Abstract
A full understanding of the structure-function relationship of the retroviral aspartic proteinase (PR) requires a consideration of the role of PR in the biology of the virus. Very little is known about the mechanisms involved in the maturation of the retroviral particle. Viral maturation undoubtedly is a complex process since several thousand copies of the individual components that comprise the virion are generated by the action of PR on the polyprotein precursors, and these components must be sorted and properly assembled to form the mature, infectious virion. Recent studies suggest that cleavage of HIV-1 Gag at its processing sites occurs in an ordered or sequential manner, and that this sequential processing is a regulated event. Taken together, these results support a model in which ordered proteolytic processing of the Gag precursor is an integral part of the regulation and control of virion maturation.
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Pettit, S.C., Sheng, N., Tritch, R., Erickson-Viitanen, S., Swanstrom, R. (1998). The Regulation of Sequential Processing of HIV-1 Gag by the Viral Protease. In: James, M.N.G. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 436. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5373-1_2
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