Pseudomonas aeruginosa strains possess specific adhesins for laminin.

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Pseudomonas aeruginosa is a major human pathogen known to infect tissues that have been previously damaged in some way. In wounded human respiratory tissues, P. aeruginosa cells were found attached to exposed basement membranes following epithelial denudation, suggesting that the affinity for extracellular matrix proteins may account for the bacterium's opportunistic character. By using microtiter wells coated with different P. aeruginosa strains, we demonstrated that laminin binds to both colonizing bacterial strains, isolated from asymptomatic carriers, and strains isolated from infected patients. Binding of soluble laminin to piliated P. aeruginosa PAK and to the nonpiliated isogenic mutant PAK/p--was shown to be saturable. Binding of laminin to the piliated PAK strain was not different from binding to th nonpiliated PAK/p--strain but was significantly higher than binding to the avirulent, nonpiliated PAK-N1 rpoN mutant. By transmission electron microscopy, we localized the laminin-binding sites on a loose material in the outermost layer of the bacteria. Western immunoblotting results suggested that 57- and 59-kDa nonpilus adhesins from the microbial outer membranes account for the binding of P. aeruginosa to laminin. We speculate that bacterial affinity for laminin may be of biological significance in the pathogenesis of P. aeruginosa infection of injured tissues.

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