The picobirnavirus crystal structure provides functional insights into virion assembly and cell entry. Export

@article{citeulike:4449373, abstract = {Double-stranded (ds) RNA virus particles are organized around a central icosahedral core capsid made of 120 identical subunits. This core capsid is unable to invade cells from outside, and animal dsRNA viruses have acquired surrounding capsid layers that are used to deliver a transcriptionally active core particle across the membrane during cell entry. In contrast, dsRNA viruses infecting primitive eukaryotes have only a simple core capsid, and as a consequence are transmitted only vertically. Here, we report the 3.4 A X-ray structure of a picobirnavirus--an animal dsRNA virus associated with diarrhoea and gastroenteritis in humans. The structure shows a simple core capsid with a distinctive icosahedral arrangement, displaying 60 two-fold symmetric dimers of a coat protein (CP) with a new 3D-fold. We show that, as many non-enveloped animal viruses, CP undergoes an autoproteolytic cleavage, releasing a post-translationally modified peptide that remains associated with nucleic acid within the capsid. Our data also show that picobirnavirus particles are capable of disrupting biological membranes in vitro, indicating that its simple 120-subunits capsid has evolved animal cell invasion properties.}, author = {Duquerroy, St\'{e}phane and Da Costa, Bruno and Henry, C\'{e}line and Vigouroux, Armelle and Libersou, Sonia and Lepault, Jean and Navaza, Jorge and Delmas, Bernard and Rey, F\'{e}lix A.}, citeulike-article-id = {4449373}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/emboj.2009.109}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19407816}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19407816}, day = {3}, doi = {10.1038/emboj.2009.109}, issn = {1460-2075}, journal = {The EMBO journal}, keywords = {picobirnavirus, structures}, month = {June}, number = {11}, pages = {1655--1665}, posted-at = {2009-10-23 15:17:28}, priority = {2}, publisher = {Nature Publishing Group}, title = {The picobirnavirus crystal structure provides functional insights into virion assembly and cell entry.}, url = {http://dx.doi.org/10.1038/emboj.2009.109}, volume = {28}, year = {2009} }

TY - JOUR ID - citeulike:4449373 L3 - citeulike-article-id:4449373 N2 - Double-stranded (ds) RNA virus particles are organized around a central icosahedral core capsid made of 120 identical subunits. This core capsid is unable to invade cells from outside, and animal dsRNA viruses have acquired surrounding capsid layers that are used to deliver a transcriptionally active core particle across the membrane during cell entry. In contrast, dsRNA viruses infecting primitive eukaryotes have only a simple core capsid, and as a consequence are transmitted only vertically. Here, we report the 3.4 A X-ray structure of a picobirnavirus--an animal dsRNA virus associated with diarrhoea and gastroenteritis in humans. The structure shows a simple core capsid with a distinctive icosahedral arrangement, displaying 60 two-fold symmetric dimers of a coat protein (CP) with a new 3D-fold. We show that, as many non-enveloped animal viruses, CP undergoes an autoproteolytic cleavage, releasing a post-translationally modified peptide that remains associated with nucleic acid within the capsid. Our data also show that picobirnavirus particles are capable of disrupting biological membranes in vitro, indicating that its simple 120-subunits capsid has evolved animal cell invasion properties. IS - 11 JF - The EMBO journal SN - 1460-2075 EP - 1665 TI - The picobirnavirus crystal structure provides functional insights into virion assembly and cell entry. PB - Nature Publishing Group VL - 28 SP - 1655 KW - picobirnavirus KW - structures AU - Duquerroy, Stéphane AU - Da Costa, Bruno AU - Henry, Céline AU - Vigouroux, Armelle AU - Libersou, Sonia AU - Lepault, Jean AU - Navaza, Jorge AU - Delmas, Bernard AU - Rey, Félix PY - 2009/06/03/ UR - http://dx.doi.org/10.1038/emboj.2009.109 ER -