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The mechanism(s) of interaction between Mycoplasma pulmonis and eucaryotic cells was studied by adherence to and hemagglutination of erythrocytes. Simple and complex carbohydrates and glycoproteins were unable to inhibit either adherence or hemagglutination, indicating that neither was a lectin activity. Both interactions appeared to be hydrophobic due to their requirement for salt and their sensitivity to temperature. Hemagglutination, but not adherence, was inhibited by both trypsin and glutaraldehyde treatment of the mycoplasma, suggesting that adherence and hemagglutination are qualitatively different. The erythrocyte receptor sites for the two activities were also separable since hemagglutination, but not adherence, required trypsinization of erythrocytes. The hemagglutinin was shown to be an integral mycoplasma component and not a broth contaminant. Once removed, hemagglutinating activity could not be replenished by incubation in serum or broth at 4 degrees C, but could be regenerated during protein synthesis under nonreplicative conditions. Thus, a mycoplasma membrane protein was detected which was capable of interacting with opposing membrane surfaces through hydrophobic interactions. Consequently, a multiphasic model of M. pulmonis-eucaryotic cell interactions was proposed.

Multiphasic interactions of Mycoplasma pulmonis with erythrocytes defined by adherence and hemagglutination