Direct interaction between human cytomegalovirus glycoprotein B and cellular annexin II.

Abstract:

:Cellular annexin II has been shown to specifically bind human cytomegalovirus (HCMV) and be a component of highly purified virions. In this report, we characterize the interaction of annexin II with HCMV. We found that the binding of annexin II to the HCMV envelope occurs partially through the calcium-dependent phospholipid-binding ability of annexin II since some annexin II was dissociated from virions with chelating agents. However, a substantial proportion of virion-associated annexin II was resistant to chelation, which suggested a calcium-independent interaction between annexin II and an HCMV envelope component. The search for a nonphospholipid component to account for this binding led to the discovery that HCMV glycoprotein B (gpUL55) (gB) can physically interact with annexin II. We present three lines of evidence to support the conclusion that HCMV gB can bind host cell annexin II.

journal_name

J Virol

journal_title

Journal of virology

authors

Pietropaolo RL,Compton T

doi

10.1128/JVI.71.12.9803-9807.1997

subject

Has Abstract

pub_date

1997-12-01 00:00:00

pages

9803-7

issue

12

eissn

0022-538X

issn

1098-5514

journal_volume

71

pub_type

杂志文章