Abstract
The role of lipopolysaccharide in the receptor function for bacteriophage T4 was studied by using Escherichia coli K-12 B23 strain. The receptor activity for T4 was monitored by inhibiting phage adsorption by saccharides that mimic sugars located at the receptor site on LPS. Coliphage T4 adsorbed to intact cells and acetone-ether treated cells, but was not adsorbed to heat-treated cells. The adsorption of phage T4 to acetone and ether-treated cells was inhibited by glucose derivatives like N-acetylglucosamine and α -methylglucoside but was not inhibited by maltose. The inhibition effect of the N-acetylglucosamine and α – methylglucoside is consistent with the observation that T4 adsorbs to the two glucoses on Cterminus of LPS’s R-core in E. coli B23. However, wild type T4 is also capable of absorbing to E. coli B23 via OmpC, a major outer membrane protein, and phage adsorption via this protein might influence results obtained. With this confounding factor, a conclusion cannot – be stated confidently until the adsorption is simplified by using OmpC mutants or OmpC- E. coli.