Change in size of the envelope glycoprotein of a human immunodeficiency virus 1 (HIV 1) strain

• Published in: Microbiologica Vol. 14; no. 1; p. 15
• Main Authors: Vitale, F, Russo Alesi, D, Bonura, F, Di Benedetto, M A, Mammina, C, Romano, N
• Format: Journal Article
• Language: English
• Published: Italy 01.01.1991
• Subjects: Acquired Immunodeficiency Syndrome - microbiology; Adult; Electrophoresis, Polyacrylamide Gel; env Gene Products, Human Immunodeficiency Virus; Gene Products, env - chemistry; HIV-1 - analysis; HIV-1 - immunology; HIV-1 - pathogenicity; Humans; Male; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - immunology; Molecular Weight; Radioimmunoprecipitation Assay; Retroviridae Proteins - chemistry; Tunicamycin - pharmacology; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - immunology; Virulence
• ISSN: 0391-5352

A strain of HIV 1 (PA 40), isolated from a patient with AIDS, showed a size variation of its external glycoprotein. This glycoprotein had an estimated molecular weight of 105 Kd and differed from that of both HIV 1 IIIb and HIV 2 Rod strains. The protein was derived from a bigger (140 Kd) precursor, detectable only in the infected cells and could incorporate labeled glucose in its prosthetic portion. The change in size of the external glycoprotein may be the result of envelope sequence variations since the unglycosylated form of the envelope precursor of PA 40 strain, detected in tunicamycin treated cells, was smaller than that of the HIV 1 IIIb strain. The different size of the external glycoprotein is a further aspect of the variability of the biological characteristic of HIV 1 strains and might be correlated with the emergence of more virulent variants which arose during the progression of the clinical disease.