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M9650015.TXT
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1996-03-09
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Document 0015
DOCN M9650015
TI Expression of HIV-1 envelope glycoprotein alters cellular calmodulin.
DT 9605
AU Radding W; Pan ZQ; Hunter E; Johnston P; Williams JP; McDonald JM;
Department of Pathology, University of Alabama at Birmingham;
35294-0007, USA.
SO Biochem Biophys Res Commun. 1996 Jan 5;218(1):192-7. Unique Identifier :
AIDSLINE MED/96136299
AB 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.
DE Binding Sites Blotting, Western Calmodulin/BIOSYNTHESIS/*METABOLISM
Cell Line Gene Products, env/*BIOSYNTHESIS/METABOLISM Human
HIV-1/METABOLISM/*PHYSIOLOGY Microscopy, Confocal Protein Binding
Protein Precursors/*BIOSYNTHESIS/METABOLISM Recombinant
Proteins/BIOSYNTHESIS/METABOLISM Sequence Deletion Subcellular
Fractions/METABOLISM Support, U.S. Gov't, P.H.S. Transfection JOURNAL
ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).