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

The lambda receptor protein (LamB) was assembled into an ordered hexagonal lattice structure with a lattice constant of about 7.8 nm in the presence of lipopolysaccharide. Both the heptose-containing polysaccharide region and the fatty acid region are suggested to be involved in the interaction with LamB. The lattice structure was preferably formed on the peptidoglycan layer when the lipoprotein was covalently bound to this layer. In the presence of chloroform, the ordered hexagonal lattice structure was active in the receptor function for lambda, resulting in phage adsorption and DNA ejection.