A cross-neutralizing antibody between HIV-1 and influenza virus

نویسندگان

چکیده

Incessant antigenic evolution enables the persistence and spread of influenza virus in human population. As principal target immune response, hemagglutinin (HA) surface antigen on viruses continuously acquires replaces N -linked glycosylation sites to shield immunogenic protein epitopes using host-derived glycans. Anti-glycan antibodies, such as 2G12, HIV-1 envelope (Env), which is even more extensively glycosylated contains under-processed oligomannose-type clusters its dense glycan shield. Here, we illustrate that 2G12 can also neutralize seasonal A H3N2 have evolved present similar their HAs from around 20 years after 1968 pandemic. Using structural biology mass spectrometric approaches, find two -glycosylation close receptor binding site (RBS) represent oligomannose cluster recognized by 2G12. One these highly conserved all strains other emerged during evolution. These become crucial for fitness recent strains. findings shed light suggest 2G12-like antibodies potentially act broad neutralizers enveloped viruses.

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ژورنال

عنوان ژورنال: PLOS Pathogens

سال: 2021

ISSN: ['1553-7366', '1553-7374']

DOI: https://doi.org/10.1371/journal.ppat.1009407