Immunohistological localization of the MrkD adhesin in the type 3 fimbriae of Klebsiella pneumoniae.
The adhesive minor protein MrkD of the type 3 fimbria of Klebsiella pneumoniae was expressed and purified from Escherichia coli as a fusion protein with an N-terminal polyhistidine tail. Polyclonal antibodies raised against MrkD specifically recognized the MrkD peptide in Western blots of fimbrial preparations. Immunoelectron microscopic analyses showed that the anti-MrkD immunoglobulins bound to the tip of the plasmid-encoded variant of the type 3 fimbria of K. pneumoniae, whereas no binding to the chromosomally encoded MrkD-deficient type 3 fimbrial variant of K. pneumoniae was detected. Immunoglobulins from an antiserum raised against purified type 3 fimbrial filaments bound laterally to both type 3 fimbrial variants. The anti-MrkD antibodies also bound to the tip of a papG deletion derivative of the E. coli P fimbria complemented with mrkD, indicating that MrkD structurally complements a PapG mutation in the P fimbria of E. coli.
Tarkkanen
A M
AM
Department of Biosciences, University of Helsinki, Finland.
Westerlund-Wikström
B
B
Erkkilä
L
L
Korhonen
T K
TK
D018829:Adhesins, Bacterial / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D000818:Animals; D000918:Antibody Specificity; D010861:Fimbriae, Bacterial / Q000737:chemistry*; D007114:Immunization; D007150:Immunohistochemistry; D007711:Klebsiella pneumoniae / Q000737:chemistry*; D016253:Microscopy, Immunoelectron; D008970:Molecular Weight; D011817:Rabbits; D011994:Recombinant Proteins / Q000096:biosynthesis
D018829:Adhesins, Bacterial; D011994:Recombinant Proteins