βC1, pathogenicity determinant encoded by Cotton leaf curl Multan betasatellite, interacts with calmodulin-like protein 11 (Gh-CML11) in Gossypium hirsutum

Autoři: Hira Kamal aff001;  Fayyaz-ul-Amir Afsar Minhas aff002;  Diwaker Tripathi aff004;  Wajid Arshad Abbasi aff002;  Muhammad Hamza aff001;  Roma Mustafa aff001;  Muhammad Zuhaib Khan aff001;  Shahid Mansoor aff001;  Hanu R. Pappu aff003;  Imran Amin aff001
Působiště autorů: National Institute for Biotechnology and Genetic Engineering, Faisalabad, Pakistan aff001;  Pakistan Institute of Engineering and Applied Sciences (PIEAS), Nilore, Islamabad, Pakistan aff002;  Department of Plant Pathology, Washington State University, Pullman, WA, United States of America aff003;  Department of Biology, University of Washington, Seattle, WA, United States of America aff004
Vyšlo v časopise: PLoS ONE 14(12)
Kategorie: Research Article
doi: https://doi.org/10.1371/journal.pone.0225876


Begomoviruses interfere with host plant machinery to evade host defense mechanism by interacting with plant proteins. In the old world, this group of viruses are usually associated with betasatellite that induces severe disease symptoms by encoding a protein, βC1, which is a pathogenicity determinant. Here, we show that βC1 encoded by Cotton leaf curl Multan betasatellite (CLCuMB) requires Gossypium hirsutum calmodulin-like protein 11 (Gh-CML11) to infect cotton. First, we used the in silico approach to predict the interaction of CLCuMB-βC1 with Gh-CML11. A number of sequence- and structure-based in-silico interaction prediction techniques suggested a strong putative binding of CLCuMB-βC1 with Gh-CML11 in a Ca+2-dependent manner. In-silico interaction prediction was then confirmed by three different experimental approaches: The Gh-CML11 interaction was confirmed using CLCuMB-βC1 in a yeast two hybrid system and pull down assay. These results were further validated using bimolecular fluorescence complementation system showing the interaction in cytoplasmic veins of Nicotiana benthamiana. Bioinformatics and molecular studies suggested that CLCuMB-βC1 induces the overexpression of Gh-CML11 protein and ultimately provides calcium as a nutrient source for virus movement and transmission. This is the first comprehensive study on the interaction between CLCuMB-βC1 and Gh-CML11 proteins which provided insights into our understating of the role of βC1 in cotton leaf curl disease.

Klíčová slova:

Cotton – Leaves – Membrane proteins – Nicotiana – Protein interactions – Protein structure – Protein structure prediction – Sequence motif analysis


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