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Several parameters which may affect the infectivity of human immunodeficiency virus type 1 in tissue culture were analyzed. In particular, we used gel exclusion chromatography to investigate how the loss of the surface glycoprotein gp120 from virions of the HTLV-IIIB (IIIB), HTLV-IIIRF (RF), and SF-2 isolates modulates infectivity. In IIIB and RF cultures, a high proportion of the total gp120 was virion bound initially but was gradually lost from the virions over time. In contrast, most of the gp120 (and p24) in SF-2-infected cultures was soluble and the few particles present had a fivefold-lower level of virus-bound gp120. However, this reduced level of virion-bound gp120 was more resistant to shedding. Loss of a major proportion of gp120 from IIIB and RF virions resulted in reduced infectivities, and in addition, the resulting accumulation of soluble gp120 in the cultures could competitively inhibit viral infection, especially with SF-2. Increased shedding of virion gp120 also affected the neutralization of IIIB and RF particles. However, the high sensitivity to human serum neutralization characteristic of SF-2 was unaffected by soluble gp120 in cultures, suggesting that the epitopes responsible are not present on soluble gp120.

Original publication

DOI

10.1128/jvi.65.2.852-860.1991

Type

Journal article

Journal

Journal of virology

Publication Date

02/1991

Volume

65

Pages

852 - 860

Addresses

Chester Beatty Laboratories, Institute of Cancer Research, London, United Kingdom.

Keywords

Cell Line, Humans, HIV-1, Virion, HIV Seropositivity, Cell Transformation, Viral, Gene Products, gag, HIV Envelope Protein gp120, HIV Core Protein p24, Viral Core Proteins, Antibodies, Enzyme-Linked Immunosorbent Assay, Neutralization Tests, Chromatography, Gel, Virus Replication, Amino Acid Sequence, Molecular Sequence Data