Packaging and structural phenotype of brome mosaic virus capsid protein with altered N-terminal {beta}-hexamer structure
- Department of Plant Pathology and Microbiology, University of California, Riverside, CA 92521-0122 (United States)
- Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210 (United States)
The first 45 amino acid region of brome mosaic virus (BMV) capsid protein (CP) contains RNA binding and structural domains that are implicated in the assembly of infectious virions. One such important structural domain encompassing amino acids {sup 28}QPVIV{sup 32}, highly conserved between BMV and cowpea chlorotic mottle virus (CCMV), exhibits a {beta}-hexamer structure. In this study we report that alteration of the {beta}-hexamer structure by mutating {sup 28}QPVIV{sup 32} to {sup 28}AAAAA{sup 32} had no effect either on symptom phenotype, local and systemic movement in Chenopodium quinoa and RNA profile of in vivo assembled virions. However, sensitivity to RNase and assembly phenotypes distinguished virions assembled with CP subunits having {beta}-hexamer from those of wild type. A comparison of 3-D models obtained by cryo electron microscopy revealed overall similar structural features for wild type and mutant virions, with small but significant differences near the 3-fold axes of symmetry.
- OSTI ID:
- 21587893
- Journal Information:
- Virology, Vol. 419, Issue 1; Other Information: DOI: 10.1016/j.virol.2011.07.016; PII: S0042-6822(11)00324-2; Copyright (c) 2011 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0042-6822
- Country of Publication:
- United States
- Language:
- English
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