Penicillin-binding proteins in Proteus species

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Abstract
Penicillin-binding proteins in 3 species of Proteus, P. mirabilis, P. morganii and P. rettgeri, were investigated by sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis. Penicillin-binding proteins in these Proteus sp. were compared with those in Escherichia coli K-12. An approximate correlation between penicillin-binding proteins in E. coli and those in Proteus sp. was shown by several criteria: electrophoretic mobilities; affinities of several .beta.-lactam antibiotics which show characteristic patterns of binding to penicillin-binding proteins in E. coli; relation between affinities of antibiotics to the proteins and effects on morphological changes in Proteus sp.; location of .beta.-lactamase activity among penicillin-binding proteins and thermostability. The electrophoretic mobilities and several other characteristics of penicillin-binding proteins among the Proteus sp. examined were similar from species to species and differed only slightly from those of E. coli.