TY - JOUR
T1 - Virion tails of Beet yellows virus
T2 - Coordinated assembly by three structural proteins
AU - Alzhanova, Dina V.
AU - Prokhnevsky, Alexey I.
AU - Peremyslov, Valera V.
AU - Dolja, Valerian V.
N1 - Funding Information:
We thank Tatineni Satyanarayana and William Dawson for stimulating discussions. This work was supported by a grant from the National Institutes of Health (GM053190) to V.V.D.
PY - 2007/3/1
Y1 - 2007/3/1
N2 - Filamentous virions of Beet yellows virus contain a long body formed by a major capsid protein and a short tail that is assembled by a minor capsid protein (CPm), an Hsp70-homolog (Hsp70h), a 64-kDa protein (p64), and a 20-kDa protein (p20). Using mutation analysis and newly developed in planta assays, here we investigate the genetic requirements for the tail assembly. We show that the inactivation of CPm dramatically reduces incorporation of both Hsp70h and p64. Furthermore, inactivation of Hsp70h prevents incorporation of p64 into virions and vice versa. Hsp70h and p64 are each required for efficient incorporation of CPm. We also show that the tails possessing normal relative amounts of CPm, Hsp70h, and p64 can be formed in the absence of the major capsid protein and p20. Similar to the tails isolated from the wild-type virions, these mutant tails encapsidate the ∼ 700 nt-long, 5′-terminal segments of the viral RNA. Taken together, our results imply that CPm, Hsp70h and p64 act cooperatively to encapsidate a defined region of the closterovirus genome.
AB - Filamentous virions of Beet yellows virus contain a long body formed by a major capsid protein and a short tail that is assembled by a minor capsid protein (CPm), an Hsp70-homolog (Hsp70h), a 64-kDa protein (p64), and a 20-kDa protein (p20). Using mutation analysis and newly developed in planta assays, here we investigate the genetic requirements for the tail assembly. We show that the inactivation of CPm dramatically reduces incorporation of both Hsp70h and p64. Furthermore, inactivation of Hsp70h prevents incorporation of p64 into virions and vice versa. Hsp70h and p64 are each required for efficient incorporation of CPm. We also show that the tails possessing normal relative amounts of CPm, Hsp70h, and p64 can be formed in the absence of the major capsid protein and p20. Similar to the tails isolated from the wild-type virions, these mutant tails encapsidate the ∼ 700 nt-long, 5′-terminal segments of the viral RNA. Taken together, our results imply that CPm, Hsp70h and p64 act cooperatively to encapsidate a defined region of the closterovirus genome.
KW - Closterovirus
KW - Helical virion
KW - Hsp70
KW - Virus assembly
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U2 - 10.1016/j.virol.2006.09.007
DO - 10.1016/j.virol.2006.09.007
M3 - Article
C2 - 17027895
AN - SCOPUS:33846833801
SN - 0042-6822
VL - 359
SP - 220
EP - 226
JO - Virology
JF - Virology
IS - 1
ER -