FUNGAL VIRUS CAPSIDS, CYTOPLASMIC COMPARTMENTS FOR THE REPLICATION OF DOUBLE-STRANDED-RNA, FORMED AS ICOSAHEDRAL SHELLS OF ASYMMETRIC GAG DIMERS

被引:88
作者
CHENG, RH
CASTON, JR
WANG, GJ
GU, F
SMITH, TJ
BAKER, TS
BOZARTH, RF
TRUS, BL
CHENG, NQ
WICKNER, RB
STEVEN, AC
机构
[1] PURDUE UNIV,DEPT BIOL SCI,W LAFAYETTE,IN 47907
[2] NIAMSD,STRUCT BIOL LAB,BETHESDA,MD 20892
[3] NIDDKD,DIV COMP RES & TECHNOL,COMP BIOSCI & ENGN LAB,BETHESDA,MD 20892
[4] NIDDKD,BIOCHEM PHARMACOL LAB,BETHESDA,MD 20892
[5] INDIANA STATE UNIV,DEPT BIOL,TERRE HAUTE,IN 47809
关键词
CRYOELECTRON MICROSCOPY; VIRUS CAPSID PROTEIN; 3-DIMENSIONAL IMAGE RECONSTRUCTION; QUASI-EQUIVALENCE; DOUBLE-STRANDED RNA;
D O I
10.1006/jmbi.1994.1726
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The primary functions of most virus capsids are to protect the viral genome in the extra-cellular milieu and deliver it to the host. In contrast, the capsids of fungal viruses, like the cores of all other known double stranded RNA viruses, are not involved in host recognition but do shield their genomes, and they also carry out transcription and replication. Nascent (+) strands are extruded from transcribing virions. The capsids of the yeast virus L-A are composed of Gag (capsid protein; 76 kDa), with a few molecules of Gag-Pol (170 kDa). Analysis of these 420 Angstrom diameter shells and those of the fungal P4 virus by cryo-electron microscopy and image reconstruction shows that they share the same novel icosahedral structure. Both capsids consist of 60 equivalent Gag dimers, whose two subunits occupy non-equivalent bonding environments. Stoichiometry data on other double-stranded RNA viruses indicate that the 120-subunit structure is widespread, implying that this molecular architecture has features that are particularly favorable to the design of a capsid that is also a biosynthetic compartment.
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页码:255 / 258
页数:4
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