Open AccessBacteriophage lambda receptor site on the Escherichia coli K-12 LamB protein
Author(s) -
Kalle Gehring,
Alain Charbit,
E Brissaud,
Maurice Hofnung
Publication year - 1987
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.169.5.2103-2106.1987
Subject(s) - biology , bacteriophage , periplasmic space , lambda phage , escherichia coli , amino acid , missense mutation , peptide sequence , mutation , biochemistry , microbiology and biotechnology , genetics , gene
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.