期刊
ARCHIVES OF VIROLOGY
卷 147, 期 7, 页码 1349-1370出版社
SPRINGER-VERLAG WIEN
DOI: 10.1007/s00705-002-0813-7
关键词
-
类别
资金
- NCI NIH HHS [CA 75911, CA 82056] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA082056, R01CA075911] Funding Source: NIH RePORTER
The gamma2 human herpesvirus-8 (HHV-8) or Kaposi's sarcoma associated herpesvirus (KSHV) ORFs 22 and 47 are counterparts to glycoproteins gH and gL, respectively, that are conserved among the members of herpesviruses. To define HHV-8 gH and gL, rabbit polyclonal antibodies were raised against GST-gH and GST-gL fusion proteins. Anti-gL and anti-gH antibodies reacted with the surface of virus carrying BCBL-1 cells. Both antibodies immunoprecipitated the HHV-8 envelope associated 120 kDa and 41-42 kDa proteins. In transfected COS-1 cells, gH was expressed as an endo-H sensitive 110 kDa glycoprotein, which was absent on the surface of the cells. However, after co-transfection with gL, gH was detected as an endo-H resistant 120 kDa glycoprotein, and was expressed on the surface of the cells. Non-covalent complex formation between gH and gL was detected in the transfected COS-1 cells. Anti-gH and anti-gL antibodies neutralized HHV-8 infectivity in the absence of complement, individually and more efficiently together. However, virus binding to the target cells was not inhibited. These studies suggest that HHV-8 gL is required for gH processing and expression on the cell surface membranes, and gH/gL complex plays an important role in the post-binding step of HHV-8 infection.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据