Interaction of the receptor binding domains of Pseudomonas aeruginosa pili strains PAK, PAO, KB7 and P1 to a cross-reactive antibody and receptor analog: implications for synthetic vaccine design

Campbell, A. Patricia; Wong, Wah Y.; Houston, Michael J.; Schweizer, Frank; Cachia, Paul J.; Irvin, Randall T.; Hindsgaul, Ole; Hodges, Robert S.; Sykes, Brian D.

doi:10.1006/jmbi.1996.0871

Cited by 34 publications

(43 citation statements)

References 66 publications

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“…2) that has been implicated as the binding domain for the eukaryotic glycolipid asialoGM 1 (aGM 1 ). Previous studies of receptor binding using peptide mimics of the C-terminal DSLs of group II pilins from strains PAK, PAO1 and KB7 and the group I pilin from strain P1 showed that all peptides bound to aGM 1 despite differences in amino acid composition (Campbell et al, 1997). In contrast, a recent study (Schroeder et al, 2001) using whole, piliated cells showed that a number of clinical isolates (of undefined pilin type), as well as laboratory strains including PAO1 and PAK, did not demonstrate differences in binding to host cells in the presence or absence of exogenously added aGM 1 receptor.…”

Section: Discussionmentioning

confidence: 99%

Significant differences in type IV pilin allele distribution among Pseudomonas aeruginosa isolates from cystic fibrosis (CF) versus non-CF patients

et al. 2004

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Type IV pili (TFP) are important colonization factors of the opportunistic pathogen Pseudomonas aeruginosa, involved in biofilm formation and attachment to host cells. This study undertook a comprehensive analysis of TFP alleles in more than 290 environmental, clinical, rectal and cystic fibrosis (CF) isolates of P. aeruginosa. Based on the results, a new system of nomenclature is proposed, in which P. aeruginosa TFP are divided into five distinct phylogenetic groups. Each pilin allele is stringently associated with characteristic, distinct accessory genes that allow the identification of the allele by specific PCR. The invariant association of the pilin and accessory genes implies horizontal transfer of the entire locus. Analysis of pilin allele distribution among isolates from various sources revealed a striking bias in the prevalence of isolates with group I pilin genes from CF compared with non-CF human sources (P<0?0001), suggesting this particular pilin type, which can be post-translationally modified by glycosylation via the action of TfpO (PilO), may confer a colonization or persistence advantage in the CF host. This allele was also predominant in paediatric CF isolates (29 of 43; 67?4 %), showing that this bias is apparent early in colonization. Group I pilins were also the most common type found in environmental isolates tested. To the authors' knowledge, this is the first example of a P. aeruginosa virulence factor allele that is strongly associated with CF isolates.

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Section: Discussionmentioning

confidence: 99%

Significant differences in type IV pilin allele distribution among Pseudomonas aeruginosa isolates from cystic fibrosis (CF) versus non-CF patients

et al. 2004

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“…The presence of PilA in the B. exovorus JSS pilus was inferred using antibodies raised against the periplasmic predator B. bacteriovorus 109J's PilA, as the antisera inhibited attachment of B. exovorus JSS to prey cells (Mahmoud and Koval, 2010). Previous studies in Pseudomonas aeruginosa have shown that PilA antibodies were able to bind to a PilA C-terminal domain of variable sequence, suggesting that conformation and not sequence was important for antibody recognition (Campbell et al, 1997). Different predatory strategies may imply different anchoring mechanisms: in B. bacteriovorus, the predator needs to reach the cytoplasmic membrane in order to penetrate its prey (Abram et al, 1974), a process that may be mediated by type IV pili (Evans et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

In and out: an analysis of epibiotic vs periplasmic bacterial predators

et al. 2013

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Bdellovibrio and like organisms (BALO) are obligate predators of Gram-negative bacteria, belonging to the a-and d-proteobacteria. BALO prey using either a periplasmic or an epibiotic predatory strategy, but the genetic background underlying these phenotypes is not known. Here we compare the epibiotic Bdellovibrio exovorus and Micavibrio aeruginosavorus to the periplasmic B. bacteriovorus and Bacteriovorax marinus. Electron microscopy showed that M. aeruginosavorus, but not B. exovorus, can attach to prey cells in a non-polar manner through its longitudinal side. Both these predators were resistant to a surprisingly high number of antibiotic compounds, possibly via 26 and 19 antibiotic-resistance genes, respectively, most of them encoding efflux pumps. Comparative genomic analysis of all the BALOs revealed that epibiotic predators have a much smaller genome (ca. 2.5 Mbp) than the periplasmic predators (ca. 3.5 Mbp). Additionally, periplasmic predators have, on average, 888 more proteins, at least 60% more peptidases, and one more rRNA operon. Fifteen and 219 protein families were specific to the epibiotic and the periplasmic predators, respectively, the latter clearly forming the core of the periplasmic 'predatome', which is upregulated during the growth phase. Metabolic deficiencies of epibiotic genomes include the synthesis of inosine, riboflavin, vitamin B6 and the siderophore aerobactin. The phylogeny of the epibiotic predators suggests that they evolved by convergent evolution, with M. aeruginosavorus originating from a non-predatory ancestor while B. exovorus evolved from periplasmic predators by gene loss.

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“…To explain how D regions with diverse sequences can provide similar functions, their adhesive properties were attributed to main chain-rather than side chain-based interactions (172). Those data led to a focus on development of anti-P. aeruginosa vaccines containing peptides corresponding to the D region (71,72,75,162,216). Newer information showing that the minor pilins are present in sheared pilus fractions (154,416) and that the orthologous PilC1 or PilC2 (Neisseria and Kingella) and PilY1 (Pseudomonas) proteins are potentially pilus associated and required for adherence to-and manipulation of-the host (174,204,217,288,289,384) suggests that additional studies are needed to unequivocally identify all T4aP adhesins.…”

Section: Figmentioning

confidence: 99%

Type IV Pilin Proteins: Versatile Molecular Modules

Giltner

Nguyen

Burrows

2012

Microbiol Mol Biol Rev

412

519

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SUMMARYType IV pili (T4P) are multifunctional protein fibers produced on the surfaces of a wide variety of bacteria and archaea. The major subunit of T4P is the type IV pilin, and structurally related proteins are found as components of the type II secretion (T2S) system, where they are called pseudopilins; of DNA uptake/competence systems in both Gram-negative and Gram-positive species; and of flagella, pili, and sugar-binding systems in the archaea. This broad distribution of a single protein family implies both a common evolutionary origin and a highly adaptable functional plan. The type IV pilin is a remarkably versatile architectural module that has been adopted widely for a variety of functions, including motility, attachment to chemically diverse surfaces, electrical conductance, acquisition of DNA, and secretion of a broad range of structurally distinct protein substrates. In this review, we consider recent advances in this research area, from structural revelations to insights into diversity, posttranslational modifications, regulation, and function.

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Interaction of the receptor binding domains of Pseudomonas aeruginosa pili strains PAK, PAO, KB7 and P1 to a cross-reactive antibody and receptor analog: implications for synthetic vaccine design

Cited by 34 publications

References 66 publications

Significant differences in type IV pilin allele distribution among Pseudomonas aeruginosa isolates from cystic fibrosis (CF) versus non-CF patients

Significant differences in type IV pilin allele distribution among Pseudomonas aeruginosa isolates from cystic fibrosis (CF) versus non-CF patients

In and out: an analysis of epibiotic vs periplasmic bacterial predators

Type IV Pilin Proteins: Versatile Molecular Modules

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