Abstract
Tobacco mosaic virus (TMV) coat protein (CP) in absence of RNA self-assembles into several different structures depending on pH and ionic strength. Transgenic plants that produce self-assembling CP are resistant to TMV infection, a phenomenon referred to as coat-protein-mediated resistance (CP-MR). The mutant CP Thr42Trp (CPT42W) produces enhanced CP-MR compared to wild-type CP. To establish the relationship between the formation of 20S CP aggregates and CP-MR, virus-like particles (VLPs) produced by TMV variants that yield high levels of CP-MR were characterized. We demonstrate that non-helical structures are found in VLPs formed in vivo by CPT42W but not by wild-type CP and suggest that the mutation shifts the intracellular equilibrium of aggregates from low to higher proportions of non-helical 20S aggregates. A similar shift in equilibrium of aggregates was observed with CPD77R, another mutant that confers high level of CP-MR. The mutant CPD50R confers a level of CP-MR similar to wild-type CP and aggregates in a manner similar to wild-type CP. We conclude that increased CP-MR is correlated with a shift in intracellular equilibrium of CP aggregates, including aggregates that interfere with virus replication.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 98-106 |
| Number of pages | 9 |
| Journal | Virology |
| Volume | 366 |
| Issue number | 1 |
| DOIs | |
| State | Published - Sep 15 2007 |
| Externally published | Yes |
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Keywords
- 20S
- CP aggregates
- CP mutants
- CP-MR mechanism
- Stacked disk
- TMV
ASJC Scopus subject areas
- Virology
- Infectious Diseases
Cite this
Aggregation of TMV CP plays a role in CP functions and in coat-protein-mediated resistance. / Asurmendi, S.; Berg, R. H.; Smith, Thomas; Bendahmane, M.; Beachy, R. N.
In: Virology, Vol. 366, No. 1, 15.09.2007, p. 98-106.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Aggregation of TMV CP plays a role in CP functions and in coat-protein-mediated resistance
AU - Asurmendi, S.
AU - Berg, R. H.
AU - Smith, Thomas
AU - Bendahmane, M.
AU - Beachy, R. N.
PY - 2007/9/15
Y1 - 2007/9/15
N2 - Tobacco mosaic virus (TMV) coat protein (CP) in absence of RNA self-assembles into several different structures depending on pH and ionic strength. Transgenic plants that produce self-assembling CP are resistant to TMV infection, a phenomenon referred to as coat-protein-mediated resistance (CP-MR). The mutant CP Thr42Trp (CPT42W) produces enhanced CP-MR compared to wild-type CP. To establish the relationship between the formation of 20S CP aggregates and CP-MR, virus-like particles (VLPs) produced by TMV variants that yield high levels of CP-MR were characterized. We demonstrate that non-helical structures are found in VLPs formed in vivo by CPT42W but not by wild-type CP and suggest that the mutation shifts the intracellular equilibrium of aggregates from low to higher proportions of non-helical 20S aggregates. A similar shift in equilibrium of aggregates was observed with CPD77R, another mutant that confers high level of CP-MR. The mutant CPD50R confers a level of CP-MR similar to wild-type CP and aggregates in a manner similar to wild-type CP. We conclude that increased CP-MR is correlated with a shift in intracellular equilibrium of CP aggregates, including aggregates that interfere with virus replication.
AB - Tobacco mosaic virus (TMV) coat protein (CP) in absence of RNA self-assembles into several different structures depending on pH and ionic strength. Transgenic plants that produce self-assembling CP are resistant to TMV infection, a phenomenon referred to as coat-protein-mediated resistance (CP-MR). The mutant CP Thr42Trp (CPT42W) produces enhanced CP-MR compared to wild-type CP. To establish the relationship between the formation of 20S CP aggregates and CP-MR, virus-like particles (VLPs) produced by TMV variants that yield high levels of CP-MR were characterized. We demonstrate that non-helical structures are found in VLPs formed in vivo by CPT42W but not by wild-type CP and suggest that the mutation shifts the intracellular equilibrium of aggregates from low to higher proportions of non-helical 20S aggregates. A similar shift in equilibrium of aggregates was observed with CPD77R, another mutant that confers high level of CP-MR. The mutant CPD50R confers a level of CP-MR similar to wild-type CP and aggregates in a manner similar to wild-type CP. We conclude that increased CP-MR is correlated with a shift in intracellular equilibrium of CP aggregates, including aggregates that interfere with virus replication.
KW - 20S
KW - CP aggregates
KW - CP mutants
KW - CP-MR mechanism
KW - Stacked disk
KW - TMV
UR - http://www.scopus.com/inward/record.url?scp=34548161189&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34548161189&partnerID=8YFLogxK
U2 - 10.1016/j.virol.2007.03.014
DO - 10.1016/j.virol.2007.03.014
M3 - Article
C2 - 17493658
AN - SCOPUS:34548161189
VL - 366
SP - 98
EP - 106
JO - Virology
JF - Virology
SN - 0042-6822
IS - 1
ER -