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

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Published inJournal of Virology Vol. 74; no. 2; pp. 627 - 643
Main Authors Binley, J M, 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
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.01.2000
Subjects
AIDS/HIV
Amino Acid Sequence
Amino Acid Substitution
Antigens, Viral - genetics
Antigens, Viral - immunology
Antigens, Viral - metabolism
Cell Line, Transformed
Centrifugation, Density Gradient
Chromatography, Gel
Cysteine - genetics
Disulfides - metabolism
env Gene Products, Human Immunodeficiency Virus
envelope protein
Furin
Gene Products, env - genetics
Gene Products, env - immunology
Gene Products, env - metabolism
glycoprotein gp120
glycoprotein gp140
glycoprotein gp41
Glycoproteins - genetics
Glycoproteins - immunology
Glycoproteins - metabolism
HIV Envelope Protein gp120 - genetics
HIV Envelope Protein gp120 - immunology
HIV Envelope Protein gp120 - metabolism
HIV Envelope Protein gp41 - genetics
HIV Envelope Protein gp41 - immunology
HIV Envelope Protein gp41 - metabolism
HIV-1 - isolation & purification
Human immunodeficiency virus 1
Humans
Molecular Sequence Data
Protein Processing, Post-Translational
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - immunology
Recombinant Fusion Proteins - metabolism
Subtilisins - metabolism
Sucrose
Vaccines and Antiviral Agents
Virion
Online AccessGet full text

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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
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.
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.
Author Aditi Master
James M. Binley
Francis Kajumo
John P. Moore
Rogier W. Sanders
Paul J. Maddon
William C. Olson
Deborah J. Anselma
Yong Guo
Brian Clas
Norbert Schuelke
AuthorAffiliation Aaron Diamond AIDS Research Center, The Rockefeller University, New York, New York 10016 1 ; Department of Human Retrovirology, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands 2 ; and Progenics Pharmaceuticals, Inc., Tarrytown, New York 10591 3
AuthorAffiliation_xml – name: Aaron Diamond AIDS Research Center, The Rockefeller University, New York, New York 10016 1 ; Department of Human Retrovirology, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands 2 ; and Progenics Pharmaceuticals, Inc., Tarrytown, New York 10591 3
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/10623724$$D View this record in MEDLINE/PubMed
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Corresponding author. Mailing address: Aaron Diamond AIDS Research Center, 455 First Ave., New York, NY 10016. Phone: (212) 725-0018. Fax: (212) 725-1126. E-mail for J. M. Binley: jbinley@adarc.org E-mail for J. P. Moore: jmoore@adarc.org.
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SSID ssj0014464
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Snippet Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
The few antibodies that can potently neutralize human immunodeficiency virus type 1 (HIV-1) recognize the limited number of envelope glycoprotein epitopes...
ABSTRACT The few antibodies that can potently neutralize human immunodeficiency virus type 1 (HIV-1) recognize the limited number of envelope glycoprotein...
SourceID pubmedcentral
proquest
crossref
pubmed
highwire
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 627
SubjectTerms AIDS/HIV
Amino Acid Sequence
Amino Acid Substitution
Antigens, Viral - genetics
Antigens, Viral - immunology
Antigens, Viral - metabolism
Cell Line, Transformed
Centrifugation, Density Gradient
Chromatography, Gel
Cysteine - genetics
Disulfides - metabolism
env Gene Products, Human Immunodeficiency Virus
envelope protein
Furin
Gene Products, env - genetics
Gene Products, env - immunology
Gene Products, env - metabolism
glycoprotein gp120
glycoprotein gp140
glycoprotein gp41
Glycoproteins - genetics
Glycoproteins - immunology
Glycoproteins - metabolism
HIV Envelope Protein gp120 - genetics
HIV Envelope Protein gp120 - immunology
HIV Envelope Protein gp120 - metabolism
HIV Envelope Protein gp41 - genetics
HIV Envelope Protein gp41 - immunology
HIV Envelope Protein gp41 - metabolism
HIV-1 - isolation & purification
Human immunodeficiency virus 1
Humans
Molecular Sequence Data
Protein Processing, Post-Translational
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - immunology
Recombinant Fusion Proteins - metabolism
Subtilisins - metabolism
Sucrose
Vaccines and Antiviral Agents
Virion
Title 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
URI http://jvi.asm.org/content/74/2/627.abstract
https://www.ncbi.nlm.nih.gov/pubmed/10623724
https://search.proquest.com/docview/17473025
https://search.proquest.com/docview/70816965
https://pubmed.ncbi.nlm.nih.gov/PMC111582
Volume 74
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