1887

Abstract

is the most common cause of enteric disease and presents a major burden on healthcare systems globally due in part to the observed rapid rise in antibiotic resistance. The ability of to form endospores is a key feature in the organism’s pathogenesis and transmission, and contributes greatly to its resilient nature. Endospores are highly resistant to disinfection, allowing them to persist on hospital surfaces. In order for the organism to cause disease, the spores must germinate and revert to a vegetative form. While spore germination in spp. is well understood, very little is known about this process in . Here we report the characterization of SleC (CD0551) from 630. Bioinformatic analysis of SleC indicated a multi-domained protein possessing a peptidoglycan-binding (PGB) domain, a SpoIID/LytB domain and an undefined N-terminal region. We have confirmed that SleC is an exo-acting lytic transglycosylase with the catalytic activity localized to the N-terminal region. Additionally, we have shown that both the N-terminal catalytic domain and the C-terminal PGB domain require muramyl-δ-lactam for substrate binding. As with carbohydrate-binding modules from cellulases and xylanases, the PGB domain may be responsible for increasing the processivity of SleC by concentrating the enzyme at the surface of the substrate.

Funding
This study was supported by the:
  • National Institute of General Medical Sciences (NIGMS)
  • National Institutes of Health (NIH) (Award 8 P20 GM103430-12)
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2014-01-01
2021-07-28
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