THE LEVANASE OPERON OF BACILLUS-SUBTILIS EXPRESSED IN ESCHERICHIA-COLI CAN SUBSTITUTE FOR THE MANNOSE PERMAESE IN MANNOSE UPTAKE AND BACTERIOPHAGE-LAMBDA INFECTION

Bacteriophage lambda adsorbs to its Escherichia coli K-12 host by inte racting with LamB, a maltose-and maltodextrin-specific porin of the ou ter membrane. LamB also serves as a receptor for several other bacteri ophages. Lambda DNA requires, in addition to LamB, the presence of two bacterial cytoplasmic integral membrane proteins for penetration, nam ely, the IICMan and IIDMan proteins of the E. coli mannose transporter , a member of the sugar-specific phosphoenolpyruvate:sugar phosphotran sferase system (PTS). The PTS transporters for mannose of E. coli, for fructose of Bacillus subtilis, and for sorbose of Klebsiella pneumoni ae were shown to be highly similar to each other but significantly dif ferent from other PTS transporters. These three enzyme II complexes ar e the only ones to possess distinct IIC and IID transmembrane proteins . In the present work, we show that the fructose-specific permease enc oded by the levanase operon of B. subtilis is inducible by mannose and allows mannose uptake in B. subtilis as well as in E. coli. Moreover, we show that the B. subtilis permease can substitute for the E. coli mannose permease cytoplasmic membrane components for phage lambda infe ction. In contrast, a series of other bacteriophages, also using the L amB protein as a cell surface receptor, do not require the mannose tra nsporter for infection.