Open AccessPurification of Papillomavirus Structural Polypeptides from Papillomas by Immunoaffinity Chromatography
Author(s) -
Yasumitsu Nakai,
Wayne D. Lancaster,
A. Bennett Jenson
Publication year - 1987
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/0022-1317-68-7-1891
Subject(s) - bovine papillomavirus , capsid , monoclonal antibody , biology , epitope , virology , affinity chromatography , antibody , antigen , microbiology and biotechnology , virus , blot , human papillomavirus , biochemistry , genome , immunology , enzyme , gene , medicine
A broadly cross-reactive monoclonal antibody directed against papillomavirus, coupled to immunoaffinity columns, was used to isolate bovine papillomavirus type 1 (BPV-1) and human papillomavirus type 1 (HPV-1) structural polypeptides from homogenates of productively infected cells. One of the polypeptides isolated from bovine fibropapillomas appeared to be the BPV-1 major capsid protein since it had a mol. wt. of 54K and was reactive by Western blots with papillomavirus genus- and BPV-1 type-specific rabbit antibodies as well as monoclonal antibodies cross-reactive with BPV-1/BPV-2 and BPV-1/deer PV. A polypeptide from human plantar warts similarly appeared to be the major capsid component since it also had a mass of 54K to 55K and reacted with papillomavirus genus- and HPV type-specific rabbit antibodies. By using this technique structural viral polypeptides from papillomavirus-induced lesions containing readily detectable viral structural antigens but relatively few virus particles, such as seen with mucosotropic HPVs can now be isolated for mapping of virus-specific epitopes.