title: Adherence to respiratory epithelia by recombinant Escherichia coli expressing Klebsiella pneumoniae type 3 fimbrial gene products.
abstract: We examined the role of Klebsiella fimbrial types 1 and 3 in mediating adherence to human buccal and tracheal cells and to lung tissue sections. We found that clinical isolates of Klebsiella pneumoniae producing type 3 fimbriae and Escherichia coli HB101 containing a recombinant plasmid encoding expression of Klebsiella type 3 fimbriae (pFK10) demonstrated increased adherence to tracheal cells, trypsinized buccal cells, and lung tissue sections, in contrast to nonfimbriate and to type 1 fimbriate bacteria. Adherence by type 3 fimbriate bacteria was inhibited by purified type 3 fimbriae and Fab fragments derived from type 3 fimbrial-specific polyclonal immunoglobulin G. Type 3 fimbriae mediated attachment to the basolateral surface of tracheal cells and to the basal epithelial cells and the basement membrane regions of bronchial epithelia. Using an E. coli transformant (pDC17/pFK52), which expresses nonadherent P fimbrial filaments, along with the type 3 fimbrial adhesin (MrkD), we demonstrated that type 3 fimbrial attachment to respiratory cells was attributable to the MrkD adhesin subunit. Subsequent experiments demonstrated that the epithelial target of the type 3 fimbrial adhesin was most likely a peptide molecule rather than a carbohydrate. The results of this study demonstrate that, in vitro, the Klebsiella type 3 fimbrial adhesin mediates adherence to human respiratory tissue.
authors.affiliation: Department of Internal Medicine, University of Iowa College of Medicine, Iowa City 52242.
authors.forename: D B
authors.initials: DB
authors.lastname: Hornick
authors.forename: B L
authors.initials: BL
authors.lastname: Allen
authors.forename: M A
authors.initials: MA
authors.lastname: Horn
authors.forename: S
authors.initials: S
authors.lastname: Clegg
mesh_terms: D000085:Acetates / Q000494:pharmacology; D019342:Acetic Acid; D018829:Adhesins, Bacterial; D001422:Bacterial Adhesion / Q000187:drug effects / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000494:pharmacology*; D002610:Cheek / Q000382:microbiology; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D004848:Epithelium / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D036781:Fimbriae Proteins; D005947:Glucose / Q000494:pharmacology; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000502:physiology; D066298:In Vitro Techniques; D007711:Klebsiella pneumoniae / Q000472:pathogenicity*; D007785:Lactose / Q000494:pharmacology; D008168:Lung / Q000382:microbiology; D008239:Lysine / Q000494:pharmacology; D003012:Microbial Collagenase / Q000494:pharmacology; D010504:Periodic Acid / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology; D011479:Protamines / Q000494:pharmacology; D011994:Recombinant Proteins / Q000494:pharmacology; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000494:pharmacology; D014132:Trachea / Q000382:microbiology
chemical_list: D000085:Acetates; D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D007140:Immunoglobulin Fab Fragments; C058768:Klebsiella pneumoniae type 3 fimbrial adhesin; D011479:Protamines; D011994:Recombinant Proteins; D010504:Periodic Acid; D036781:Fimbriae Proteins; D011107:Polylysine; D013096:Spermine; C009288:metaperiodate; D003012:Microbial Collagenase; D005947:Glucose; D007785:Lactose; D008239:Lysine; D019342:Acetic Acid; D013095:Spermidine