Aminoglycoside resistance (AMGr) in Pseudomonas aeruginosa is most commonly due to a membrane permeability factor. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of outer membrane proteins (OMPs) from AMGr strains of P. aeruginosa (resistant to tobramycin, gentamicin, and amikacin) revealed a unique OMP of 42 kilodaltons (kDa) when compared with aminoglycoside-susceptible strains of P. aeruginosa. A monoclonal antibody (MAb) to an AMGr strain of P. aeruginosa was prepared and used to study AMGr. This MAb, PS1, recognized a unique OMP of 42 kDa present primarily in AMGr strains. MAb PS1 had a binding sensitivity of 83% (n = 46), for AMGr P. aeruginosa, and a specificity of 85% (n = 36), as determined by immunoblot assay. This MAb may be useful for investigating the basis of AMGr in P. aeruginosa.
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Norris et al. (1988) studied this question.
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