The heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap

Abstract We examined the penicillin-binding proteins (PBPs) of certain field strains of Streptococcus suis , as well as those from laboratory variants having different degrees of resistance to penicillin. Results indicated that (i) S. suis possesses three distinct groups of PBPs, arbitrarily named here PBP 1, PBP 2, and PBP 3, with approximate molecular weights of 97, 82, and 45 kDa respectively; (ii) PBP profiles of field strains of S. suis having different MICs (≤ 0.03 to 16.0 μg/ml) were not uniform (PBP 2 being difficult to detect in strains whose MICs exceeded 0.10 μg/ml, and PBP 3 which exhibited shifts in molecular weight of approximately 5 kDa); (iii) laboratory variant PBPs 1 and 2 showed decreased affinity for penicillin as compared to the parent strain in antibiotic competition experiments, even though the PBP profiles of both were similar. We suggest that PBP modifications (altered molecular weight and/or decreased affinity for penicillin) are involved in the mechanism of resistance to penicillin by S. suis .