HIV Antigens for Disease Intervention
Abstract
HIV-1 is the etiologic agent of AIDS. The outer envelope glycoprotein of HIV-1 is more than half sugar, with an average of 24 N-linked glycosylation sites. The sugar mass may provide a form of immune masking. In this effort, we evaluated, by site directed mutagenesis, the relative importance of each of the 24 N-linked glycosylation sites of gpl20 in the molecular clone HXB2 in terms of viral infectivity. We found that most of the individual consensus N-linked glycosylation sites are dispensable for activity, and that the five consensus N- linked sites that are likely to have important roles in infectivity are all located in the amino terminal half of gpl20, indicating that the N-linked glycosylation sites important for infectivity are not randomly distributed in gpl20. In comparing the N-linked glycosylation sites of the N-terminal and C- terminal region of gpl20, combination glycosylation site mutants were generated. While N-linked oligosaccharides at the C-terminus were not critical, the removal of three or more N-linked glycosylation sites from the N-terminal region affected envelope processing and viral infectivity. The conservation of carbohydrate moieties at the C-terminus of gpl20 may be an evolutionary response for HIV to escape immune masking. Based on this, we believe that gp 120 molecules that lack some of the N-linked glycosylation sites in the C-terminal half will be better candidates for vaccines. HIV; Envelope; Gpl20; Vaccine development; AIDS; RA 1.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 27, 1992
- Accession Number
- ADA253796
Entities
People
- Tun-hou Lee
Organizations
- Harvard University