J Gen Virol
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J Gen Virol 84 (2003), 215-225; DOI 10.1099/vir.0.18670-0

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© 2003 Society for General Microbiology

Rabbit endogenous retrovirus-H encodes a functional protease

Cécile Voisset1, Richard E. Myers1, Alex Carne2,{dagger}, Paul Kellam1 and David J. Griffiths1

1 Wohl Virion Centre, Windeyer Institute of Medical Sciences, University College London, 46 Cleveland Street, London W1T 4JF, UK
2 Institute of Cancer Research, Chester Beatty Laboratories, London, UK

Correspondence
David Griffiths
d.j.griffiths{at}ucl.ac.uk

Recent studies have revealed that ‘human retrovirus-5’ sequences found in human samples belong to a rabbit endogenous retrovirus family named RERV-H. A part of the gag–pro region of the RERV-H genome was amplified by PCR from DNA in human samples and several forms of RERV-H protease were expressed in bacteria. The RERV-H protease was able to cleave itself from a precursor protein and was also able to cleave the RERV-H Gag polyprotein precursor in vitro whereas a form of the protease with a mutation engineered into the active site was inactive. Potential N- and C-terminal autocleavage sites were characterized. The RERV-H protease was sensitive to pepstatin A, showing it to be an aspartic protease. Moreover, it was strongly inhibited by PYVPheStaAMT, a pseudopeptide inhibitor specific for Mason–Pfizer monkey virus and avian myeloblastosis-associated virus. A structural model of the RERV-H protease was constructed that, together with the activity data, confirms that this is a retroviral aspartic protease.

{dagger}Present address: Proteomika, Parc Científic de Barcelona, 08028 Barcelona, Spain.

The sequence of the RERV-H PR shown in Fig. 1(a) has been deposited in GenBank under accession no. AF515800.




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