Arrangement of bacteriophage lambda receptor protein (LamB) in the cell surface of Escherichia coli: a reconstitution study.

The LamB protein purified in a solution of sodium dodecyl sulfate was assembled into an ordered hexagonal lattice structure with a lattice constant of about 7.8 nm in the presence of lipopolysaccharide. The LamB alone formed aggregates with some lattice structure. However, the regularity of the lattice was only maintained within a very small area. An ordered hexagonal lattice was also formed when the wild-type lipopolysaccharide was replaced by heptoseless lipopolysaccharide, lipid A, and even fatty acid. However, the lattice constants were appreciably smaller than that with the wild-type lipopolysaccharide. The results suggest that the heptose-containing polysaccharide region, as well as the fatty acid region, are involved in the interaction with the LamB protein. The LamB-lipopolysaccharide lattice was preferably formed on the peptidoglycan layer when the lipoprotein was covalently bound to this layer. These results indicate that the molecular arrangement of the LamB protein in the outer membrane is similar to that of matrix proteins, OmpC and OmpF, which exist as trimers. The ordered hexagonal lattice was active in the receptor function for lambda, resulting in phage adsorption and deoxyribonucleic acid ejection. Thus, this reconstitution system should provide a useful means of studying the mechanism of lambda infection.