Characterization of Envelope and Core Structural Gene Products of HTLV-III with Sera from AIDS Patients

Abstract

The envelope (env) and structural (gag) gene products of human T-cell leukemia (lymphotropic) virus type III were identified by immunoaffinity chromatography, immunoprecipitation, and two-dimensional oligopeptide mapping methods. The env gene specifies a glycosylated polypeptide with a molecular weight of 160,000 (gp160) that is processed to gp120 and smaller gene products. The gag gene specifies two polypeptides of 70,000 and 55,000 molecular weight (p70 and p55), both of which contain p24, the major structural protein of the mature virion. The techniques in this study can be used to define the extent of variability of the env gene product among different virus isolates and may identify the nature and patterns of the humoral immune response that lead to an immunologically protected state.

Virus-specific Polypeptides of Caprine Arthritis-Encephalitis Virus Recognized by Monoclonal Antibodies to Virion Proteins p24 and p14

“…We did not detect the cell-associated 49K polypeptide described for EIAV (Henderson et al, 1987). However, under conditions of prolonged incubation with several changes of MAb, we detected a 70K CAEV protein which may be analogous to the 70K polypeptide present at low levels in HIV-l-infected cells (Robey et al, 1985). Other CAEV protein bands detected only weakly by the MAbs to p24 and p14 may represent either degradation products or minor proteolytic fragments resulting from the incomplete cleavage of the gag gene precursor.…”

“…However, little information is available to date on the production and processing of the CAEV gag gene product. The CAEV 55K, 41K and 33K polypeptides identified in this study may be analogous to the p55, p50 and p35 detected in VV (Vigne et al, 1982), to the p55, p41 to p43 and p34 described for HIV (Robey et al, 1985) and to the p55, p40 and p35 of EIAV (Henderson et al, 1987). We did not detect the cell-associated 49K polypeptide described for EIAV (Henderson et al, 1987).…”

“…The structural proteins of the gag gene of retroviruses are derived by proteolytic cleavage of a polypeptide precursor (reviewed by Dickson et al, 1982). In both VV and HIV, this gag gene precursor is believed to be a polypeptide of approximately 55K, as determined from pulse-chase experiments (Vigne et al, 1982;Robey et al, 1985) and from nucleic acid sequencing data (Sonigo et al, 1985;Ratner et al, 1985). The appearance of several intermediates in the processing of gag precursors to the mature polypeptides has been well documented for avian and murine RNA tumour viruses (Dickson et al, 1982).…”

“…The appearance of several intermediates in the processing of gag precursors to the mature polypeptides has been well documented for avian and murine RNA tumour viruses (Dickson et al, 1982). Several proteins which are serologically related to the major core protein have been observed in lysates of cells infected with VV (Vigne et al, 1982), HIV (Robey et al, 1985) and EIAV (Henderson et al, 1987) in addition to the 55K polypeptide. However, little information is available to date on the production and processing of the CAEV gag gene product.…”

Monoclonal Idiotypic and Anti-idiotypic Antibodies to Human Immunodeficiency Virus Type 1 Envelope Glycoprotein

“…During viral maturation, the env gene product of HIV-1 (160K) is glycosylated and further processed to a 120K external envelope glycoprotein (Robey et al, 1985) and a 41K transmembrane glycoprotein (Di Marzo-Veronese et al, 1985). These envelope glycoproteins are involved in virus-cell receptor interactions (McDougal et al, 1986), virus-ceU fusion and syncytium formation (Lifson et al, 1986 ;Sodroski et al, 1986;Kowalski et al, 1987;Stein et al, 1987) and the induction of neutralizing antibodies (Chanh et al, 1986;Dalgleish et al, 1988;Evans et al, 1989).…”