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

Abstract:

: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.

journal_name

J Virol

journal_title

Journal of virology

authors

Faccini AM,Cairney M,Ashrafi GH,Finbow ME,Campo MS,Pitts JD

doi

10.1128/JVI.70.12.9041-9045.1996

subject

Has Abstract

pub_date

1996-12-01 00:00:00

pages

9041-5

issue

12

eissn

0022-538X

issn

1098-5514

journal_volume

70

pub_type

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