Identification of Mycoplasma pneumoniae proteins associated with hemadsorption and virulence

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Abstract
Twenty-two mutants of M. pneumoniae spontaneously deficient in hemadsorption were isolated. Examination of mutant protein profiles by 1- and 2-dimensional polyacrylamide gel electrophoresis permitted the grouping of these mutants into 4 classes. The largest class of mutants was deficient in 4 high-MW proteins (215,000, 210,000, 190,000 and 140,000). A 2nd class of mutants lacked 3 proteins previously designated A, B and C (72,000, 85,000 and 37,000, respectively). A single mutant, in addition to lacking proteins A, B and C, was missing a 4th protein of 165,000 MW. The remaining mutants exhibited protein profiles apparently identical to that of the wild-type strain. All mutant strains attached to the respiratory epithelium of hamster tracheal rings in vitro at reduced levels; however, mutants lacking proteins A, B and C recognized only neuraminidase-insensitive receptors. None of the mutants tested produced detectable pneumonia in intranasally inoculated hamsters, although 1 mutant class demonstrated low-level survival in vivo.