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Identification of receptors for two novel Escherichia coli 0157:H7 bacteriophage E. coli 0157:H7 is a major human pathogen transmitted to humans primarily through contaminated meat products. Reducing the pathogen load in food animals with the use of natural bacteriophage can improve food safety. The objective of this thesis was to characterize the receptor sites of two novel bacteriophage that form part of an effective cocktail product under development at Gangagen Life Sciences Inc. This was accomplished by developing and characterizing mutants resistant to R26, a Tl-like phage and P39, a T4-like phage. Most mutants resistant to P39 were sensitive to R26 and vice versa suggesting that the two phage target different receptor molecules. Lipopolysaccharide (LPS) was identified as a potential receptor for phage R26 as indicated by differences in LPS profiles of the R26-resistant mutants. Sequence analysis of the rfaF gene in Ec4BIMR26R12, an R26-resistant mutant, revealed a mutation that would give rise to a truncated non-functional enzyme, resulting in truncated LPS. OmpC was shown to be required for P39 binding using PCR, Southern blot analysis and genome walking. A deletion in the region of the ompC gene resulting in a non-functional OmpC protein was identified. This was confirmed by sequencing and complementation studies by expressing OmpC from E. coli 0157:H7 in a P39-resistant mutant, Ec4BIMP39R3.

Identification of receptors for two novel Escherichia coli O157:H7 bacteriophage