Human monoclonal antibodies against a recombinant HIV envelope-antigen produced by primary in vitro immunization. Characterization and epitope mapping.
Ohlin, Mats LU
; Broliden, PA
; Danielsson, Lena
LU
; Wahren, Britta
; Rosen, J
; Jondal, M
and Borrebaeck, Carl
LU
(1989)
In Immunology
68(3).
p.325-331
- Abstract
- Peripheral blood lymphocytes from healthy, HIV sero-negative blood donors have been in vitro immunized using penv9, a recombinant fragment of the envelope of HIV-1. This primary in vitro immunization followed by Epstein-Barr virus (EBV) transformation and somatic cell fusion subsequently gave rise to several specific anti-penv9 monoclonal antibodies (MO28, MO30 and MO43) of μ isotype. The hybridomas have been kept in culture for over 6 months and the antibody productivity for MO30 was measured to 18 μg × (24 hr × 106 cells)-1. The fine specificity of the antibodies was mapped by a peptide inhibition enzyme immunoassay, using overlapping synthetic pentadeca peptides covering the whole penv9. These human monoclonal antibodies exhibited a... (More)
- Peripheral blood lymphocytes from healthy, HIV sero-negative blood donors have been in vitro immunized using penv9, a recombinant fragment of the envelope of HIV-1. This primary in vitro immunization followed by Epstein-Barr virus (EBV) transformation and somatic cell fusion subsequently gave rise to several specific anti-penv9 monoclonal antibodies (MO28, MO30 and MO43) of μ isotype. The hybridomas have been kept in culture for over 6 months and the antibody productivity for MO30 was measured to 18 μg × (24 hr × 106 cells)-1. The fine specificity of the antibodies was mapped by a peptide inhibition enzyme immunoassay, using overlapping synthetic pentadeca peptides covering the whole penv9. These human monoclonal antibodies exhibited a similar epitope specificity directed against a non-sequential determinant, including the amino acids 632–646, 677–681 and 687–691. This specificity is very rarely found in immune sera from sero-positive patients and presently not reported in human monoclonal antibodies derived from in vivo immunized individuals, indicating that different antibody specificities can be obtained by the in vitro immunization technology. These human monoclonal antibodies did not neutralize HIV. The results presented here demonstrate the feasability of generating human monoclonal antibodies against HIV by primary in vitro immunizations, thereby avoiding the use of lymphocytes derived from infected patients when human monoclonal antibodies for therapeutic purposes are to be produced. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/bc8cf46c-7a31-4278-9eeb-e6f332934fc4
- author
- Ohlin, Mats
LU
; Broliden, PA
; Danielsson, Lena
LU
; Wahren, Britta
; Rosen, J
; Jondal, M
and Borrebaeck, Carl
LU
- organization
- publishing date
- 1989
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Immunology
- volume
- 68
- issue
- 3
- pages
- 325 - 331
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0024414250
- ISSN
- 0019-2805
- language
- English
- LU publication?
- yes
- id
- bc8cf46c-7a31-4278-9eeb-e6f332934fc4
- alternative location
- https://ludwig.lub.lu.se/login?url=https://search.ebscohost.com/login.aspx?direct=true&AuthType=ip,uid&db=a9h&AN=13354928&site=eds-live&scope=site
- date added to LUP
- 2022-11-30 08:52:48
- date last changed
- 2024-01-03 00:34:38
@article{bc8cf46c-7a31-4278-9eeb-e6f332934fc4,
abstract = {{Peripheral blood lymphocytes from healthy, HIV sero-negative blood donors have been in vitro immunized using penv9, a recombinant fragment of the envelope of HIV-1. This primary in vitro immunization followed by Epstein-Barr virus (EBV) transformation and somatic cell fusion subsequently gave rise to several specific anti-penv9 monoclonal antibodies (MO28, MO30 and MO43) of μ isotype. The hybridomas have been kept in culture for over 6 months and the antibody productivity for MO30 was measured to 18 μg × (24 hr × 106 cells)-1. The fine specificity of the antibodies was mapped by a peptide inhibition enzyme immunoassay, using overlapping synthetic pentadeca peptides covering the whole penv9. These human monoclonal antibodies exhibited a similar epitope specificity directed against a non-sequential determinant, including the amino acids 632–646, 677–681 and 687–691. This specificity is very rarely found in immune sera from sero-positive patients and presently not reported in human monoclonal antibodies derived from in vivo immunized individuals, indicating that different antibody specificities can be obtained by the in vitro immunization technology. These human monoclonal antibodies did not neutralize HIV. The results presented here demonstrate the feasability of generating human monoclonal antibodies against HIV by primary in vitro immunizations, thereby avoiding the use of lymphocytes derived from infected patients when human monoclonal antibodies for therapeutic purposes are to be produced.}},
author = {{Ohlin, Mats and Broliden, PA and Danielsson, Lena and Wahren, Britta and Rosen, J and Jondal, M and Borrebaeck, Carl}},
issn = {{0019-2805}},
language = {{eng}},
number = {{3}},
pages = {{325--331}},
publisher = {{Wiley-Blackwell}},
series = {{Immunology}},
title = {{Human monoclonal antibodies against a recombinant HIV envelope-antigen produced by primary in vitro immunization. Characterization and epitope mapping.}},
url = {{https://ludwig.lub.lu.se/login?url=https://search.ebscohost.com/login.aspx?direct=true&AuthType=ip,uid&db=a9h&AN=13354928&site=eds-live&scope=site}},
volume = {{68}},
year = {{1989}},
}