| Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA. | |
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MedLine Citation:
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PMID: 23046130 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Jean-Philippe Julien; Peter S Lee; Ian A Wilson |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: Immunological reviews Volume: 250 ISSN: 1600-065X ISO Abbreviation: Immunol. Rev. Publication Date: 2012 Nov |
Date Detail:
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Created Date: 2012-10-10 Completed Date: 2013-02-25 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 7702118 Medline TA: Immunol Rev Country: England |
Other Details:
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Languages: eng Pagination: 180-98 Citation Subset: IM |
Copyright Information:
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© 2012 John Wiley & Sons A/S. |
Affiliation:
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Department of Molecular Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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AIDS Vaccines
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chemistry,
immunology Antibodies, Neutralizing / chemistry*, immunology, pharmacology Antigenic Variation Gene Products, env / antagonists & inhibitors, chemistry*, immunology HIV Antibodies / chemistry*, immunology, pharmacology HIV-1 / drug effects, immunology Hemagglutinin Glycoproteins, Influenza Virus / chemistry*, immunology, metabolism Humans Influenza A virus / drug effects, immunology Influenza Vaccines / chemistry, immunology Models, Molecular Receptors, Virus / antagonists & inhibitors*, immunology Species Specificity Structural Homology, Protein Virus Internalization / drug effects |
| Grant Support | |
ID/Acronym/Agency:
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AI84817/AI/NIAID NIH HHS; GM080209/GM/NIGMS NIH HHS; R01 AI084817/AI/NIAID NIH HHS; T32 GM080209/GM/NIGMS NIH HHS; //Canadian Institutes of Health Research |
| Chemical | |
Reg. No./Substance:
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0/AIDS Vaccines; 0/Antibodies, Neutralizing; 0/Gene Products, env; 0/HIV Antibodies; 0/Hemagglutinin Glycoproteins, Influenza Virus; 0/Influenza Vaccines; 0/Receptors, Virus; 0/hemagglutinin, human influenza A virus |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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