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Research Article Free access | 10.1172/JCI117260

Temporal analysis of the antibody response to HIV envelope protein in HIV-infected laboratory workers.

S H Pincus, K G Messer, P L Nara, W A Blattner, G Colclough, and M Reitz

Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Disease, Hamilton, Montana 59840.

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Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Disease, Hamilton, Montana 59840.

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Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Disease, Hamilton, Montana 59840.

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Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Disease, Hamilton, Montana 59840.

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Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Disease, Hamilton, Montana 59840.

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Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Disease, Hamilton, Montana 59840.

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Published June 1, 1994 - More info

Published in Volume 93, Issue 6 on June 1, 1994
J Clin Invest. 1994;93(6):2505–2513. https://doi.org/10.1172/JCI117260.
© 1994 The American Society for Clinical Investigation
Published June 1, 1994 - Version history
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Abstract

Three laboratory workers have been infected with the IIIB strain of HIV; their antibody response to HIV has been studied in serial serum specimens. Because the infecting virus is known, the fine specificity of the antibody response was studied on the homologous strain of HIV. Anti-p17, anti-p24, anti-gp160, CD4/gp120 blocking and neutralizing antibodies developed in parallel. Epitope mapping of the anti-gp160 response indicated several regions that consistently induced an antibody response. Serum contained antibody which reacted with V3-specific peptides corresponding to the very tip of the loop and crossreactivity was seen with V3 loop peptides from other sequence divergent strains of HIV. Antibody to the V1 loop was produced at levels comparable with that seen for the V3-loop. Anti-V1 neutralized HIV with a titration curve equivalent to an anti-V3 monoclonal antibody. Because the infecting virus is known and serial reisolates have been obtained, we explored the relationship between production of antibody to a given epitope and mutation in the virus. The data suggest that an association exists, but do not clearly indicate that antibody drives the selection for mutant viruses. The findings presented here provide a fine specificity analysis of the evolution of the antibody response to HIV in greater detail than has previously been performed.

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