Proteolysis in the maturation of avian retroviruses does not require calcium.
After budding from the plasma membrane, retrovirus particles undergo a process of maturation, which includes changes in morphology caused by several proteolytic cleavages of the precursor of the internal structural proteins, products of the gag gene. Cleavage is mediated by the viral protease, PR. The fact that in most systems cleavage appears to occur only after assembly is complete, suggests that PR may become enzymatically active as a consequence of release of the virion from the cell. Using avian leukosis virus as a model system, we tested the hypothesis that leakage of calcium ions into newly budded virions plays a role in their maturation. We found that in both quail Qt35 cells and monkey COS-1 cells, maturation occurred normally in calcium-free medium and in the presence of EGTA. A calcium ionophore also did not affect maturation. We conclude that calcium influx does not act as a trigger for PR-mediated maturation.
Vogt
V M
VM
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853.
Burstein
H
H
Skalka
A M
AM
D001355:Alpharetrovirus / Q000254:growth & development* / Q000648:ultrastructure; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002460:Cell Line; D002522:Chlorocebus aethiops; D003370:Coturnix; D004533:Egtazic Acid / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism*; D015683:Gene Products, gag / Q000378:metabolism*; D066298:In Vitro Techniques; D011499:Protein Processing, Post-Translational; D014422:Turkeys
D015683:Gene Products, gag; D004533:Egtazic Acid; D010450:Endopeptidases; D002118:Calcium