Characterization of the type 3 fimbriae with different MrkD adhesins: possible role of the MrkD containing an RGD motif.
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(V3)F] 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(V3)F] to HCT-8, an ileocecal epithelial cell line. In addition, the adhesion activity was reduced by the addition of anti-alpha5beta1 integrin monoclonal antibody, indicating that the RGD containing region in MrkD(V3) is responsible for the binding of type 3 fimbriae to integrin.
Huang
Ying-Jung
YJ
Department of Biological Science and Technology, National Chiao Tung University, Hsin Chu 30050, Taiwan, ROC.
Wu
Chien-Chen
CC
Chen
Mei-Chen
MC
Fung
Chang-Phone
CP
Peng
Hwei-Ling
HL
D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000494:pharmacology*; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion / Q000187:drug effects*; D036781:Fimbriae Proteins / Q000737:chemistry* / Q000494:pharmacology*; D007711:Klebsiella pneumoniae / Q000187:drug effects / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry* / Q000494:pharmacology*
D018829:Adhesins, Bacterial; C058768:Klebsiella pneumoniae type 3 fimbrial adhesin; D009842:Oligopeptides; D036781:Fimbriae Proteins; C047981:arginyl-glycyl-aspartic acid