Genome Segment - reoviridae.org

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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)
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5
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)
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6
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)
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7
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)
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8
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)
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9
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)
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10
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)
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11
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)
86. Zeng, C.Q.Y., M. Labbe, J. Cohen, B.V.V. Prasad, D. Chen, R.F. Ramig and M.K. Estes. 1994. Characterization of rotavirus VP2
particles. Virology 201: 55-65.
87. Zeng, C.Q.Y., M.J. Wentz, J. Cohen, M.K. Estes, and R.F. Ramig. 1996. Characterization and replicase activity of double-layered and
single-layered rotavirus-like particles expressed from baculovirus recombinants. Journal of Virology 70:2736-2742.
88. Prasad, B.V.V. Burns, J.W., Marietta, E., Estes, M.K., and Chiu, W. 1990, Localization of VP4 neutralization sites in rotavirus by threedimensional electron cryo-microscopy, Nature, 343: 476-479.
89. Shaw, A., L., Rothnagel, R., Chen, D., Ramig, R.F., Chiu, W. and Prasad, B.V.V. 1993 Three-dimensional visualization of rotavirus
hemagglutinin structure. Cell 74:693-701.
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