H2N2V1, Main, Exploration, bibRecord, 000B07

Structural insights into key sites of vulnerability on HIV‐1 Env and influenza HA

Identifieur interne : 000B07 ( Main/Exploration ); précédent : 000B06; suivant : 000B08

Structural insights into key sites of vulnerability on HIV‐1 Env and influenza HA

Auteurs : Jean-Philippe Julien [États-Unis] ; Peter S. Lee [États-Unis] ; Ian A. Wilson [États-Unis]

Source :

Immunological Reviews [ 0105-2896 ] ; 2012-11.

RBID : ISTEX:E2A1E933328DDEEF9F20F4B8AD44AD33C5586457

English descriptors

Teeft :
- Acad, Antibody, Antibody responses, Antigenic, Binding site, Biol, Biol chem, Bnab, Bnabs, Carbohydrate, Cd4bs, Chem, Conformational, Conformational change, Crystal structure, Crystal structures, Curr, Different subtypes, Electron microscopy studies, Elite neutralizers, Entry process, Envelope glycoprotein, Envelope glycoproteins, Epitope, External region, Fusion machinery, Germline, Glycan, Glycan coat, Glycan recognition, Glycan shield, Glycans, Glycoprotein, Glycosylation, Glycosylation sites, Hcdr3, Heavy chain, Hemagglutinin, High degree, Hiv1, Host cells, Human envelope protein, Human virus, Human virus type, Humoral, Hydrogen bonds, Immune, Immune evasion, Immune response, Immunogen, Immunogen design, John wiley sons, Julien, Membrane, Membrane fusion, Moiety, Monoclonal antibodies, Mper, Natl, Neutralization, Neutralizing, Neutralizing antibodies, Neutralizing antibody, Neutralizing antibody responses, Oligomannose, Outer domain, Pandemic, Pandemic virus, Pathog, Peptide, Plo, Plos pathog, Potent neutralization, Potential glycosylation sites, Proc, Proc natl acad, Quaternary, Receptor, Receptor binding, Receptor binding site, Residue, Reviews julien, Scripps research institute, Secondary structure, Sequence variability, Sequence variation, Sialic, Sialic acid, Skehel, Small molecules, Spike, Structural basis, Structural characterization, Structural information, Subtypes, Trimer, Trimeric, Universal vaccine, Vaccination, Vaccine, Vaccine design, Viral, Viral entry, Viral infection, Viral membrane, Virol, Virology, Virus, Virus hemagglutinin, Virus type, Wiley.

Abstract

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.

Url:

DOI: 10.1111/imr.12005

Affiliations:

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<term>Human envelope protein</term>
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<term>Human virus type</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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Structural insights into key sites of vulnerability on HIV‐1 Env and influenza HA

Structural insights into key sites of vulnerability on HIV‐1 Env and influenza HA

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Abstract

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