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Characterization of human monoclonal antibodies directed against the pp65 kD matrix antigen of human cytomegalovirus.

Ohlin, Mats LU orcid ; Sundqvist, Vivi Anne ; Gilliam, G ; Rudén, U. ; Gombert, F. ; Wahren, Britta and Borrebaeck, Carl LU (1991) In Clinical and Experimental Immunology 84. p.508-514
Abstract
Human monoclonal antibodies specific for human cytomegalovirus (CMV) antigens have been established using peripheral blood lymphocytes from a seropositive donor. Immortalization of antigen-specific B cells was achieved by Epstein-Barr virus transformation followed by somatic cell fusion of antigen-specific lymphoblastoid cells. Four clones producing high-affinity antibodies (0.2-7 × 109 M-1) specific for the viral matrix protein pp65 have been further characterized with respect to epitope specificity of secreted antibodies. The studied antigen represents a major protein produced by in vitro-cultivated virus, and is important in the scrodiagnosis of CMV infection. The human monoclonal antibodies recognized different epitopes. some of which... (More)
Human monoclonal antibodies specific for human cytomegalovirus (CMV) antigens have been established using peripheral blood lymphocytes from a seropositive donor. Immortalization of antigen-specific B cells was achieved by Epstein-Barr virus transformation followed by somatic cell fusion of antigen-specific lymphoblastoid cells. Four clones producing high-affinity antibodies (0.2-7 × 109 M-1) specific for the viral matrix protein pp65 have been further characterized with respect to epitope specificity of secreted antibodies. The studied antigen represents a major protein produced by in vitro-cultivated virus, and is important in the scrodiagnosis of CMV infection. The human monoclonal antibodies recognized different epitopes. some of which proved to be overlapping. The fine specificity of these antibodies was evaluated using synthetic peptides covering the sequence of pp65. The antibody MO58 recognized a linear epitope (residues 283-288) whereas antibody MO53 recognized a discontinuous epitope involving residues 208-216 and 280-285. Despite the close proximity of these epitopes, the antibodies did not compete with each other for the same binding site on intact antigen. (Less)
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author
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organization
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type
Contribution to journal
publication status
published
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in
Clinical and Experimental Immunology
volume
84
pages
508 - 514
publisher
British Society for Immunology
external identifiers
  • scopus:0025756091
ISSN
0009-9104
language
English
LU publication?
yes
id
9b677e2a-7483-41f8-821f-338a7faf8e7f
alternative location
https://ludwig.lub.lu.se/login?url=https://search.ebscohost.com/login.aspx?direct=true&AuthType=ip,uid&db=a9h&AN=16017622&site=eds-live&scope=site
date added to LUP
2022-11-30 08:57:03
date last changed
2022-12-01 04:23:58
@article{9b677e2a-7483-41f8-821f-338a7faf8e7f,
  abstract     = {{Human monoclonal antibodies specific for human cytomegalovirus (CMV) antigens have been established using peripheral blood lymphocytes from a seropositive donor. Immortalization of antigen-specific B cells was achieved by Epstein-Barr virus transformation followed by somatic cell fusion of antigen-specific lymphoblastoid cells. Four clones producing high-affinity antibodies (0.2-7 × 109 M-1) specific for the viral matrix protein pp65 have been further characterized with respect to epitope specificity of secreted antibodies. The studied antigen represents a major protein produced by in vitro-cultivated virus, and is important in the scrodiagnosis of CMV infection. The human monoclonal antibodies recognized different epitopes. some of which proved to be overlapping. The fine specificity of these antibodies was evaluated using synthetic peptides covering the sequence of pp65. The antibody MO58 recognized a linear epitope (residues 283-288) whereas antibody MO53 recognized a discontinuous epitope involving residues 208-216 and 280-285. Despite the close proximity of these epitopes, the antibodies did not compete with each other for the same binding site on intact antigen.}},
  author       = {{Ohlin, Mats and Sundqvist, Vivi Anne and Gilliam, G and Rudén, U. and Gombert, F. and Wahren, Britta and Borrebaeck, Carl}},
  issn         = {{0009-9104}},
  language     = {{eng}},
  pages        = {{508--514}},
  publisher    = {{British Society for Immunology}},
  series       = {{Clinical and Experimental Immunology}},
  title        = {{Characterization of human monoclonal antibodies directed against the pp65 kD matrix antigen of human cytomegalovirus.}},
  url          = {{https://ludwig.lub.lu.se/login?url=https://search.ebscohost.com/login.aspx?direct=true&AuthType=ip,uid&db=a9h&AN=16017622&site=eds-live&scope=site}},
  volume       = {{84}},
  year         = {{1991}},
}