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PMID: 10623724 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure.

Journal of virology ·Vol. 74 ·No. 2 ·2000-01-00 ·Pages 627-43

Binley JM, Sanders RW, Clas B, Schuelke N, Master A, Guo Y, Kajumo F, Anselma DJ, Maddon PJ, Olson WC, Moore JP

Abstract

The few antibodies that can potently neutralize human immunodeficiency virus type 1 (HIV-1) recognize the limited number of envelope glycoprotein epitopes exposed on infectious virions. These native envelope glycoprotein complexes comprise three gp120 subunits noncovalently and weakly associated with three gp41 moieties. The individual subunits induce neutralizing antibodies inefficiently but raise many nonneutralizing antibodies. Consequently, recombinant envelope glycoproteins do not elicit strong antiviral antibody responses, particularly against primary HIV-1 isolates. To try to develop recombinant proteins that are better antigenic mimics of the native envelope glycoprotein complex, we have introduced a disulfide bond between the C-terminal region of gp120 and the immunodominant segment of the gp41 ectodomain. The resulting gp140 protein is processed efficiently, producing a properly folded envelope glycoprotein complex. The association of gp120 with gp41 is now stabilized by the supplementary intermolecular disulfide bond, which forms with approximately 50% efficiency. The gp140 protein has antigenic properties which resemble those of the virion-associated complex. This type of gp140 protein may be worth evaluating for immunogenicity as a component of a multivalent HIV-1 vaccine.

MeSH Terms
Amino Acid Sequence Amino Acid Substitution Antigens, Viral/genetics,immunology,metabolism Cell Line, Transformed Centrifugation, Density Gradient Chromatography, Gel Cysteine/genetics Disulfides/metabolism Furin Gene Products, env/genetics,immunology,metabolism Glycoproteins/genetics,immunology,metabolism HIV Envelope Protein gp120/genetics,immunology,metabolism HIV Envelope Protein gp41/genetics,immunology,metabolism HIV-1/isolation & purification Humans Molecular Sequence Data Protein Processing, Post-Translational Recombinant Fusion Proteins/genetics,immunology,metabolism Subtilisins/metabolism Sucrose Virion env Gene Products, Human Immunodeficiency Virus
Chemicals
Antigens, Viral Disulfides Gene Products, env Glycoproteins HIV Envelope Protein gp120 HIV Envelope Protein gp41 Recombinant Fusion Proteins env Gene Products, Human Immunodeficiency Virus gp140 envelope protein, Human immunodeficiency virus 1 Sucrose Subtilisins Furin Cysteine
Authors & Affiliations
11 authors, click to expand affiliations / ORCID
Binley J M
Aaron Diamond AIDS Research Center, The Rockefeller University, New York, New York 10016, USA.
Sanders R W
Clas B
Schuelke N
Master A
Guo Y
Kajumo F
Anselma D J
Maddon P J
Olson W C
Moore J P
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/jvi.74.2.627-643.2000
Published
2000-01-00
Pages
627-43
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC111582
Subset
IM
Grants
NIAID NIH HHS · R01 AI039420 · United States
NIAID NIH HHS · R01 AI045463 · United States
NIAID NIH HHS · R01 AI 39420 · United States
NIAID NIH HHS · R01 AI 45463 · United States
External Links
PubMed source DOI: 10.1128/jvi.74.2.627-643.2000 PMC Full Text View journal details
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