Identification and characterization of the genes encoding the type 3 and type 1 fimbrial adhesins of Klebsiella pneumoniae

Gerlach, Gerald-F.; Clegg, Steven; Allen, Bradley L.

doi:10.1128/jb.171.3.1262-1270.1989

Cited by 123 publications

(115 citation statements)

References 28 publications

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“…4) shows that three open reading frames similar to those for fimbrial proteins, phfB, phfA, and phfD, are located 5Ј and on the same strand as ngrA. The phfB gene is located 54 bp from ngrA and is 1,014 bp in length, with residues 215 to 337 of the predicted protein product being 37% identical and 53% similar to the type I fimbrial subunit (FimA/PapA family) (spP12903) (29). The next gene 5Ј of ngrA, phfA, is 966 bp in length with residues 115 to 320 of the predicted protein product being 28% identical and 42% similar to the fimbrial adhesin MrkD from Klebsiella pneumoniae (spP21648) (3).…”

Section: Resultsmentioning

confidence: 99%

A Phosphopantetheinyl Transferase Homolog Is Essential for Photorhabdus luminescens To Support Growth and Reproduction of the Entomopathogenic Nematode Heterorhabditis bacteriophora

et al. 2001

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The bacterium Photorhabdus luminescens is a symbiont of the entomopathogenic nematode Heterorhabditis bacteriophora. The nematode requires the bacterium for infection of insect larvae and as a substrate for growth and reproduction. The nematodes do not grow and reproduce in insect hosts or on artificial media in the absence of viable P. luminescens cells. In an effort to identify bacterial factors that are required for nematode growth and reproduction, transposon-induced mutants of P. luminescens were screened for the loss of the ability to support growth and reproduction of H. bacteriophora nematodes. One mutant, NGR209, consistently failed to support nematode growth and reproduction. This mutant was also defective in the production of siderophore and antibiotic activities. The transposon was inserted into an open reading frame homologous to Escherichia coli EntD, a 4-phosphopantetheinyl (Ppant) transferase, which is required for the biosynthesis of the catechol siderophore enterobactin. Ppant transferases catalyze the transfer of the Ppant moiety from coenzyme A to a holo-acyl, -aryl, or -peptidyl carrier protein(s) required for the biosynthesis of fatty acids, polyketides, or nonribosomal peptides. Possible roles of a Ppant transferase in the ability of P. luminescens to support nematode growth and reproduction are discussed.Photorhabdus luminescens (Enterobacteriaceae) bacteria are symbiotic with entomopathogenic rhabditid nematodes of the family Heterorhabditidae, with which they cooperate in infecting a wide variety of insect larvae (38, 45; for reviews, see references 25 and 26). The nematode requires P. luminescens for insect pathogenicity (34), while the bacteria depend on the nematodes for transmission between insect prey. The infective juvenile (IJ)-stage nematodes specifically retain symbiotic P. luminescens cells in their gut mucosa, and transmission of the bacteria is a requisite for insect pathogenicity (31,32,34). The nematodes require P. luminescens cells as a substrate for growth and reproduction (2,21,22,30). It was suggested previously that symbiotic P. luminescens cells provide favorable nutritional conditions for Heterorhabditis bacteriophora nematodes to grow and reproduce (45).During prolonged laboratory culture, P. luminescens strains show a tendency to undergo an apparent phase variation phenomenon (8, 9, 36). The native form of the bacteria, termed primary phase, is isolated from the IJ stage of the nematode. The secondary-phase variants appear at high frequency during prolonged culturing, while more rare is the generation of primary-phase cells from secondary phase (6). The secondaryphase cells differ from the primary-phase cells in colony morphology, cell size, and dye uptake characteristics (6, 7, 9, 52). Also, typical primary-phase characteristics such as bioluminescence, pigment synthesis, phospholipase and siderophore activities, and production of intracellular crystalline inclusion proteins are depressed or absent in secondary-phase cells. The mechanism and role of phase variati...

