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Title: Packaging and structural phenotype of brome mosaic virus capsid protein with altered N-terminal {beta}-hexamer structure

Abstract

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.

Authors:
;  [1];  [2];  [1]
  1. Department of Plant Pathology and Microbiology, University of California, Riverside, CA 92521-0122 (United States)
  2. Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210 (United States)
Publication Date:
OSTI Identifier:
21587893
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 419; Journal 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)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AMINO ACIDS; ELECTRON MICROSCOPY; IN VIVO; MUTANTS; PHENOTYPE; PROTEINS; RNA; SENSITIVITY; VIRUSES; CARBOXYLIC ACIDS; MICROORGANISMS; MICROSCOPY; NUCLEIC ACIDS; ORGANIC ACIDS; ORGANIC COMPOUNDS; PARASITES

Citation Formats

Wispelaere, Melissanne de, Chaturvedi, Sonali, Wilkens, Stephan, and Rao, A.L.N., E-mail: arao@ucr.edu. Packaging and structural phenotype of brome mosaic virus capsid protein with altered N-terminal {beta}-hexamer structure. United States: N. p., 2011. Web. doi:10.1016/j.virol.2011.07.016.
Wispelaere, Melissanne de, Chaturvedi, Sonali, Wilkens, Stephan, & Rao, A.L.N., E-mail: arao@ucr.edu. Packaging and structural phenotype of brome mosaic virus capsid protein with altered N-terminal {beta}-hexamer structure. United States. doi:10.1016/j.virol.2011.07.016.
Wispelaere, Melissanne de, Chaturvedi, Sonali, Wilkens, Stephan, and Rao, A.L.N., E-mail: arao@ucr.edu. Mon . "Packaging and structural phenotype of brome mosaic virus capsid protein with altered N-terminal {beta}-hexamer structure". United States. doi:10.1016/j.virol.2011.07.016.
@article{osti_21587893,
title = {Packaging and structural phenotype of brome mosaic virus capsid protein with altered N-terminal {beta}-hexamer structure},
author = {Wispelaere, Melissanne de and Chaturvedi, Sonali and Wilkens, Stephan and Rao, A.L.N., E-mail: arao@ucr.edu},
abstractNote = {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.},
doi = {10.1016/j.virol.2011.07.016},
journal = {Virology},
number = 1,
volume = 419,
place = {United States},
year = {Mon Oct 10 00:00:00 EDT 2011},
month = {Mon Oct 10 00:00:00 EDT 2011}
}