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Inhibition of viral replication by monoclonal antibodies directed against human immunodeficiency virus gp120 (1992)
| Citations: | 3 - 0 self |
BibTeX
@MISC{Niedrig92inhibitionof,
author = {M. Niedrig and H. -p. Harthus and J. Hinkula and M. Brijker and H. Bickhard and G. Pauli and H. R. Gelderblom and B. Wahren},
title = {Inhibition of viral replication by monoclonal antibodies directed against human immunodeficiency virus gp120},
year = {1992}
}
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Abstract
Monoclonal antibodies (MAbs) were raised against the glycoprotein gp 120 of human immunodeficiency virus type 1 (strain HTLV-1IIB). The reactivity of five selected MAbs was characterized in several tests: ELISA, immunostaining of Western blots, immuno-fluorescence, immunoprecipitation, immunoelectron microscopy, alkaline phosphatase-anti-alkaline phos-phatase assay and neutralization. The binding region was delimited by sequential overlapping Escherichia coli fusion proteins of the gpl20 sequence between amino acids (aa) 49 and 280. In the ELISA, when using sequential overlapping 15 aa peptides, the binding epitopes were localized between aa 64 and 78 for three MAbs and between aa 114 and 123 for the fourth Mab. The fifth Mab showed multiple reactions with different peptides possibly indicating a reaction with a discon-tinuous epitope. In virus growth inhibition assays, all five MAbs inhibited the spread of HIV-1 infection in cell cultures after a single or repeated treatment at a concentration of 63 ~tg/ml of the purified MAbs. All MAbs showed low but significant neutralizing activity at concentrations of 100 pg/ml. The surface glycoprotein gp 120 of HIV (SU) is proteoly-tically processed by cellular proteases from the env precursor gpl60 (McCune et al., 1988). SU forms tri- or tetrameric virus envelope knobs non-covalently connect-ed by salt bonds to the viral transmembrane (TM; Leis et al., 1988) protein gp41 (Weiss et al., 1990). SU is the virus receptor for the cellular CD4 molecule present on the T helper subset of lymphocytes and antigen-presenting cells of the monocyte-macrophage lineage (Sattentau & Weiss, 1988). Gpl20 is a major target for immunological antiviral attack either by neutralizing antibodies or by cellular immune mechanisms (Javaherian et al., 1989;
Keyphrases
monoclonal antibody viral replication human immunodeficiency virus gp120 amino acid monocyte-macrophage lineage tetrameric virus envelope javaherian et al discon-tinuous epitope significant neutralizing activity western blot cellular protease binding epitope cellular cd4 molecule present alkaline phosphatase-anti-alkaline phos-phatase assay aa peptide helper subset antigen-presenting cell cellular immune mechanism viral transmembrane fifth mab immunoelectron microscopy protein gp41 env precursor gpl60 purified mabs hiv-1 infection gpl20 sequence virus receptor escherichia coli fusion protein pg ml major target different peptide surface glycoprotein fourth mab immunological antiviral attack cell culture sattentau wei tg ml several test human immunodeficiency virus type binding region virus growth inhibition assay multiple reaction salt bond
