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

  • Jatin Sharma
  • Rituraj PurohitEmail author
  • Vipin Hallan
Bacterial Fungal and Virus Molecular Biology - Research Paper


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.


Coat protein-mediated resistance Coat protein Tobacco mosaic virus Flexibility 



Coat protein-mediated resistance


Tobacco mosaic virus


Coat protein


Root mean square deviation


Root mean square fluctuation


Radius of gyration


Molecular Dynamics



We gratefully acknowledge to the Director, CSIR-Institute of Himalayan Bioresource Technology, Palampur for providing the facilities to carry out this work. CSIR support in the form of projects MLP0201 and MLP0140 for these studies is highly acknowledged. This manuscript represents CSIR-IHBT communication no. 4494.

Data availability statement

The data that support the findings of this study are openly available in Research Collaboratory for Structural Bioinformatics – Protein Data Bank (RCSB-PDB) at, PDB id – 1EI7.

Author contribution

RP conceived of and designed the study. RP, JS analyzed and interpreted the data. JS drafted the paper and RP critically revised it for important intellectual content and and VP provided intellectual inputs. All authors gave final approval of the version to be published.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

42770_2020_225_MOESM1_ESM.pdf (45.5 mb)
ESM 1 (PDF 46586 kb)


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Copyright information

© Sociedade Brasileira de Microbiologia 2020

Authors and Affiliations

  1. 1.Structural Bioinformatics LabCSIR-Institute of Himalayan Bioresource Technology (CSIR-IHBT)PalampurIndia
  2. 2.Biotechnology division, CSIR-IHBTPalampurIndia
  3. 3.Academy of Scientific & Innovative Research (AcSIR)CSIR-IHBT CampusPalampurIndia

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