2005
DOI: 10.1111/j.1365-2958.2005.05002.x
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The Pseudomonas aeruginosa type IV pilin receptor binding domain functions as an adhesin for both biotic and abiotic surfaces

Abstract: 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 pur… Show more

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Cited by 130 publications
(71 citation statements)
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“…In P. aeruginosa, this subdomain has been the subject of intense research focus due to data implicating it in the adhesive function of T4P. 35,36 Recent evidence from our group showed that mutation of either Cys residue involved in disulfide bond formation to Ala prevents pilus assembly altogether, 13 suggesting that the configuration of the disulfide loop is essential for recognition by the pilus assembly system or for the inter-subunit interactions needed for stable pilus formation. In the process of preparing SeMet-labeled protein, we found that expression of PilA 0594 in a methionineauxotrophic strain of E. coli (B384) with a typical reducing cytoplasm resulted in low yields of soluble protein that subsequently precipitated, suggesting that the protein was not correctly folded.…”
Section: Resultsmentioning
confidence: 97%
“…In P. aeruginosa, this subdomain has been the subject of intense research focus due to data implicating it in the adhesive function of T4P. 35,36 Recent evidence from our group showed that mutation of either Cys residue involved in disulfide bond formation to Ala prevents pilus assembly altogether, 13 suggesting that the configuration of the disulfide loop is essential for recognition by the pilus assembly system or for the inter-subunit interactions needed for stable pilus formation. In the process of preparing SeMet-labeled protein, we found that expression of PilA 0594 in a methionineauxotrophic strain of E. coli (B384) with a typical reducing cytoplasm resulted in low yields of soluble protein that subsequently precipitated, suggesting that the protein was not correctly folded.…”
Section: Resultsmentioning
confidence: 97%
“…Tfp are well-known for facilitating twitching motility in the model opportunistic pathogen Pseudomonas aeruginosa (13). In hostmicrobe interactions, Tfp mediate biofilm formation in P. aeruginosa (14,15) and host colonization in the human pathogen Moraxella catarrhalis (16). Moreover, the importance of Tfp in plant-pathogen interactions is demonstrated in Xylella fastidiosa, where they help in the spread of the pathogen through grapevines (17).…”
mentioning
confidence: 99%
“…These organelles mediate bacterial adhesion to surfaces as diverse as stainless steel (4) and host cells (1), a property that is tightly linked to their ability to promote the formation of adhesive 3D microcolonies by mediating interbacterial interactions (5,6). Tfp are therefore one of the most widespread virulence factors in bacteria and play a key role in infection in several human pathogens, including our working model Neisseria meningitidis.…”
mentioning
confidence: 99%