Expression of HIV-1 envelope glycoprotein alters cellular calmodulin.

Abstract:

:Removal of parts of a known calmodulin binding site at the C-terminus of HIV-1 envelope glycoprotein, gp160, can result in diminished infectivity. We investigated whether expression of full length gp160 would result in changes in intracellular calmodulin compared to expression of gp160 truncated to remove both known calmodulin binding sites. Both Western and Northern blots demonstrated that expression of gp160 led to increased calmodulin when compared to expression of truncated gp160. The induced calmodulin was associated preferentially with a particulate subcellular fraction. Confocal immunomicroscopy confirmed the increase in calmodulin and also showed that there was enhanced colocalization of calmodulin with gp160. Understanding of the role of calmodulin in the viral life-cycle may lead to new therapeutics.

authors

Radding W,Pan ZQ,Hunter E,Johnston P,Williams JP,McDonald JM

doi

10.1006/bbrc.1996.0034

subject

Has Abstract

pub_date

1996-01-05 00:00:00

pages

192-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X96900340

journal_volume

218

pub_type

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