Prokaryotic expression of a large fragment of the most antigenic cytomegalovirus DNA-binding protein (ppUL44) and its reactivity with human antibodies

We isolated and characterized from a λgt11 expression library clones expressing portions of human cytomegalovirus (HCMV)-p52. This non-structural viral protein is encoded by UL44 and is known to be one of the best IgM reactive antigens. The reactivity of these clones was studied with human antibody...

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Veröffentlicht in:Journal of virological methods 1994, Vol.46 (1), p.39-50
Hauptverfasser: Ripalti, A., Monte, P.Dal, Boccuni, M.C., Campanini, F., Lazzarotto, T., Campisi, B., Ruan, Q., Landini, M.P.
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Sprache:eng
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Zusammenfassung:We isolated and characterized from a λgt11 expression library clones expressing portions of human cytomegalovirus (HCMV)-p52. This non-structural viral protein is encoded by UL44 and is known to be one of the best IgM reactive antigens. The reactivity of these clones was studied with human antibody and the gene fragment coding for the most immune-reactive portion of p52 (aa 202–434) was cloned in a prokaryotic expression vector, pROS, which overexpresses the antigen as a fusion protein to a truncated molecule of β-galactosidase.
ISSN:0166-0934
1879-0984
DOI:10.1016/0166-0934(94)90015-9