Antigenicity and immunogenicity of domains of the human immunodeficiency virus (HIV) envelope polypeptide expressed in the yeast Saccharomyces cerevisiae

Barr, Philip J.; Steimer, K.S.; Sabin, Elizabeth A.; Parkes, Debbie; George-Nascimento, Carlos; Stephens, John E.; Powers, Maureen A.; Gyenes, A; VANNEST, G; Miller, Emma Parker

doi:10.1016/0264-410x(87)90053-3

Cited by 64 publications

(27 citation statements)

References 44 publications

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“…The gp120 expressed in E. coli or yeast does not bind CD4 and is nonglycosylated (Barr et al 1987;Haigwood et al 1990;Morikawa et al 1990a). Both mammalian (Chakrabarti et al 1986;Hu et al 1986;Kieny et al 1986;Dewar et al 1989) and insect (Hu et al 1987;Lynn et al 1988;Wells & Compans 1990;Morikawa et al 1990b) viral vectors have been successfully used to produce a small amount of recombinant gp120 or gp120/gp41 which is capable of binding to CD4.…”

Section: Introductionmentioning

confidence: 99%

Sendai virus‐based expression of HIV‐1 gp120: reinforcement by the V(−) version

Yu¹,

Shioda²,

Kato³

et al. 1997

Genes to Cells

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Background: We have established a system for recovering Sendai virus (SeV), a nonsegmented negative strand RNA virus, entirely from cDNA at an extremely high rate, and have succeeded in creating a V(-) SeV whose gene expression was greatly enhanced by the deletion of the nonessential V gene. Because of its extreme medical importance, there has been a strong need for the establishment of a better system to express the gp120 envelope glycoprotein of the human immunodeficiency virus type 1 (HIV-1) in sufficient quantity and purity. It also remains to be established to produce gp120 in in vitro natural host cells for HIV-1 such as human primary blood mononuclear cells, macrophages or established T cell lines.

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Section: Introductionmentioning

confidence: 99%

Sendai virus‐based expression of HIV‐1 gp120: reinforcement by the V(−) version

Yu¹,

Shioda²,

Kato³

et al. 1997

Genes to Cells

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“…Research Laboratories, Emeryville, CA) were produced in the yeast, Sacchromyces cerevisiae, using intracellular expression vectors similar to those described previously (9). These vectors yield products that are not glycosylated.…”

Section: Introductionmentioning

confidence: 99%

“…All of these antigens were insoluble when produced intracellularly in yeast. The recombinant antigens were purified from the insoluble fraction of yeast lysates as described previously for other recombinant HIV-1 envelope polypeptides (9). Fig.…”

Section: Introductionmentioning

confidence: 99%

Identification of human immunodeficiency virus (HIV) envelope type-specific T helper cells in an HIV-infected individual.

Walker

Steimer²,

Rosenthal³

et al. 1988

J. Clin. Invest.

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MethodsTwo T helper cell clones recognizing the gp 120 envelope protein of HIV were generated from the peripheral blood of a healthy seropositive individual. These cells were type specific as they proliferated and produced IL 2 when stimulated by an epitope in the amino-terminal half of gp 120 of HIVsF2, but not by a similar region of HIVz,6, a Zairian HIV-1 isolate. These two viruses differ by 26% in the deduced amino sequence of the gp 120 protein. Moreover, the antigenic site(s) recognized by the cloned T cells are distinct from those recognized by envelope-specific antibodies. These observations have important implications for the development and use of anti-HIV vaccines.

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“…In addition to the env2-3 (SF2) antigen from HIV-l(SF2), equivalent molecules from two other HIV-l isolates, HN/HTLV-IIIB (human T lymphotropic virus type IIIB) [27] and HIV(Zr6) [28], were used in serologic assays. These antigens were purified as described previously [16,17,29]. Fully glycosylated native gp120 from HIV-l(SF2), referred to as gp120 (SF2), which retains the ability to bind to CD4, was produced in genetically engineered CHO cells [30].…”

Section: Methodsmentioning

confidence: 99%