Journal article

Virion associated proteins of equine rhinitis B virus 1 (ERBV1): The non-structural protein 3C(pro) co-purifies with virions

Wesley D Black, Carol A Hartley, Nino P Ficorilli, Michael J Studdert

VIRUS RESEARCH | ELSEVIER SCIENCE BV | Published : 2009

Abstract

Equine rhinitis B virus (ERBV), genus Erbovirus, is most closely related to the Cardiovirus genus in the family Picornaviridae. The structural proteins (VP1-4) of erboviruses are not well described, but are predicted by sequence to be 35, 29, 26 and 7 kDa. Methods for the purification of cardioviruses (polyethylene glycol, trypsin treatment) were used to characterise the structural proteins of ERBV1. Only one of the virus proteins detected was an expected molecular mass, and this 26 kDa protein was identified as VP3 by N-terminal amino acid sequencing. N-terminal sequencing of the 56 and a 29 kDa protein identified sequences consistent with VP2 and VP1 respectively, despite these being 27 kD..

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Grants

Funding Acknowledgements

We thank John A. Marshall, Victorian infectious Diseases Reference Laboratory, and Liliana Tartaczuch, School of Veterinary Science, University of Melbourne, for electron micrography. We thank Cynthia Brown for technical assistance. W.D.B. was the recipient of an Australian Postgraduate Award (industry) with Racing Victoria the industry partner for the award. Other financial support was from Racing Victoria and the CEV Special Virology Fund.