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

@article{citeulike:6055154, abstract = {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.}, author = {Pietil\"{a}, Maija K. and Laurinavicius, Simonas and Sund, Jukka and Roine, Elina and Bamford, Dennis H.}, citeulike-article-id = {6055154}, citeulike-linkout-0 = {http://dx.doi.org/10.1128/JVI.01347-09}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19864380}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19864380}, day = {28}, doi = {10.1128/JVI.01347-09}, issn = {1098-5514}, journal = {Journal of virology}, keywords = {archaea, envelope, structure, virus}, month = {October}, posted-at = {2009-11-02 04:16:53}, priority = {2}, title = {The ssDNA Genome of Novel Archaeal Virus HRPV-1 Is Enclosed in the Envelope Decorated with Glycoprotein Spikes.}, url = {http://dx.doi.org/10.1128/JVI.01347-09}, year = {2009} }

TY - JOUR ID - citeulike:6055154 L3 - citeulike-article-id:6055154 N2 - 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. JF - Journal of virology SN - 1098-5514 TI - The ssDNA Genome of Novel Archaeal Virus HRPV-1 Is Enclosed in the Envelope Decorated with Glycoprotein Spikes. KW - archaea KW - envelope KW - structure KW - virus AU - Pietilä, Maija AU - Laurinavicius, Simonas AU - Sund, Jukka AU - Roine, Elina AU - Bamford, Dennis PY - 2009/10/28/ UR - http://dx.doi.org/10.1128/JVI.01347-09 ER -