Abstract
ABSTRACTSialidases, which are widely distributed in nature, cleave the α-ketosidic bond of terminal sialic acid residue. These emerging virulence factors degrade the host glycan. We report here the release of seven sialidase and one sialic acid transporter deletion in Salmonella enterica serovar Typhimurium strain LT2, which are important in cellular invasion during infection.
Highlights
Sialidases, which are widely distributed in nature, cleave the ␣-ketosidic bond of terminal sialic acid residue
Sialidases play an important role in infection by altering the host glycan structure to gain access of the host epithelial cells by binding to terminal sialic acid receptors to initiate glycan degradation [6]
The two sialidases (⌬nanH and ⌬STM1252) from Salmonella enterica serovar Typhimurium LT2 have the same domains and function as sialidases, but they are structurally very different, indicating domain shuffling and lack of structural conservation; this difference led to different invasion phenotypes during the in vitro infection of differentiated colonic epithelial cells (Caco-2) [6]
Summary
Sialidases, which are widely distributed in nature, cleave the ␣-ketosidic bond of terminal sialic acid residue. The presence of sialidases is highly correlated with the progress and severity of the disease, and the most probable role of sialidases is for successful attachment and colonization. Microbes use sialidases to reveal the cell surface that holds sialic acidcontaining cell membrane receptors during infection.
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