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Clostridium perfringens can produce up to three different sialidases, including NanI, its major exosialidase. The current study first showed that human intestinal strains ofC. perfringens can grow by utilizing either glucose or sialic acids, such asN -acetylneuraminic acid (Neu5Ac), which are the end products of sialidase activity. For the human enteropathogenic strain F4969, it was then determined that culture supernatant sialidase activity and expression of exosialidase genes, particularlynanI , are influenced by the presence of Neu5Ac or glucose. Low Neu5Ac concentrations increased culture supernatant sialidase activity, largely by stimulatingnanI transcription. In contrast, low glucose concentrations did not affect exosialidase activity ornanI transcription. However, either high Neu5Ac or high glucose concentrations repressed F4969 culture supernatant sialidase activity andnanI transcription levels. Furthermore, high glucose levels repressed F4969 culture sialidase activity andnanI expression even in the presence of low Neu5AC concentrations. To begin to evaluate the mechanistic basis fornanI expression, ananR null mutant was used to demonstrate that NanR, a member of the RpiR family of regulatory proteins, decreases exosialidase activity andnanI transcription in the absence of sialic acid. The ability ofC. perfringens to regulate its exosialidase activity, largely by controllingnanI expression, may affect intestinal pathogenesis by affecting the production of NanI, which may affectC. perfringens growth, adhesion, and toxin bindingin vivo .

NanR Regulates nanI Sialidase Expression by Clostridium perfringens F4969, a Human Enteropathogenic Strain