f Proteolytic cleavage of microtubule-associated proteins by retroviral proteinases
- Authors: Margareta Wallin, Johanna Deinum, Laura Goobar, U. Helena Danielson
- First Published Online: 01 September 1990, Journal of General Virology 71: 1985-1991, doi: 10.1099/0022-1317-71-9-1985
- Subject: Animal
- Issue Published:
Aspartic proteinases from human immunodeficiency virus type 1 (HIV-1) and avian myeloblastosis virus (AMV) were found to interfere with microtubule assembly. Preincubation of the proteinases with purified brain microtubule proteins (tubulin and microtubule-associated proteins) at low ionic strength (pH 6.8), completely inhibited microtubule assembly. Analysis of microtubule proteins after incubation with proteinase showed no effect on tubulin but extensive cleavage of the microtubule-associated proteins 1 and 2 was observed. The digestion by the two proteinases differed. In the presence of HIV-1 proteinase, a fragment with an M r of approximately 300000 appeared, as well as at least three other new fragments, with M r values of 188000, 124000 and 73000. In the presence of AMV proteinase, the microtubule-associated proteins were extensively digested to many small fragments. The extending microtubule-associated proteins normally seen by electron microscopy on the microtubule surface disappeared after treatment with AMV proteinase. Our results show that retroviral proteinases are not restricted to cleavage of viral polyproteins in vitro. It is suggested that proteolysis of microtubular proteins by viral proteinases is an important step in viral pathogenicity and that it may be part of a mechanism causing degenerative effects in infected cells.
© Society for General Microbiology 1990 | Published by the Microbiology Society
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