A IIIman protein is involved in the transport of glucose, mannose and fructose by oral streptococci

Abstract

We show in this article that the transport of glucose, mannose and fructose by the phosphoenolpyruvate: mannose phosphotransferase system of oral streptococci requires the participation of a protein component that we have called IIIman. This protein was purified from Streptococcus salivarius by chromatography on DEAE-cellulose, DEAE-TSK, hydroxyapatite, and Dyematrex Green A. The purified protein migrated as a 38,900 molecular weight protein on a sodium dodecyl sulfate polyacrylamide gel. However, electrophoretic analysis of phosphoproteins and Western blot experiments indicated the presence in membrane-free cellular extracts of S. salivarius of 2 different forms of IIIman having molecular weights of 38,900 and 35,200. The presence of the high-molecular-weight form of IIIman was observed by immunodiffusion, Western blot and phosphorylation by [32]PEP in S. salivarius, Streptococcus mutans, Streptococcus sobrinus, and Streptococcus lactis but not in Streptococcus faecium, Staphylococcus aureus, Bacillus subtilis and Lactobacillus casei. Antibodies directed against the IIIman of S. salivarius did not react with the IIIman of Escherichia coli.