The bovine papillomavirus type 4 E8 protein binds to ductin and causes loss of gap junctional intercellular communication in primary fibroblasts

被引:56
作者
Faccini, AM [1 ]
Cairney, M [1 ]
Ashrafi, GH [1 ]
Finbow, ME [1 ]
Campo, MS [1 ]
Pitts, JD [1 ]
机构
[1] BEATSON INST CANC RES,CRC,BEATSON LABS,GLASGOW G61 1BD,LANARK,SCOTLAND
关键词
D O I
10.1128/JVI.70.12.9041-9045.1996
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The E8 open reading frame of bovine papillomavirus type 4 encodes a small hydrophobic polypeptide which contributes to cell transformation by conferring anchorage-independent growth. Using an in vitro translation system, we show that the E8 polypeptide binds to ductin, the 16-kDa proteolipid that forms transmembrane channels in both gap junctions and vacuolar H+-ATPase, This association is not due to nonspecific hydrophobic interactions, PPA1, a Saccharomyces cerevisiae polypeptide homologous (with 25% identity) to ductin, does not complex with E8. Furthermore, E5B, structurally similar to E8 but with no transforming activity, does not form a complex with ductin, Primary bovine fibroblasts expressing E8 show a loss of gap junctional intercellular communication, and it is suggested that this results from the interaction between E8 and ductin.
引用
收藏
页码:9041 / 9045
页数:5
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