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Conformational behavior of coat protein in plants and association with coat protein-mediated resistance against TMV.

Authors
  • Sharma, Jatin1, 2
  • Purohit, Rituraj3, 4, 5
  • Hallan, Vipin2, 6
  • 1 Structural Bioinformatics Lab, CSIR-Institute of Himalayan Bioresource Technology (CSIR-IHBT), Palampur, HP, 176061, India. , (India)
  • 2 Biotechnology division, CSIR-IHBT, Palampur, HP, 176061, India. , (India)
  • 3 Structural Bioinformatics Lab, CSIR-Institute of Himalayan Bioresource Technology (CSIR-IHBT), Palampur, HP, 176061, India. [email protected] , (India)
  • 4 Biotechnology division, CSIR-IHBT, Palampur, HP, 176061, India. [email protected] , (India)
  • 5 Academy of Scientific & Innovative Research (AcSIR), CSIR-IHBT Campus, Palampur, HP, 176061, India. [email protected] , (India)
  • 6 Academy of Scientific & Innovative Research (AcSIR), CSIR-IHBT Campus, Palampur, HP, 176061, India. , (India)
Type
Published Article
Journal
Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]
Publication Date
Sep 01, 2020
Volume
51
Issue
3
Pages
893–908
Identifiers
DOI: 10.1007/s42770-020-00225-0
PMID: 31933177
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Tobacco mosaic virus (TMV) coat protein (CP) self assembles in viral RNA deprived transgenic plants to form aggregates based on the physical conditions of the environment. Transgenic plants in which these aggregates are developed show resistance toward infection by TMV referred to as CP-MR. This phenomenon has been extensively used to protect transgenic plants against viral diseases. The mutants T42W and E50Q CP confer enhanced CP-MR as compared to the WT CP. The aggregates, when examined, show the presence of helical discs in the case of WT CP; on the other hand, mutants show the presence of highly stable non-helical long rods. These aggregates interfere with the accumulation of MP as well as with the disassembly of TMV in plant cells. Here, we explored an atomic level insight to the process of CP-MR through MD simulations. The subunit-subunit interactions were assessed with the help of MM-PBSA calculations. Moreover, classification of secondary structure elements of the protein also provided unambiguous information about the conformational changes occurring in the two chains, which indicated toward increased flexibility of the mutant protein and seconded the other results of simulations. Our finding indicates the essential structural changes caused by the mutation in CP subunits, which are critically responsible for CP-MR and provides an in silico insight into the effects of these transitions over CP-MR. These results could further be utilized to design TMV-CP-based small peptides that would be able to provide appropriate protection against TMV infection.

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