Second Conserved Domain of gp120 is Important for HIV Infectivity and Antibody Neutralization

Rabbit antisera were raised against three overlapping synthetic peptides with sequence homology to the second conserved domain of the external envelope glycoprotein (gp120) of the human immunodeficiency virus (HIV). All of the antisera immunoprecipitated the envelope glycoprotein. In particular, an...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1988-02, Vol.239 (4843), p.1021-1023
Main Authors: Ho, David D., Kaplan, Joan C., Rackauskas, Indre E., Gurney, Mark E.
Format: Article
Language:English
Subjects:
Acquired immune deficiency syndrome
Acquired Immunodeficiency Syndrome - immunology
AIDS
AIDS/HIV
Amino Acid Sequence
Amino acids
Antibodies
Antibodies, Viral - immunology
Antigens, Differentiation, T-Lymphocyte - immunology
Antiserum
Cell lines
Glucose-6-Phosphate Isomerase
Glycoproteins
Growth Substances
Hemocyanins - immunology
HIV
HIV (Viruses)
HIV - immunology
HIV - physiology
HIV Antibodies
HIV Envelope Protein gp120
HIV Seropositivity
Human immunodeficiency virus
Humans
Immune Sera - immunology
Immunity (Disease)
Immunization
Immunoglobulins
Immunosorbent Techniques
Lymphokines
Medical research
Molecular Sequence Data
Neutralization Tests
Protein research
Receptors, Antigen, T-Cell - immunology
Retroviridae Proteins - immunology
Retroviridae Proteins - physiology
Sequence homology
Sequence Homology, Nucleic Acid
T lymphocytes
T-Lymphocytes - immunology
T-Lymphocytes - microbiology
Vaccination
Vaccination & vaccines
Viral Envelope Proteins - immunology
Viral Envelope Proteins - physiology
Viruses
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Description
Summary:Rabbit antisera were raised against three overlapping synthetic peptides with sequence homology to the second conserved domain of the external envelope glycoprotein (gp120) of the human immunodeficiency virus (HIV). All of the antisera immunoprecipitated the envelope glycoprotein. In particular, an antiserum directed against amino acids 254 to 274 of env was efficient in neutralizing three different isolates of HIV in vitro, without affecting the binding of the virus to CD4-positive cells. Therefore, this conserved region of gp120 appears to be critical in a postbinding event during virus penetration and may represent a target for antibody neutralization of HIV. These findings may be applicable in the design of a vaccine for the acquired immunodeficiency syndrome.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2830667