TY - JOUR

T1 - Autologous antibody response against the principal neutralizing domain of human immunodeficiency virus type 1 isolated from infected humans

AU - Holmbäck, K

AU - Kusk, P

AU - Hulgaard, E F

AU - Bugge, T H

AU - Scheibel, E

AU - Lindhardt, B O

PY - 1993/3

Y1 - 1993/3

N2 - High titers of neutralizing antibodies in human immunodeficiency virus type 1 (HIV-1) infection are directed primarily against the third hypervariable domain (V3) of the virion envelope glycoprotein gp120. This region has been designated the principal neutralizing domain of HIV-1. Because the frequency and significance of autologous V3 antibodies in natural infection are not fully clarified, we have cloned, sequenced, and expressed the V3 domain from virus of HIV-1-infected patients to test the autologous and heterologous V3 antibody response. The resulting recombinant Escherichia coli V3 fusion proteins reacted strongly with both autologous and heterologous patient antibodies in Western blots. Thirty-one different V3 fragments were cloned from 24 hemophiliac patients with different immunological and clinical statuses. Antibody reactivity against the autologous V3 fusion proteins was detected in all serum samples except one; moreover, all serum samples contained antibody reactivity against a vast majority of heterologous fusion proteins despite significant amino acid variability in V3. The results suggest that V3 antibodies are highly prevalent; further, we find no association between the stage of the HIV-1 infection and the presence of V3 antibodies.

AB - High titers of neutralizing antibodies in human immunodeficiency virus type 1 (HIV-1) infection are directed primarily against the third hypervariable domain (V3) of the virion envelope glycoprotein gp120. This region has been designated the principal neutralizing domain of HIV-1. Because the frequency and significance of autologous V3 antibodies in natural infection are not fully clarified, we have cloned, sequenced, and expressed the V3 domain from virus of HIV-1-infected patients to test the autologous and heterologous V3 antibody response. The resulting recombinant Escherichia coli V3 fusion proteins reacted strongly with both autologous and heterologous patient antibodies in Western blots. Thirty-one different V3 fragments were cloned from 24 hemophiliac patients with different immunological and clinical statuses. Antibody reactivity against the autologous V3 fusion proteins was detected in all serum samples except one; moreover, all serum samples contained antibody reactivity against a vast majority of heterologous fusion proteins despite significant amino acid variability in V3. The results suggest that V3 antibodies are highly prevalent; further, we find no association between the stage of the HIV-1 infection and the presence of V3 antibodies.

KW - Amino Acid Sequence

KW - Antibodies, Heterophile

KW - Base Sequence

KW - Cloning, Molecular

KW - Cross Reactions

KW - Genetic Variation

KW - HIV Antibodies/blood

KW - HIV Envelope Protein gp120/biosynthesis

KW - HIV Infections/immunology

KW - HIV-1/immunology

KW - Hemophilia A/complications

KW - Humans

KW - Molecular Sequence Data

KW - Oligodeoxyribonucleotides

KW - Polymerase Chain Reaction

KW - Recombinant Proteins/biosynthesis

KW - Sequence Alignment

KW - Sequence Analysis, DNA

M3 - Journal article

C2 - 8437232

VL - 67

SP - 1612

EP - 1619

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 3

ER -