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Section: Resultsmentioning

confidence: 99%

A Phosphopantetheinyl Transferase Homolog Is Essential for Photorhabdus luminescens To Support Growth and Reproduction of the Entomopathogenic Nematode Heterorhabditis bacteriophora

et al. 2001

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“…The heterogeneity in the binding traits of FimHE, FimHK, and FimHS after they are incorporated into their native fimbriae suggests that the restrictive impact of each shaft is distinct. Because FimA, which constitutes Ͼ95% of the fimbrial shaft, is structurally and antigenically heterogeneous among various enterobacteria with sizes ranging from 14 to 22 kDa (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22), the conformational change undergone by FimH is likely to be different in each fimbrial structure.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, isolated FimH mimics many of the mannose-specific binding reactions of type 1 fimbriae (9,10). On the other hand, FimA is the major subunit that makes up Ͼ95% of the fimbrial shaft and is structurally and antigenically heterogeneous among different species (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22). FimH has been crystallized, and the sugar-binding region was mapped to the N-terminal half (residues 1-156) of the molecule, whereas the region that associates with the fimbrial shaft was mapped to the C-terminal half (residues 160 -277) of the FimH molecule (23).…”

mentioning

confidence: 99%

The Distinct Binding Specificities Exhibited by Enterobacterial Type 1 Fimbriae Are Determined by Their Fimbrial Shafts

Duncan

Mann

Cohen

et al. 2005

Journal of Biological Chemistry

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Type 1 fimbriae of enterobacteria are heteropolymeric organelles of adhesion composed of FimH, a mannose-binding lectin, and a shaft composed primarily of FimA. We compared the binding activities of recombinant clones expressing type 1 fimbriae from Escherichia coli, Klebsiella pneumoniae, and Salmonella typhimurium for gut and uroepithelial cells and for various soluble mannosylated proteins. Each fimbria was characterized by its capacity to bind particular epithelial cells and to aggregate mannoproteins. However, when each respective FimH subunit was cloned and expressed in the absence of its shaft as a fusion protein with MalE, each FimH bound a wide range of mannose-containing compounds. In addition, we found that expression of FimH on a heterologous fimbrial shaft, e.g. K. pneumoniae FimH on the E. coli fimbrial shaft or vice versa, altered the binding specificity of FimH such that it closely resembled that of the native heterologous type 1 fimbriae. Furthermore, attachment to and invasion of bladder epithelial cells, which were mediated much better by native E. coli type 1 fimbriae compared with native K. pneumoniae type 1 fimbriae, were found to be dependent on the background of the fimbrial shaft (E. coli versus K. pneumoniae) rather than the background of the FimH expressed. Thus, the distinct binding specificities of different enterobacterial type 1 fimbriae cannot be ascribed solely to the primary structure of their respective FimH subunits, but are also modulated by the fimbrial shaft on which each FimH subunit is presented, possibly through conformational constraints imposed on FimH by the fimbrial shaft. The capacity of type 1 fimbrial shafts to modulate the tissue tropism of different enterobacterial species represents a novel function for these highly organized structures.

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“…Type 3 fimbriae are characterized by their ability to agglutinate tannic acid-treated, but not native, RBCs in a mannose-resistant manner (Gerlach et al, 1989). The commercially available sheep RBCs used in this study were delivered as a glutaraldehyde-treated dry powder, and we speculate that either the drying or the glutaraldehyde treatment exposed type 3 fimbriae receptors on the RBCs that are not present on the surface of native RBCs.…”

Section: Discussionmentioning

confidence: 99%

Klebsiella pneumoniae type 3 fimbriae agglutinate yeast in a mannose-resistant manner

Stahlhut

Struve

Krogfelt

2012

Journal of Medical Microbiology

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Identification and characterization of the genes encoding the type 3 and type 1 fimbrial adhesins of Klebsiella pneumoniae

Cited by 123 publications

References 28 publications

A Phosphopantetheinyl Transferase Homolog Is Essential for Photorhabdus luminescens To Support Growth and Reproduction of the Entomopathogenic Nematode Heterorhabditis bacteriophora

A Phosphopantetheinyl Transferase Homolog Is Essential for Photorhabdus luminescens To Support Growth and Reproduction of the Entomopathogenic Nematode Heterorhabditis bacteriophora

The Distinct Binding Specificities Exhibited by Enterobacterial Type 1 Fimbriae Are Determined by Their Fimbrial Shafts

Klebsiella pneumoniae type 3 fimbriae agglutinate yeast in a mannose-resistant manner

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