Issue
Copyright (c) 2025 Fahimeh Dolatabadi, Mansoor Karimi-Jashni
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
The undersigned hereby assign all rights, included but not limited to copyright, for this manuscript to CMB Association upon its submission for consideration to publication on Cellular and Molecular Biology. The rights assigned include, but are not limited to, the sole and exclusive rights to license, sell, subsequently assign, derive, distribute, display and reproduce this manuscript, in whole or in part, in any format, electronic or otherwise, including those in existence at the time this agreement was signed. The authors hereby warrant that they have not granted or assigned, and shall not grant or assign, the aforementioned rights to any other person, firm, organization, or other entity. All rights are automatically restored to authors if this manuscript is not accepted for publication.In-silico analysis of Rcr3 polymorphism in Solanaceous species and its influence on tomato Cf-2 mediated recognition of the Fulvia fulvum Avr2 effector
Corresponding Author(s) : Mansoor Karimi-Jashni
Cellular and Molecular Biology,
Vol. 71 No. 10: Issue 10
Abstract
Understanding how pathogen recognition has evolved in plants is essential for uncovering the mechanisms of host resistance and enhancing crop resilience. In this study, we examined how polymorphisms influence the evolutionary dynamics of Avr2 effector recognition from Fulvia fulvum across selected Rcr3 proteins in Solanaceae species. Rcr3, a co-receptor protein central to pathogen recognition, displays notable sequence variation that may affect its interaction with Avr2. Amino acid sequences of Rcr3 from ten Solanaceous plant species were obtained from public databases and categorized into compatible or incompatible groups according to their hypersensitive response. Structural modeling and comparative analyses revealed significant polymorphism in the Rcr3 binding sites, with 73 amino acid substitutions in the compatible group and 33 in the incompatible group, relative to the reference species Solanum lycopersicum. Structural assessments indicated that amino acids within the binding grooves of Rcr3 variants exhibit considerable diversity, particularly within incompatible species, where tighter binding interactions (less than 2Å) were observed. In contrast, compatible species displayed more variable, longer-range interactions (up to 6Å), suggesting a correlation between binding site polymorphism and recognition capability. These findings provide critical insights into the molecular basis of pathogen resistance in Solanaceae, highlighting the evolutionary pressures shaping Rcr3 diversity and its functional implications for plant immunity.
Keywords
Download Citation
Endnote/Zotero/Mendeley (RIS)BibTeX
