SINDBIS VIRUS PROTEINS NSP1 AND NSP2 CONTAIN HOMOLOGY TO NONSTRUCTURAL PROTEINS FROM SEVERAL RNA PLANT-VIRUSES
SINDBIS VIRUS PROTEINS NSP1 AND NSP2 CONTAIN HOMOLOGY TO NONSTRUCTURAL PROTEINS FROM SEVERAL RNA PLANT-VIRUSES
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DOI:
10.1128/jvi.53.2.536-542.1985
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发表时间:
1985-01-01
影响因子:
5.4
通讯作者:
ZIMMERN, D
中科院分区:
文献类型:
--
作者:
AHLQUIST, P;STRAUSS, EG;ZIMMERN, D
Although the genetic organization of tobacco mosaic virus (TMV) differs considerably from that of the tripartite viruses (alfalfa mosaic virus [AIMV] and brome mosaic virus [BMV]), all of these RNA plant viruses share 3 domains of homology among their nonstructural proteins. One such domain, common to the AIMV and BMV 2a proteins, and the readthrough portion of TMV p183, is also homologous to the readthrough protein nsP4 of Sindbis virus. Two more domains are conserved among the AIMV and BMV 1a proteins and TMV p126. These domains have homology with portions of the Sindbis proteins nsP1 and nsP2, respectively. These results strengthen the view that the 4 viruses share mechanistic similarities in their replication strategies and may be evolutionarily related. These results also suggest that either the AIMV 1a, BVM 1a and TMV p126 proteins are multifunctional or Sindbis proteins nsP1 and nsP2 function together as subunits in a single complex.