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• W2024392521 abstract "Surface layers (S-layers) form regular crystalline structures on the outermost surface of many bacteria. Clostridium difficile possesses such an S-layer consisting of two protein subunits. Treatment of whole cells of C. difficile with 5 M guanidine hydrochloride revealed two major proteins of different molecular masses characteristic of the S-layer on SDS-PAGE. In this study 25 isolates were investigated. A high degree of variability in the molecular mass of the two S-layer proteins was evident. Molecular masses ranged from 48 to 56 kDa for the heavier protein and from 37 to 45 kDa for the lighter protein. A further protein component of 70 kDa was detectable in all isolates. No cross-reaction was seen between the two major proteins from isolates that produced different S-layer patterns, and most S-layer proteins from isolates with the same or similar banding patterns did not cross-react. The S-layer proteins, when detected by a combination of Coomassie blue staining and immunoblotting, are a useful marker for phenotyping." @default.
• W2024392521 created "2016-06-24" @default.
• W2024392521 creator A5027852010 @default.
• W2024392521 creator A5052040174 @default.
• W2024392521 date "2001-08-01" @default.
• W2024392521 modified "2023-10-12" @default.
• W2024392521 title "Variation in the surface layer proteins of<i>Clostridium difficile</i>" @default.
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• W2024392521 doi "https://doi.org/10.1111/j.1574-695x.2001.tb00509.x" @default.
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