Rapid Assessment of Relationships Among HIV Isolates by Oligopeptide Analyses of External Envelope Glycoproteins
Autor: | Mikulas Popovic, McLane Mf, Peter J. Fischinger, Max Essex, W G Robey, Peter L. Nara, Francis Barin, C. M. Poore |
---|---|
Rok vydání: | 1987 |
Předmět: |
viruses
Immunology Retroviridae Proteins HIV Envelope Protein gp120 Chromatography Affinity Neutralization Virus Cell Line Microbiology Viral Envelope Proteins Viral envelope Virology Antigenic variation Chymotrypsin Humans chemistry.chemical_classification Oligopeptide biology HIV virus diseases Infectious Diseases chemistry Cell culture biology.protein Electrophoresis Polyacrylamide Gel Antibody Glycoprotein Oligopeptides |
Zdroj: | AIDS Research and Human Retroviruses. 3:401-408 |
ISSN: | 1931-8405 0889-2229 |
DOI: | 10.1089/aid.1987.3.401 |
Popis: | The most variable proteins, the gp120's, of the many isolates of HIV-I can be readily compared by two-dimensional oligopeptide maps. The gp120 in a given cell line is completely stable, but the cell line defines the actual gp120 size and may induce minor peptide changes. HTLV-IIIB and LAV differ slightly from each other even when grown in the same cell line, while LAV grown in a B cell line is less related. Molecularly distant isolates have unique patterns. While anti-HTLV-IIIB gp120 antibody neutralized both HTLV-IIIB and LAV, it recognizes only the homologous HTLV-IIIB infected cells in cytotoxicity assays. Structural analysis of isolates should be helpful in defining the range of immunological reactivities among variants as a contribution to a rational approach to a vaccine against AIDS. |
Databáze: | OpenAIRE |
Externí odkaz: |