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Human MoAbs produced from normal, HIV-1-negative donors and specific for glycoprotein gp120 of the HIV-1 envelope

Ohlin, M. LU ; Hinkula, J.; Broliden, P. A.; Grunow, R.; Borrebaeck, C. A K LU and Wahren, B. (1992) In Clinical and Experimental Immunology 89(2). p.290-295
Abstract

Human MoAbs ofIgM class were developed against three regions of the HIV-1 envelope. Uninfected donor lymphocytes were immunized in vitro with recombinant protein pB1. Four out of five antibodies were directed to different parts of the V3 region, which contains a major neutralizing site. Two out of these antibodies were directed to more than one amino acid sequence, indicating reactivity to discontinuous sites. Two of the human MoAbs inhibited viral spread between cells in tissue culture, interpreted as reactivities to conserved amino acid sequences exposed during viral maturation. No MoAb neutralized virus, which may be explained by the relatively low avidity of the antibodies. One MoAb was directed to a region containing amino acids... (More)

Human MoAbs ofIgM class were developed against three regions of the HIV-1 envelope. Uninfected donor lymphocytes were immunized in vitro with recombinant protein pB1. Four out of five antibodies were directed to different parts of the V3 region, which contains a major neutralizing site. Two out of these antibodies were directed to more than one amino acid sequence, indicating reactivity to discontinuous sites. Two of the human MoAbs inhibited viral spread between cells in tissue culture, interpreted as reactivities to conserved amino acid sequences exposed during viral maturation. No MoAb neutralized virus, which may be explained by the relatively low avidity of the antibodies. One MoAb was directed to a region containing amino acids participating in CD4 binding. This technique appears to allow formation of antibodies with fine specificities other than those obtained in infected hosts.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
gp120, HIV-1, human MoAbs, in vitro immunization, V3 region
in
Clinical and Experimental Immunology
volume
89
issue
2
pages
6 pages
publisher
British Society for Immunology
external identifiers
  • Scopus:0026719854
ISSN
0009-9104
DOI
10.1111/j.1365-2249.1992.tb06947.x
language
English
LU publication?
yes
id
8cb9961b-9950-4983-bc77-000bc2ae5076
date added to LUP
2016-04-20 16:11:04
date last changed
2016-09-20 03:24:20
@misc{8cb9961b-9950-4983-bc77-000bc2ae5076,
  abstract     = {<p>Human MoAbs ofIgM class were developed against three regions of the HIV-1 envelope. Uninfected donor lymphocytes were immunized in vitro with recombinant protein pB1. Four out of five antibodies were directed to different parts of the V3 region, which contains a major neutralizing site. Two out of these antibodies were directed to more than one amino acid sequence, indicating reactivity to discontinuous sites. Two of the human MoAbs inhibited viral spread between cells in tissue culture, interpreted as reactivities to conserved amino acid sequences exposed during viral maturation. No MoAb neutralized virus, which may be explained by the relatively low avidity of the antibodies. One MoAb was directed to a region containing amino acids participating in CD4 binding. This technique appears to allow formation of antibodies with fine specificities other than those obtained in infected hosts.</p>},
  author       = {Ohlin, M. and Hinkula, J. and Broliden, P. A. and Grunow, R. and Borrebaeck, C. A K and Wahren, B.},
  issn         = {0009-9104},
  keyword      = {gp120,HIV-1,human MoAbs,in vitro immunization,V3 region},
  language     = {eng},
  number       = {2},
  pages        = {290--295},
  publisher    = {ARRAY(0x87a4df8)},
  series       = {Clinical and Experimental Immunology},
  title        = {Human MoAbs produced from normal, HIV-1-negative donors and specific for glycoprotein gp120 of the HIV-1 envelope},
  url          = {http://dx.doi.org/10.1111/j.1365-2249.1992.tb06947.x},
  volume       = {89},
  year         = {1992},
}