A computational study integrating antiviral peptide mediated inhibition of trafficking complex in Sesbania Mosaic Virus

Abstract

Plant viruses pose a serious threat to global agriculture and although chemical, genetic, and biological control strategies exist, but each method have limitations in effectiveness and sustainability. Recently, the use of microbial peptides for curbing the movement of plant viruses has gained momentum. In this work, five peptides viz. Peptamine, indolicidin 10R, indolicidin 11R, Recombinant Thanatin (RT) and Recombinant Chimeric Lactoferricin + Lactoferrampin (RCLL), were identified and analysed for their role in disrupting the virus movement. The Sesbania Mosaic Virus (SeMV) is known to use a trafficking complex (a heteroprotein complex consisting of movement protein (MP), RdRp, VPg, and P10) for its intercellular movement. In this work, the ability of these peptides in binding to the major constituents of the trafficking complex (the MP and the RdRp) and their ability to disrupt the formation of trafficking complex was analysed using in silico tools. All five peptides were found to be disrupting the formation of the trafficking complex. Our findings suggest that these peptides can serve as potential antiviral agents by interfering with essential viral functions. This study provides new insights into peptide-based inhibition of plant viruses, offering an alternative to conventional control strategies.