Antibody responses raised against a conformational V3 loop peptide of HIV-1.

Abstract:

:The amino acid sequence of the principal neutralizing determinant (PND) of 224 cases of human immunodeficiency virus type 1 (HIV-1) was determined and the most frequently occurring sequence was used as a peptide antigen for studying virus-specific antibody responses. In our present study, a linear peptide of the most frequent PND was first synthesized and then oxidized to create a disulfide-bridged loop conformation. Then, in order to construct a macromolecular structure for the purpose of increasing antigenicity, the synthetic peptide was conjugated to a core peptide. We compared the immunogenicity of the disulfide-bridged loop PND peptide antigen (AG4) and the linear PND peptide antigen (AG5). After immunizing rabbits 5 and 6 times with both peptides, the results obtained using ELISA revealed that AG4 (conformational-loop type) was more capable of inducing a high titer of antigen-specific antibodies than was AG5 (linear type). Despite an amino acid sequence homology of 72%, a 1:8 dilution of serum raised against AG4 inhibited 81.9% of HIV-1IIIB-mediated cell fusion, suggesting that conformational V3 loop peptide is able to elicit an antibody response which is strongly HIV-1-specific.

journal_name

Microbiol Immunol

authors

Bukawa H,Fukushima J,Hamajima K,Kimura M,Tsuji T,Xin KQ,Okuda K

doi

10.1111/j.1348-0421.1995.tb02249.x

subject

Has Abstract

pub_date

1995-01-01 00:00:00

pages

607-14

issue

8

eissn

0385-5600

issn

1348-0421

journal_volume

39

pub_type

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