Bacteriophage lambda adsorbs to its Escherichia coli K-12 host by interacting with LamB, a
maltose- and
maltodextrin-specific
porin of the outer membrane. LamB also serves as a receptor for several other bacteriophages. Lambda
DNA requires, in addition to LamB, the presence of two bacterial cytoplasmic
integral membrane proteins for penetration, namely, the IIC(Man) and IID(Man)
proteins of the E. coli
mannose transporter, a member of the
sugar-specific
phosphoenolpyruvate:sugar phosphotransferase system (PTS). The PTS transporters for
mannose of E. coli, for
fructose of Bacillus subtilis, and for
sorbose of Klebsiella pneumoniae were shown to be highly similar to each other but significantly different from other PTS transporters. These three
enzyme II complexes are the only ones to possess distinct IIC and IID transmembrane
proteins. In the present work, we show that the
fructose-specific
permease encoded 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
infection. In contrast, a series of other bacteriophages, also using the LamB
protein as a
cell surface receptor, do not require the
mannose transporter for
infection.