JVI Accepts, published online ahead of print on 28 October 2009

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J. Virol. doi:10.1128/JVI.01347-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The ssDNA Genome of Novel Archaeal Virus HRPV-1 Is Enclosed in the Envelope Decorated with Glycoprotein Spikes

Maija K. Pietilä, Simonas Laurinaviius, Jukka Sund, Elina Roine, and Dennis H. Bamford^*

Institute of Biotechnology and Department of Biological and Environmental Sciences, University of Helsinki, P.O. Box 56, Viikinkaari 5, 00014 Helsinki, Finland; and Institute of Biomedicine and Department of Biochemistry and Developmental Biology, University of Helsinki, P.O. Box 63, Haartmaninkatu 8, 00014 Helsinki, Finland

^* To whom correspondence should be addressed. Email: dennis.bamford{at}helsinki.fi.

Only a few archaeal viruses have been subjected to detailed structural analyses. Major obstacles have been the extreme conditions such as high salinity or temperature needed for the propagation of such viruses. In addition, unusual morphotypes of many archaeal viruses have made it difficult to obtain further information on virion architectures. Here we used controlled virion dissociation to reveal the structural organization of HRPV-1 (Halorubrum pleomorphic virus 1) infecting an extremely halophilic archaeal host. The single-stranded DNA genome is enclosed in a pleomorphic membrane vesicle without detected nucleoproteins. VP4, the larger major structural protein of HRPV-1, forms glycosylated spikes on the virion surface and VP3, the smaller major structural protein, resides on the inner surface of the membrane vesicle. Together these proteins organize the structure of the membrane vesicle. Quantitative lipid comparison of HRPV-1 and its host Halorubrum sp. revealed that HRPV-1 acquires lipids non-selectively from the host cell membrane, which is typical of pleomorphic enveloped viruses.