Characterization of human monoclonal antibodies directed against the pp65 kD matrix antigen of human cytomegalovirus.
(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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https://lup.lub.lu.se/record/9b677e2a-7483-41f8-821f-338a7faf8e7f
- author
- Ohlin, Mats LU ; Sundqvist, Vivi Anne ; Gilliam, G ; Rudén, U. ; Gombert, F. ; Wahren, Britta and Borrebaeck, Carl LU
- organization
- publishing date
- 1991
- type
- Contribution to journal
- publication status
- published
- subject
- 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
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- 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
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- 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}}, }