Aqsa Parvaiz, Mishal Subhan, Saba Zafar, Faiz Ahmad Joyia, Sadam Munawar, Muhammad Zarar Hasan and Ghulam Mustafa
1Department of Biochemistry and Biotechnology, The Women University Multan, Multan, Pakistan; 2Department of Microbiology and Molecular Genetics, The Women University Multan, Multan, Pakistan; 3Center of Agricultural Biochemistry and Biotechnology (CABB), Department of Plant Breeding & Genetics, University of Agriculture Faisalabad, 38040, Punjab, Pakistan
*Corresponding author: drmustafa8@gmail.com
Various pathogenesis-related (PR) proteins have been used in combination for effective disease management in plants. However, the mechanism underlying their synergistic effect has not been elucidated at the molecular level. Here, we explore the fundamental molecular mechanism of synergism between thaumatin-like protein (TLP) and PR1 proteins using an in-silico approach. This approach revealed physicochemical properties, predicted subcellular localization, performed topological and domain analyses, analyzed conserved motifs, performed phylogenetic analysis, predicted secondary and tertiary structures, and conducted molecular docking studies of TLP and PR1 proteins alone and in combination with significant components of the fungal cell wall. Physicochemical analyses revealed that TLP is a neutral protein, whereas PR1 is a negatively charged, acidic protein. Both proteins were found to be thermostable based on their aliphatic index values. Similarly, GRAVY values indicated that TLP was hydrophobic, while PR1 was hydrophilic. Furthermore, subcellular localization predicted that both proteins were extracellular. Through topological analysis, TLP was found to be a transmembrane protein, whereas PR1 protein was found on the outer side of the membrane. Lastly, protein-ligand interaction studies via docking between TLP and PR1 alone and in combination with fungal cell wall components such as chitin, chitosan, glucan, and mannan showed a stronger interaction for the TLP-PR1 combination than for TLP and PR1 alone. It can be concluded that these proteins may have more vigorous anti-pathogenic activity co-expressed in plants, hence resulting in broad-spectrum resistance against fungal pathogens.