期刊
VIROLOGY
卷 366, 期 1, 页码 98-106出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2007.03.014
关键词
TMV; CP-MR mechanism; CP mutants; CP aggregates; stacked disk; 20S
类别
资金
- NIAID NIH HHS [R01 AI027161-13, AI27161, R01 AI027161] Funding Source: Medline
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 Cp-T42w 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 Cp-D50R 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. (c) 2007 Elsevier Inc. All rights reserved.
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