Science. 1988 Feb 26;239(4843):1021-3. Unique Identifier : AIDSLINE
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.
Acquired Immunodeficiency Syndrome/IMMUNOLOGY Amino Acid Sequence
Antibodies, Viral/IMMUNOLOGY Antigens, Differentiation,
T-Lymphocyte/IMMUNOLOGY Growth Substances Hemocyanin/IMMUNOLOGY Human
HIV/*IMMUNOLOGY/PHYSIOLOGY HIV Seropositivity Immune Sera/IMMUNOLOGY
Immunization Immunosorbent Techniques Lymphokines Molecular Sequence
Data Neutralization Tests Receptors, Antigen, T-Cell/IMMUNOLOGY
Retroviridae Proteins/*IMMUNOLOGY/PHYSIOLOGY Sequence Homology, Nucleic
Acid Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S.
T-Lymphocytes/IMMUNOLOGY/MICROBIOLOGY Viral Envelope
Proteins/*IMMUNOLOGY/PHYSIOLOGY JOURNAL ARTICLE