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Komba, S.

Publications and source records attributed to Komba, S..

2 recordsLinked to original sources

Discovery of a wide variety of α-1,6-cyclized β-1,2-glucan synthases: a new entrance for host-microbe interactions.

-1,6-Cyclized {beta}-1,2-glucans (C{beta}G) are established virulence factors in Xanthomonas, yet functional breadth and distribution of C{beta}Gs in nature have remained unclear. Here, we biochemically identified enzymes synthesizing C{beta}Gs with specific chain lengths, exhibiting potential natural occurrence of various C{beta}Gs. Structural analyses identify subtle variations in a loop, named Loop X, as a key determinant of product size, leading to understanding of the whole picture of the mechanism that controls the sizes. We further demonstrated that C{beta}G composed of 13 glucose units contributes to plant-virulence in Ralstonia pseudosolanacearum, expanding the functional scope of virulence-associated cyclic glucans. Overall, it provides the potential targets for regulating various plant-microbe interactions and also serves as a vital lead to discovering unknown host-microbe interactions with significant potential for agricultural applications.

biochemistry↗

Phytopathogenic cyclic glucohexadecaose from an inverting transglycosylase

Xanthomonas species contain numerous notoriously well-known plant pathogens. Among various pathogenic factors, the role of -1,6-cyclized {beta}-1,2-glucohexadecaose (C{beta}G16) produced by Xanthomonas campestris pv. campestris was shown previously to be vital for infecting model organisms Arabidopsis thaliana and Nicotiana benthamiana. However, enzymes responsible for biosynthesising C{beta}G16 are essentially unknown, which limits the generation of agrichemicals that inhibit C{beta}G16 synthesis. In this study, we discovered that OpgD from X. campestris pv. campestris converts linear {beta}-1,2-glucan to C{beta}G16. Structural and functional analyses revealed that OpgD from X. campestris pv. campestris possesses an anomer-inverting transglycosylation mechanism, which is unprecedented among carbohydrate-active enzymes. The discovery of this unprecedented glucan-generating mechanism reveals a new foundation for the enzymatic synthesis of carbohydrates. Furthermore, identifying C{beta}G16 synthase highly conserved in Xanthomonas provides a broadly adaptable drug target for new-genre agrichemicals that overcome antimicrobial-resistant bacterial issues.

biochemistry↗