STABILIZATION OF BROME MOSAIC-VIRUS
STABILIZATION OF BROME MOSAIC-VIRUS
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DOI:
10.1098/rstb.1976.0100
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发表时间:
1976-01-01
影响因子:
6.3
通讯作者:
HIRTH, L
中科院分区:
文献类型:
--
作者:
PFEIFFER, P;HERZOG, M;HIRTH, L
The relative importances of protein-protein and RNA-protein interactions in stabilizing the architecture of brome mosaic virus particles are discussed in the light of the following experimental evidence: disassembly pathways of the virus particles, reassembly of the virus and self-association capacity of the protein moiety, and the role of divalent cations in virus stabilization and their relevance to localization of the RNA in the virus particles. The capsid of BMV may be primarily stabilized by hydrophobic bonds at low pH, but not around and above neutrality where RNA-protein electrostatic interactions are essential to the integrity of the virus particles. A model is proposed for the structure of BMV in the different configurational states.