Abstract
Four novel mrkD alleles namely mrkD V1 , mrkD V2 , mrkD V3 , and mrkD V4 were identified in seventeen Klebsiella pneumoniae meningitis strains using PCR-RFLP and sequence determination. Comparative analysis revealed a most variable region containing an RGD motif in the receptor domain of MrkD V3. In order to determine if the sequence confers the K. pneumoniae mrkD V3 the highest level of the fimbrial activity, a type 3 fimbriae display system was constructed in Escherichia coli. The E. coli JM109[pmrkABCD V3F] displaying meshwork-like fimbriae also had the most fimbrial activity, supporting a possible role of the varied sequences. In a dose-dependent manner, the GRGDSP hexapeptide appeared to inhibit the adhesion of the E. coli JM109[pmrkABCD V3F] to HCT-8, an ileocecal epithelial cell line. In addition, the adhesion activity was reduced by the addition of anti-α5β1 integrin monoclonal antibody, indicating that the RGD containing region in MrkD V3 is responsible for the binding of type 3 fimbriae to integrin.
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