Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 41, Issue 18, Pages 9039-9056Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2022.2139763
Keywords
Rare lipoprotein A; molecular docking; MD simulations; effector-protease interaction; hypersensitive response; cell-death suppression
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This study reveals the mechanism of interaction between a novel secreted effector protein, MoRlpA, from the blast fungus Magnaporthe oryzae and rice cathepsin B enzyme, which helps the pathogen suppress host's counter-attack and establish a successful infection. This research provides insights for developing potential fungicides.
The blast fungus Magnaporthe oryzae is one of the most notorious pathogens affecting rice production worldwide. The cereal killer employs a special class of small secreted proteins called effectors to manipulate and perturb the host metabolism. In turn, the host plants trigger effector-triggered immunity (ETI) via localized cell death and hypersensitive response (HR). We have identified and characterized a novel secreted effector MoRlpA from M. oryzae by extensive in silico methods. The localization studies suggested that it is exclusively secreted in the host apoplasts. Interestingly, MoRlpA interacts with a protease, cathepsin B from rice with highest affinity. The 3D structural models of both the proteins were generated. Cathepsin B-like cysteine proteases are usually involved in programmed cell death (PCD) and autophagy in plants which lead to generation of HR upon infection. Our results suggest that MoRlpA interacts with rice cathepsin B-like cysteine protease and demolish the host counter-attack by suppressing cell death and HR during an active blast infection. This was further validated by molecular docking and molecular dynamic simulation analyses. The important residues involved in the rice-blast pathogen interactions were deciphered. Overall, this research highlights stable interactions between MoRlpA-OsCathB during rice blast pathogenesis and providing an insight into how this novel RlpA protease inhibitor-cum-effector modulates the host's apoplast to invade the host tissues and establish a successful infection. Thus, this research will help to develop potential fungicide to block the binding region of MoRlpA target so that the cryptic pathogen would be recognized by the host.
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