Expression of HIV-1 envelope glycoprotein alters cellular calmodulin

Wilson Radding, Zhiqi Q. Pan, Eric Hunter, Patrick Johnston, John P. Williams, Jay M. McDonald

Research output: Contribution to journalArticle

22 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)192-197
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume218
Issue number1
DOIs
StatePublished - Jan 5 1996

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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