Characterization of the Pseudomonas aeruginosa pilus adhesin: confirmation that the pilin structural protein subunit contains a human epithelial cell-binding domain

Irvin, Randall T.; Doig, P.; Lee, K K; Sastry, P A; Paranchych, W.; Todd, Tom; Hodges, Robert S.

doi:10.1128/iai.57.12.3720-3726.1989

Cited by 98 publications

(53 citation statements)

References 33 publications

(30 reference statements)

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“…In this study, we examine the initial event of P. aeruginosa biofilm formation on stainless steel, namely the binding of the organism to the surface. We demonstrate that type IV pili specifically mediate binding to stainless steel and that the interaction with steel involves the previously identified pilin C-terminal epithelial cell receptor binding domain (Irvin et al ., 1989). This synthetic peptide receptor binding domain was observed to bind to steel with high affinity and prevent binding of a variety of P. aeruginosa strains to steel.…”

Section: Introductionsupporting

confidence: 57%

The Pseudomonas aeruginosa type IV pilin receptor binding domain functions as an adhesin for both biotic and abiotic surfaces

Giltner

Schaik

Audette

et al. 2005

Molecular Microbiology

125

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SummaryPseudomonas aeruginosa readily binds to stainless steel and other abiotic surfaces, causing major problems in both the medical and food industries. In this study, we show that P. aeruginosa binds to abiotic surfaces in a concentration-dependent, saturable manner during the initial stages of biofilm formation. P. aeruginosa type IV pili mediate binding to stainless steel as a pilus-deficient strain does not bind to steel, purified type IV pili bound in a concentration-dependent, saturable manner, and purified pili competitively inhibited whole cell binding. PAK pili can also bind polystyrene and polyvinylchloride in a concentrationdependant and saturable manner.

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Section: Introductionsupporting

confidence: 57%

The Pseudomonas aeruginosa type IV pilin receptor binding domain functions as an adhesin for both biotic and abiotic surfaces

Giltner

Schaik

Audette

et al. 2005

Molecular Microbiology

125

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“…This may be cell specific. For example, if asialo-GM1, to which the pilin binds [24,25,33], varies in B A Fig. 2.…”

Section: Discussionmentioning

confidence: 99%

Pseudomonas aeruginosa injects type III effector ExoS into epithelial cells through the function of type IV pili

et al. 2015

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a b s t r a c tTranslocation of Pseudomonas aeruginosa through epithelial tissues can cause sepsis. Here, we examined whether P. aeruginosa penetrates epithelial cell layers using type IV pili (TFP). Deletion of TFP (pilA) did not affect association with Caco-2 cells, although it decreased penetration through, and disruption of, Caco-2 cell monolayers. We found that TFP are necessary for injection of the type III effector ExoS, which impairs defense against P. aeruginosa penetration, into host cells. Deletion of pilA attenuated oral infection in silkworms. We conclude that P. aeruginosa injects ExoS into cells through the function of TFP, enabling penetration of epithelial barriers.

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“…Pili, also known as fimbriae, are rod-like proteinaceous structures 2-1 0 nm in diameter and up to several micrometres in length. While some fimbriae are composed of multiple proteins, including a specialized 'tip adhesin' (Lindberg etal., 1987;Rude1 etal., 1995), others are composed of a single pilin subunit which acts as structural protein as well as an adhesin (Irvin et al, 1989;Lee etal., 1994).…”

Section: Introductionmentioning

confidence: 99%

A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilus

Stone

Zhang

Carlson

et al. 1996

Molecular Microbiology

260

195

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Enteropathogenic Escherichia coli (EPEC) adhere to epithelial cells in microcolonies, a pattern termed localized adherence (LA). LA is dependent upon the presence of 50-70 MDa plasmids, termed EPEC adherence factor (EAF) plasmids. Expression of an EAF plasmid-encoded type IV fimbria, the bundle-forming pilus (BFP), is associated with the LA phenotype. TnphoA insertions in bfpA, the gene encoding the major structural subunit of the BFP, abolish LA. While bfpA::TnphoA mutants cannot be complemented for LA by plasmids carrying the bfpA gene alone in trans, this work shows that they can be complemented by plasmids carrying the bfpA gene, as well as approximately 10 kb of downstream sequence, suggesting that such mutations have polar effects on downstream genes. The identification and characterization of a cluster of 13 genes immediately downstream of bfpA are described. The introduction into a laboratory Escherichia coli strain of a plasmid containing these 14 bfp gene cluster genes, along with pJPN14, a plasmid containing another fragment derived from the EAF plasmid, confers LA ability and BFP biogenesis. However, when a mutation is introduced into the last gene of the bfp cluster, neither LA nor BFP biogenesis is conferred. This work also provides evidence to show that the fragment cloned in pJPN14 encodes a factor(s) which results in increased levels of the pilin protein. Finally, it is shown that expression of the 14 genes in the bfp cluster from an IPTG-inducible promoter, in the absence of pJPN14, is sufficient to reconstitute BFP biogenesis in a laboratory E. coli strain, but is insufficient for LA. This is the first report demonstrating the reconstitution of a type IV pilus in a laboratory E. coli strain with a defined set of genes. The BFP system should prove to be a useful model for studying the molecular mechanisms of type IV pilus biogenesis.

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Characterization of the Pseudomonas aeruginosa pilus adhesin: confirmation that the pilin structural protein subunit contains a human epithelial cell-binding domain

Cited by 98 publications

References 33 publications

The Pseudomonas aeruginosa type IV pilin receptor binding domain functions as an adhesin for both biotic and abiotic surfaces

The Pseudomonas aeruginosa type IV pilin receptor binding domain functions as an adhesin for both biotic and abiotic surfaces

Pseudomonas aeruginosa injects type III effector ExoS into epithelial cells through the function of type IV pili

A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilus

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