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Open AccessReview

Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase

Lehrstuhl Biopolymere, Universität Bayreuth, D-95440 Bayreuth, Germany
Viruses 2019, 11(7), 598; https://doi.org/10.3390/v11070598
Received: 12 June 2019 / Revised: 28 June 2019 / Accepted: 29 June 2019 / Published: 2 July 2019
(This article belongs to the Special Issue Spumaretroviruses)
Reverse transcription describes the process of the transformation of single-stranded RNA into double-stranded DNA via an RNA/DNA duplex intermediate, and is catalyzed by the viral enzyme reverse transcriptase (RT). This event is a pivotal step in the life cycle of all retroviruses. In contrast to orthoretroviruses, the domain structure of the mature RT of foamy viruses is different, i.e., it harbors the protease (PR) domain at its N-terminus, thus being a PR-RT. This structural feature has consequences on PR activation, since the enzyme is monomeric in solution and retroviral PRs are only active as dimers. This review focuses on the structural and functional aspects of simian and prototype foamy virus reverse transcription and reverse transcriptase, as well as special features of reverse transcription that deviate from orthoretroviral processes, e.g., PR activation. View Full-Text
Keywords: foamy virus; protease; reverse transcriptase; RNase H; reverse transcription; antiviral drugs; resistance foamy virus; protease; reverse transcriptase; RNase H; reverse transcription; antiviral drugs; resistance
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MDPI and ACS Style

Wöhrl, B.M. Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase. Viruses 2019, 11, 598.

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