Purification of papillomavirus structural polypeptides from papillomas by immunoaffinity chromatography.
Purification of papillomavirus structural polypeptides from papillomas by immunoaffinity chromatography.
复制标题
通过免疫亲和层析从乳头状瘤中纯化乳头状瘤病毒结构多肽。
DOI：
10.1099/0022-1317-68-7-1891
复制
发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Jenson,AB
中科院分区：
文献类型：
--
作者：
Nakai,Y;Lancaster,WD;Jenson,AB
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-l/BPV-2 and BPV-l/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 HP Vs can now be isolated for mapping of virus-specific epitopes.
