دورية أكاديمية
The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120.
| العنوان: | The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. |
|---|---|
| المؤلفون: | Sanders RW; Dept. of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA., Venturi M, Schiffner L, Kalyanaraman R, Katinger H, Lloyd KO, Kwong PD, Moore JP |
| المصدر: | Journal of virology [J Virol] 2002 Jul; Vol. 76 (14), pp. 7293-305. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society For Microbiology Country of Publication: United States NLM ID: 0113724 Publication Model: Print Cited Medium: Print ISSN: 0022-538X (Print) Linking ISSN: 0022538X NLM ISO Abbreviation: J Virol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Washington Dc : American Society For Microbiology Original Publication: Baltimore, American Society for Microbiology. |
| مواضيع طبية MeSH: | Epitope Mapping*, Antibodies, Monoclonal/*immunology , HIV Antibodies/*immunology , HIV Envelope Protein gp120/*immunology , Mannose/*chemistry, Carbohydrate Sequence ; Glycoside Hydrolases/metabolism ; Glycosylation ; HIV Envelope Protein gp120/chemistry ; HIV Envelope Protein gp120/genetics ; HIV-1/immunology ; Humans ; Mannose/metabolism ; Models, Molecular ; Molecular Sequence Data ; Neutralization Tests ; Sequence Analysis, DNA |
| مستخلص: | We have analyzed the unique epitope for the broadly neutralizing human monoclonal antibody (MAb) 2G12 on the gp120 surface glycoprotein of human immunodeficiency virus type 1 (HIV-1). Sequence analysis, focusing on the conservation of relevant residues across multiple HIV-1 isolates, refined the epitope that was defined previously by substitutional mutagenesis (A. Trkola, M. Purtscher, T. Muster, C. Ballaun, A. Buchacher, N. Sullivan, K. Srinivasan, J. Sodroski, J. P. Moore, and H. Katinger, J. Virol. 70:1100-1108, 1996). In a biochemical study, we digested recombinant gp120 with various glycosidase enzymes of known specificities and showed that the 2G12 epitope is lost when gp120 is treated with mannosidases. Computational analyses were used to position the epitope in the context of the virion-associated envelope glycoprotein complex, to determine the variability of the surrounding surface, and to calculate the surface accessibility of possible glycan- and polypeptide-epitope components. Together, these analyses suggest that the 2G12 epitope is centered on the high-mannose and/or hybrid glycans of residues 295, 332, and 392, with peripheral glycans from 386 and 448 on either flank. The epitope is mannose dependent and composed primarily of carbohydrate, with probably no direct involvement of the gp120 polypeptide surface. It resides on a face orthogonal to the CD4 binding face, on a surface proximal to, but distinct from, that implicated in coreceptor binding. Its conservation amidst an otherwise highly variable gp120 surface suggests a functional role for the 2G12 binding site, perhaps related to the mannose-dependent attachment of HIV-1 to DC-SIGN or related lectins that facilitate virus entry into susceptible target cells. |
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| معلومات مُعتمدة: | AI39420 United States AI NIAID NIH HHS; R01 AI039420 United States AI NIAID NIH HHS; R01 AI036082 United States AI NIAID NIH HHS; R37 AI036082 United States AI NIAID NIH HHS; AI45463 United States AI NIAID NIH HHS; R01 AI045463 United States AI NIAID NIH HHS; AI36082 United States AI NIAID NIH HHS |
| المشرفين على المادة: | 0 (Antibodies, Monoclonal) 0 (HIV Antibodies) 0 (HIV Envelope Protein gp120) EC 3.2.1.- (Glycoside Hydrolases) PHA4727WTP (Mannose) |
| تواريخ الأحداث: | Date Created: 20020620 Date Completed: 20020725 Latest Revision: 20200409 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC136300 |
| DOI: | 10.1128/jvi.76.14.7293-7305.2002 |
| PMID: | 12072528 |
| قاعدة البيانات: | MEDLINE |
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