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Effect of the cortex-lytic enzyme SleC from non-food-borne Clostridium perfringens on the germination properties of SleC-lacking spores of a food poisoning isolate

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The hallmark of bacterial spore germination is peptidoglycan cortex hydrolysis by cortex-lytic enzymes. In spores of Clostridium perfringens wild-type strain SM101, which causes food poisoning, the sole essential cortex-lytic enzyme SleC is activated by a unique serine protease CspB. Interestingly, the non-food-borne wild-type strain F4969 encodes a significantly divergent SleC variant (SleCF4969) and 3 serine proteases (CspA, CspB, and CspC). Consequently, in this study we evaluated the functional compatibility of SleCF4969 and SleCSM101 by complementing the germination phenotypes of SM101ΔsleC spores with sleCF4969. Our results show that although pro-SleCF4969 was processed into mature SleCF4969 in the SM101ΔsleC spores, it partially restored spore germination with nutrient medium, with a mixture of l-asparagine and KCl, or with a 1:1 chelate of Ca2+ and dipicolinic acid. While the amount of dipicolinic acid released was lower, the amount of hexosamine-containing material released during germination of SM101ΔsleC(sleCF4969) spores was similar to the amount released during germination of SM101 wild-type spores. The viability of SM101ΔsleC(sleCF4969) spores was 8- and 3-fold lower than that of SM101 and F4969 spores, respectively. Together, these data indicate that the peptidoglycan cortex hydrolysis machinery in the food poisoning isolate SM101 is functionally divergent than that in the non-food-borne isolate F4969.

La caractéristique de la germination des spores bactériennes consiste en l’hydrolyse du peptidoglycane cortical par des enzymes lytiques du cortex. Chez les spores de la souche SM101 sauvage de Clostridium perfringens associée à l’intoxication alimentaire, la seule enzyme lytique essentielle, SleC, est activée par une sérine protéase unique, CspB. Fait intéressant, la souche F4969 sauvage d’origine non alimentaire code un variant significativement divergent de SleC (SelCF4969) et 3sérine protéases (CspA, CspB et CspC). Ainsi, cette étude visait à évaluer la compatibilité fonctionnelle de SleCF4969 envers SleCSM101 en complémentant les phénotypes de germination des spores SM101ΔsleC avec sleCF4969. Nos résultats montrent que même si la pro-SleCF4969 est maturée en SleCF4969 dans les spores SM101ΔsleC, elle ne rétablit que partiellement la germination des spores dans un milieu nutritif composé d’un mélange de l-asparagine et de KCl, ou dans un chélate 1 :1 de Ca+2 et d’acide dipicolinique. Alors que la libération d’acide dipicolinique est plus faible, la libération de matériel comprenant de l’hexosamine durant la germination des spores SM101ΔsleC (sleCF4969) était similaire à celle des spores SM101 sauvages. La viabilité des spores SM101ΔsleC (sleCF4969) était 8 fois et 3 fois inférieure que celle des spores SM101 et F4969 respectivement. En somme, ces données indiquent que la machinerie enzymatique d’hydrolyse du peptidoglycane cortical de l’isolat SM101 associé à l’intoxication alimentaire est fonctionnellement divergente de celle de l’isolat F4969 d’origine non alimentaire.

Document Type: Research Article

Publication date: 2010-11-01

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  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
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