MOLECULAR-ORGANIZATION OF LEISHMANIA RNA VIRUS-1

被引:133
作者
STUART, KD
WEEKS, R
GUILBRIDE, L
MYLER, PJ
机构
[1] Seattle Biomed. Research Institute, Seattle, WA 98109-1651
[2] Bristol-Myers Squibb P.R.I., Seattle, WA 98121
关键词
RNA-DEPENDENT RNA POLYMERASE; GAG-POL FUSION PROTEIN; TRANSLATION FRAMESHIFT;
D O I
10.1073/pnas.89.18.8596
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The complete 5284-nucleotide sequence of the double-stranded RNA genome of Leishmania RNA virus 1 (LRV1) was determined and contains three open reading frames (ORFs) on the plus (+) (mRNA) strand. The predicted amino acid sequence of ORF3 has motifs characteristic of viral RNA-dependent RNA polymerases. ORF2, which may encode the major viral coat protein, overlaps ORF3 by 71 nucleotides, suggesting a +1 translational frameshift to produce a gag-pol type of fusion protein. Two alternative models for the frame-shift are presented. The 5' splice leader sequence of kinetoplastid mRNAs is not in LRV1 RNA. This suggests that the 450-base region at the 5' end of the LRV1 (+)-strand, which contains ORF1 and is highly conserved among viral strains, does not encode protein but has a role in initiation of translation and/or RNA stability. The similarity of LRV1 genomic organization, replication cycle, and RNA-dependent RNA polymerase sequence to those of the yeast virus ScV L-A suggests a common ancestral origin. The possibility that LRV1 affects pathogenesis in leishmaniasis is intriguing.
引用
收藏
页码:8596 / 8600
页数:5
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