Properties of PSE-2 beta-lactamase and genetic basis for its production in Pseudomonas aeruginosa.

The properties of PSE-2 beta-lactamase have been examined by using two new PSE-2-producing plasmids, pMG33 and pMG74, as well as plasmid R151, found in Pseudomonas aeruginosa. PSE-2 beta-lactamase resembled other PSE enzymes in activity against carbenicillin, but it also resembled OXA enzymes, such as OXA-1, in rapid hydrolysis of oxacillin, cloxacillin, and methicillin and in inhibition by sodium chloride but not by cloxacillin. Antisera that inactivated TEM-1, TEM-2, OXA-1, or PSE-1 and PSE-4 beta-lactamase failed to cross-react with PSE-2, which thus appears to be immunologically distinct. The plasmids determining PSE-2 varied in geographical origin, size, transfer proficiency, and incompatibility specificity, but all determined resistance to carbenicillin, gentamicin, kanamycin, streptomycin, spectinomycin, sulfonamide, and tobramycin. From a pUZ8-R151 recombinant plasmid in Escherichia coli, the PSE-2 beta-lactamase gene could be transposed to a second plasmid in a 6.4-megadalton unit together with resistance to gentamicin, kanamycin, streptomycin, spectinomycin, sulfonamide, and tobramycin. Transposition was recA independent. We propose the designation Tn1404 for this unit, which, like transposons carrying OXA-1, PSE-1, PSE-4, and some transposons determining TEM-1, includes genes for beta-lactam, aminoglycoside, and sulfonamide resistance.