Expression of HIV-1 envelope glycoprotein alters cellular calmodulin.
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.
Radding
W
W
Department of Pathology, University of Alabama at Birmingham 35294-0007, USA.
Pan
Z Q
ZQ
Hunter
E
E
Johnston
P
P
Williams
J P
JP
McDonald
J M
JM
D001665:Binding Sites; D015153:Blotting, Western; D002147:Calmodulin / Q000096:biosynthesis / Q000378:metabolism*; D002460:Cell Line; D015686:Gene Products, env / Q000096:biosynthesis* / Q000378:metabolism; D019302:HIV Envelope Protein gp160; D015497:HIV-1 / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D018613:Microscopy, Confocal; D011485:Protein Binding; D011498:Protein Precursors / Q000096:biosynthesis* / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D017384:Sequence Deletion; D013347:Subcellular Fractions / Q000378:metabolism; D014162:Transfection
D002147:Calmodulin; D015686:Gene Products, env; D019302:HIV Envelope Protein gp160; D011498:Protein Precursors; D011994:Recombinant Proteins