Detection of Antibodies to Human T-Cell Lymphotropic Virus-III (HTLV-III) with an Immunoassay Employing a Recombinant Escherichia coli-Derived Viral Antigenic Peptide

Chang, Tse Wen; Kato, Ikuo; McKinney, Sam; Chanda, Pranab K.; Barone, Anthony D.; Wong‐Staal, Flossie; Gallo, Robert C.; Chang, Nancy

doi:10.1038/nbt1085-905

Cited by 65 publications

(32 citation statements)

References 20 publications

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“…We thus performed an analysis similar to that shown in Fig. 2 B and C using an affinity column containing the recombinant peptide 121 (17). This molecule contains only about one-half of the gp4l sequences but a major portion of the immunodominant epitopes of gp4l (17).…”

Section: Resultsmentioning

confidence: 99%

Restricted neutralization of divergent human T-lymphotropic virus type III isolates by antibodies to the major envelope glycoprotein.

Matthews¹,

Langlois²,

Robey³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

186

104

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By analogy to other retroviruses, the major envelope glycoprotein, gpl20, of human T-lymphotropic virus type III (HTLV-Ill) is a probable target for neutralizing antibody. This antigen has been purified from H9 cells chronically infected with the HTLV-IllB prototype strain. Several goats immunized with the gpl20 produced antibodies that neutralized infection of H9 cells by the homologous virus isolate. These same sera failed to neutralize the divergent HTLV-IllRF isolate. Individuals infected with HTLV-11I commonly develop antibodies to gpl20 that could be isolated by using the gpl20 antigen coupled to an immunoadsorbent resin. The antibody fraction that bound tightly to such a resin was found to neutralize the IIIB but not the RF isolate in a similar fashion as the goat anti-gpl20 sera. However, the nonbinding fraction (effluent) from the resin also contained neutralizing activity that was able to block infection by both virus isolates with similar efficacy. Human antibodies to the other virus envelope gene product, the transmembrane gp4l, were also affinity purified by utilizing the recombinant peptide 121, but these failed to influence infection by either virus isolate.

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Section: Resultsmentioning

confidence: 99%

Restricted neutralization of divergent human T-lymphotropic virus type III isolates by antibodies to the major envelope glycoprotein.

Matthews¹,

Langlois²,

Robey³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

186

104

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“…Rather, the goal of this study was to localize T-cell sites from the HIV envelope that might be useful in vaccine development, as, to our knowledge, no T-cell epitopes have been identified in any AIDS virus protein. Studies with AIDS virus peptides have been directed at antibody specificities (1)(2)(3)(4)(5)(6)(7)(8)(9) or pharmacologic blocking of gpl20 binding to CD4 (51) and have dealt with sites distinct from those of the present study.…”

Section: Discussionmentioning

confidence: 99%

Helper T-cell antigenic site identification in the acquired immunodeficiency syndrome virus gp120 envelope protein and induction of immunity in mice to the native protein using a 16-residue synthetic peptide.

Cease¹,

Margalit²,

Cornette³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

165

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authors request that the following correction be noted. Mutant 49 of the Tac receptor subunit in which Thr-85, Thr-86 were replaced by Ala-85, Gly-86 was also modified at the C terminus of the polypeptide chain. The oligonucleotide used in the mutation reaction apparently hybridized with the single-stranded template at the correct location surrounding Thr-85, Thr-86 and also at a site after the codon for Gln-202. As a consequence, the C-terminal region of the mutant 49 protein differed markedly from that of the native molecule. The mutant protein bound to affinity supports coupled with interleukin 2 and the anti-Tac monoclonal antibody, but was defective for expression on the cell surface. Examination of a new mutant of the Tac protein in which Thr-85 and Thr-86 were replaced by Ala and Gly, respectively, but in which the remaining sequence was identical to that of the native protein, indicates that this substitution has no effect on cell-surface expression. Moreover Correction. In the article "Helper T-cell antigenic site identification in the acquired immunodeficiency syndrome virus gp120 envelope protein and induction of immunity in mice to the native protein using a 16-residue synthetic peptide" by

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“…In certain protocols, used successfully to solubilize recombinant polypeptides, thiol reagents were used in conjunction with the denaturants (Cabilly et al, 1984;George et al, 1985;Koths et al, 1985;Vogel et al, 1985;Chang et al, 1985;Winkler et al, 1985). If the inclusion of thiol reagents is essential for the recovery of activity, covalent disulphide bonds may exist in the aggregates Many of the eukaryotic polypeptides insoluble when expressed in the E. coli cytoplasm are normally secreted by their natural cells and contain disulphide bonds which form between cysteine residues during the process of secretion.…”

Section: Direct Expressionmentioning

confidence: 99%

The purification of eukaryotic polypeptides synthesized in Escherichia coli

Marston¹

1986

Biochemical Journal

858

379

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Detection of Antibodies to Human T-Cell Lymphotropic Virus-III (HTLV-III) with an Immunoassay Employing a Recombinant Escherichia coli-Derived Viral Antigenic Peptide

Cited by 65 publications

References 20 publications

Restricted neutralization of divergent human T-lymphotropic virus type III isolates by antibodies to the major envelope glycoprotein.

Restricted neutralization of divergent human T-lymphotropic virus type III isolates by antibodies to the major envelope glycoprotein.

Helper T-cell antigenic site identification in the acquired immunodeficiency syndrome virus gp120 envelope protein and induction of immunity in mice to the native protein using a 16-residue synthetic peptide.

The purification of eukaryotic polypeptides synthesized in Escherichia coli

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