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Structural insights into key sites of vulnerability on HIV ‐1 Env and influenza HA
Author(s) -
Julien JeanPhilippe,
Lee Peter S.,
Wilson Ian A.
Publication year - 2012
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/imr.12005
Subject(s) - virology , biology , context (archaeology) , hemagglutinin (influenza) , glycoprotein , viral envelope , virus , gp41 , antibody , viral entry , immune system , glycosylation , hiv vaccine , immunology , human immunodeficiency virus (hiv) , viral replication , epitope , genetics , vaccine trial , paleontology
Summary Human immunodeficiency virus‐1 ( HIV ‐1) envelope protein (Env) and influenza hemagglutinin ( HA ) are the surface glycoproteins responsible for viral entry into host cells, the first step in the virus life cycle necessary to initiate infection. These glycoproteins exhibit a high degree of sequence variability and glycosylation, which are used as strategies to escape host immune responses. Nonetheless, antibodies with broadly neutralizing activity against these viruses have been isolated that have managed to overcome these barriers. Here, we review recent advances in the structural characterization of these antibodies with their viral antigens that defines a few sites of vulnerability on these viral spikes. These broadly neutralizing antibodies tend to focus their recognition on the sites of similar function between the two viruses: the receptor‐binding site and membrane fusion machinery. However, some sites of recognition are unique to the virus neutralized, such as the dense shield of oligomannose carbohydrates on HIV ‐1 Env. These observations are discussed in the context of structure‐based design strategies to aid in vaccine design or development of antivirals.