The RNAs and Proteins of dsRNA Viruses: Edited by Peter. P. C. Mertens and Dennis H. Bamford The dsRNA segments and proteins of simian rotavirus A / SA11 (genus Rotavirus: family Reoviridae) : Structural studies (17, 31, 37, 72, 73, 88, 89): last updated April 2003, references in [square brackets] Genome Segment † Size [bp] 1 (3302) 2 (2690) 3 (2591) ORFs 183282 172659 502554 10 2337 4 (2362) Gene Product(s) (': Protein Function) VP1 (Pol) VP2 (T1) VP3 (Cap) VP4 Protein Size aa (Da) 1088 (125005) 881 (102431) Location in Virus Particle Inner capsid, 5-fold axis Inner capsid 835 (98120) Inner capsid, 5-fold axis 776 (86782) Outer capsid spike - VP5* 529 247-776 (60000) - VP8* 247 1-247 (28000) Copy Number/ Particle 12 120 12 Cognate Proteins‡ Orthoreovirus 3(Pol) Orbivirus VP 1(Pol) Coltivirus VP1(Pol) Cypovirus Pol Orbivirus: VP3 Orthoreovirus: 1 Orbivirus: VP4 Orthoreovirus: 2 GenBank Accession Number (s) X16830 [56] RNA-dependent RNA polymerase [87]. Part of minimal replication complex [63,87], Virus specific 3’-mRNA binding [61,62] Part of virion transcription complex with VP3 [11,73] X16831 [56] Inner capsid structural protein [8]. Non-specific ss & dsRNA-binding activity [10] Myristoylated [15]. Cleaved [23,86]. Part of minimal replication complex [63]. Leucine zipper [56]. Interacts with VP5 [7]. X16062 [44] X16387 [56] 120 D16346 [77] X14204 [55] 1 Functions and Properties Guanylyltransferase [45,68]. Methyltransferase [13]. Basic Protein [44,56]. Part of virion transcription complex with VP1 [11,73]. Non-specific ssRNA binding [62]. VP4 Dimers form outer capsid spike [3]. Interacts with VP6 [89]. Virus infectivity enhanced by trypsin cleavage of VP4 into VP5* and VP8* [22,46]. Hemagglutinin [26,38]. Cell attachment protein [47,75,85]. P-type neutralization antigen [32,58]. VP5* permeabilizes membranes [16]. Crystal structure of VP8 fragment (galectin fold) [19]. TRAF2 signaling [43]. Protection [33]. The RNAs and Proteins of dsRNA Viruses: Edited by Peter. P. C. Mertens and Dennis H. Bamford 5 (1611) 311515 NSP1 495 (58654) L18944 [35] Nonstructural 0 X14914 [57] L15384 [48] 6 (1356) 241214 VP6 (T13) 397 (4816) Middle capsid 780 Orbivirus: VP7 L33365 [48] M27824 [76] 7 (1105) 26-970 NSP3 315 (34600) Nonstructural 0 - M87502 [51] 8 (1059) 47-997 NSP2 (VIP) 317 (36700) Nonstructural 0 Orbivirus: NS2 Orthoreovirus: NS L04531 [64] 9 (1062) 491026 VP7 326 [7368) Outer capsid glycoprotein 780 - K02028 [4] 10 (751) 41-569 NSP4 175 (20290) Nonstructural 0 - AF087678 [9] 2 Associates with cytoskeleton [34]. Extensive sequence diversity between strains [20,42,57]. Two conserved cysteine-rich zinc-finger motifs [57,60]. Virus specific 5’-mRNA binding [34,62]. Interacts with host IFN regulatory factor 3 [29]. Major virion protein [49,72]. Middle capsid structural protein [72]. Homotrimeric 4o structure [72]. Subgroup antigen [30,39]. Myristoylated [15]. Protection (? Mechanism) [11,84]. Crystal structure [50]. Hydrophobic [48,76]. Homodimer [51,66]. Virus-specific 3’- mRNA binding [69,70]. Binds eIF4G1 and circularizes mRNA on initiation complex [67]. Involved in translational regulation and host shut-off [14,59,82]. Crystal structure: NSP3 NH3 fragment with 3’- viral RNA [17] and NSP3 COOH fragment with eIF4G fragment [31]. Non-specific ssRNA-binding [41,62] Accumulates in viroplasm [65] Involved in viroplasm formation with NSP5 [25] NTPase activity [79] Helix destabilization activity [78] Functional octamer [79,80] Binds NSP5 and VP1 [1, 40] Regulates NSP5 autophosphorylation [1] Crystal structure (HIT-like fold) [37] Outer capsid structural glycoprotein [21,49]. G-type neutralization antigen [32]. N-linked high mannose glycosylation and trimming [21]. RER transmembrane protein, cleaved signal sequence [22]. Ca2+ binding [18]. Protection [33]. Enterotoxin [6]. Receptor for budding of double-layer particle through ER membrane [5, 53]. RER transmembrane glycoprotein [22]. Ca++/ Sr++ binding site [36]. N-linked high mannose glycosylation [21]. Protection [24]. Host cell [Ca2+]i mobilization [81]. The RNAs and Proteins of dsRNA Viruses: Edited by Peter. P. C. Mertens and Dennis H. Bamford 22-615 NSP5 11 (667) 198 (21725) Nonstructural 0 X07831 - [54] M28347 [83] 80-355 NSP6 92 (11012) Nonstructural 0 - Interacts with VP2, NSP2 and NSP6 [1, 27]. Homomultimerizes [27,71]. O-linked glycosylation [28]. (Hyper-) Phosphorylated [2, 83]. Autocatalytic kinase activity enhanced by NSP2 interaction [2]. Non-specific ssRNA binding [52,62]. Product of second, out-of-frame ORF [52]. Interacts with NSP5 [27]. Localizes to viroplasm [52]. ': Protein structure/function: RNA polymerase = A(Pol)@; capping enzyme = A(CaP)@; Inner virus structural protein with T = 13 symmetry = A(T13)"; viral inclusion body or viroplasm matrix protein = A(ViP)@. Other species within the genus may have proteins with significant differences in sizes. † Segments numbered based on migration of SA11 genome segments in SDS-PAGE gel. Migration order may differ among other members of the genus. ‡ Proteins with similar functions from other genera. Updated April 2003, by R.F. Ramig & M.K. Estes (from : The RNAs and Proteins of dsRNA Viruses: Edited by Peter. P. C. Mertens and Dennis H. Bamford http://www.iah.bbsrc.ac.uk/dsRNA_virus_proteins/Rotavirus.htm) Please make suggestions for changes or updates to this table by e-mail to Peter Mertens peter.mertens@bbsrc.ac.uk 3 Table supplied by Eric Mossel , Mary Estes and Frank Ramig (from : The RNAs and Proteins of dsRNA Viruses: Edited by Peter. P. C. Mertens and Dennis H. Bamford) Reference List 1. Afrikanova, I., E. Fabbretti, M.C. Miozzo, and O.R. Burrone. 1998. Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2. Journal of General Virology 79:2679-2686. 2. Afrikanova, I., M.C. 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