenza vaccines.
Source: International Immunology
Institutions: Duke University, National Institute of Infectious Diseases
Language: English
Subfield: Epidemiology
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
Awards: Immunity to novel T/F SHIVs: variability in the co-evolution of virus and host immunity, Understanding the development and protective mechanism of broadly reactive influenza antibody, Cross-protective antibody response in the lungs upon influenza virus infection, Modeling affinity maturation at molecular resolution, G9000028040, G9000337902, Structure-function analysis of infection- and vaccine-induced B-cell repertoires
OpenAlex ID: W3017312411