Abstract
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 Å 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 255-258 |
| Number of pages | 4 |
| Journal | Journal of Molecular Biology |
| Volume | 244 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1994 |
| Externally published | Yes |
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Keywords
- Cryo-electron microscopy
- Double-stranded RNA
- Quasi-equivalence
- Three-dimensional image reconstruction
- Virus capsid protein
ASJC Scopus subject areas
- Virology
Cite this
Fungal virus capsids, cytoplasmic compartments for the replication of double-stranded RNA, formed as icosahedral shells of asymmetric gag dimers. / Cheng, R. Holland; Caston, Jose R.; Wang, Guo Ji; Gu, Fei; Smith, Thomas; Baker, Timothy S.; Bozarth, Robert F.; Trus, Benes L.; Cheng, Naiqian; Wickner, Reed B.; Steven, Alasdair C.
In: Journal of Molecular Biology, Vol. 244, No. 3, 1994, p. 255-258.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Fungal virus capsids, cytoplasmic compartments for the replication of double-stranded RNA, formed as icosahedral shells of asymmetric gag dimers
AU - Cheng, R. Holland
AU - Caston, Jose R.
AU - Wang, Guo Ji
AU - Gu, Fei
AU - Smith, Thomas
AU - Baker, Timothy S.
AU - Bozarth, Robert F.
AU - Trus, Benes L.
AU - Cheng, Naiqian
AU - Wickner, Reed B.
AU - Steven, Alasdair C.
PY - 1994
Y1 - 1994
N2 - 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 Å 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.
AB - 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 Å 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.
KW - Cryo-electron microscopy
KW - Double-stranded RNA
KW - Quasi-equivalence
KW - Three-dimensional image reconstruction
KW - Virus capsid protein
UR - http://www.scopus.com/inward/record.url?scp=0027973510&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027973510&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1994.1726
DO - 10.1006/jmbi.1994.1726
M3 - Article
C2 - 7966336
AN - SCOPUS:0027973510
VL - 244
SP - 255
EP - 258
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 3
ER -