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Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase

Title data

Wöhrl, Birgitta M.:
Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase.
In: Viruses. Vol. 11 (2019) Issue 7 . - No. 598.
ISSN 1999-4915
DOI: https://doi.org/10.3390/v11070598

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: foamy virus; protease; reverse transcriptase; RNase H; reverse transcription; antiviral drugs; resistance
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Lehrstuhl Biopolymere - Apl. Prof. Dr. Birgitta Wöhrl
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 05 Jul 2019 13:34
Last Modified: 05 Jul 2019 13:34
URI: https://eref.uni-bayreuth.de/id/eprint/49861