Chitin-binding function and glycosyl hydrolysis/motor-like system facilitate the spread of the wheat mosaic virus

27 October 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Infecting cereals and grasses worldwide, wheat mosaic disease poses a serious risk to food security. The major grain producing regions have been threatened by major crop diseases and insect pests. The wheat curl mite was previously thought to be the primary vector for the spread of the wheat mosaic virus. However, recent research has shown that soil may actually be more influential. In this present study,we used domain search of the bioinformatics method to study the coat protein of the Chinese wheat mosaic virus. The wheat mosaic virus's binding regions to chitin, chitosan, and cellulose, as well as the active region of cell wall degrading enzymes, and the related domains of endocytotic entry, were determined through the domain search.There are Ca2+ and Mg2+-ATP binding sites in the wheat mosaic virus coat protein. It demonstrates that wheat mosaic virus can complete its transmission by binding chitin via its coat protein. By binding Ca2+ via an EF-hand, the coat protein is capable of inducing the binding of Mg2+-ATP, which is essential for initiating serine-threonine kinase activity. A coating containing serine kinase activity facilitates the capacity of proteins to bind chitin, collagen, or fibrillar cellulose. Upon activation of the PPM enzyme domain that binds Mg2+-ATP, glycosyl hydrolases and swelling enzymes become active. This process necessitates the hydrolysis of glycosyl chains contained in proteins, which contributes to the enlargement of the cell wall. As they continue to move, the motor domains of the coat protein rotate and puncture holes in the cell wall. Using phospholipid transporter domains, it creates membrane fusion pores on the cell membrane. At the same time, the coat protein inserts viral genetic material into plant cells.


serine-threonine kinase
Glycosyl hydrolase
Phospholipid transporting


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