Bacteriophage lambda receptor site on the Escherichia coli K-12 LamB protein.
We have analyzed eight new phage-resistant missense mutations in lamB. These mutations identify five new amino acid residues essential for phage lambda adsorption. Two mutations at positions 245 and 382 affect residues which were previously identified, but lead to different amino acid changes. Three mutations at residues 163, 164, and 250 enlarge and confirm previously proposed phage receptor sites. Two different mutations at residue 259 and one at 18 alter residues previously suggested as facing the periplasmic face. The mutation at residue 18 implicates for the first time the amino-terminal region of the LamB protein in phage adsorption. The results are discussed in terms of the topology of the LamB protein.
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism; D010582:Bacteriophage lambda / Q000378:metabolism*; D001665:Binding Sites; D002462:Cell Membrane / Q000648:ultrastructure; D004926:Escherichia coli / Q000235:genetics*; D009154:Mutation; D018272:Porins; D011991:Receptors, Virus / Q000235:genetics / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins