Abstract
Yersinia adhesin A (YadA) is a key virulence factor of Yersinia enterocolitica and Yersinia pseudotuberculosis. YadA is a trimeric autotransporter adhesin, a class of adhesins that have been shown to enable many Gram-negative pathogens to adhere to/interact with the host extracellular matrix proteins such as collagen, vitronectin, and fibronectin. Here, we show for the first time that YadA of Yersinia enterocolitica serotype O:9 not only interacts with proteinaceous surface molecules but can also attach directly to glycan moieties. We show that YadA from Y. enterocolitica serotype O:9 does not interact with the vitronectin protein itself but exclusively with its N-linked glycans. We also show that YadA can target other glycan moieties as found in heparin, for example. So far, little is known about specific interactions between bacterial autotransporter adhesins and glycans. This could potentially lead to new antimicrobial treatment strategies, as well as diagnostic applications.
Highlights
Yersinia adhesin A (YadA), a type Vc trimeric autotransporter adhesin of Yersinia spp. is crucial for virulence
We first aimed to describe the molecular details of the interaction between the YadA head domain of Y. enterocolitica serotype O:9 (YadAO:9) and Vn
Vn purified from plasma (Vnplasma), Vn expressed in HEK cell culture (VnHEK), and Vn recombinantly expressed in E. coli (VnEc) were tested for their capacity to be bound by E. coli expressing either full-length YadAO:8 or YadAO:9 (Figure 1B)
Summary
Yersinia adhesin A (YadA), a type Vc trimeric autotransporter adhesin of Yersinia spp. is crucial for virulence. YadA is encoded on a virulence plasmid, the pYV plasmid. YadA is a surface-exposed adhesin that is anchored in the bacterial outer membrane via a trimeric β-barrel domain (Shahid et al, 2015). The passenger domain of YadA, a trimeric coiledcoil stalk, and an N-terminal β-roll head domain are channeled through the barrel in an unfolded state during the autotransport process (Chauhan et al, 2019). The passenger domain starts folding, building a rigid structure protruding toward the outside of the cell (Chauhan et al, 2019). The head domain has been shown to be responsible for many of YadA’s adhesion properties (Leo et al, 2008; Mühlenkamp et al, 2015)
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