Open AccessCharacterization of the interactions between Escherichia coli receptors, LPS and OmpC, and bacteriophage T4 long tail fibers
Author(s) -
Washizaki Ayaka,
Yonesaki Tetsuro,
Otsuka Yuichi
Publication year - 2016
Publication title -
microbiologyopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.881
H-Index - 36
ISSN - 2045-8827
DOI - 10.1002/mbo3.384
Subject(s) - bacteriophage , escherichia coli , mutant , strain (injury) , receptor , bacterial outer membrane , lipopolysaccharide , fiber , biology , microbiology and biotechnology , chemistry , gene , biophysics , biochemistry , anatomy , organic chemistry , endocrinology
Bacteriophages have strict host specificity and the step of adsorption is one of key factors for determining host specificity. Here, we systematically examined the interaction between the Escherichia coli receptors lipopolysaccharide ( LPS ) and outer membrane protein C (OmpC), and the long tail fibers of bacteriophage T4. Using a variety of LPS mutants, we demonstrated that T4 has no specificity for the sugar sequence of the outer core (one of three LPS regions) in the presence of OmpC but, in the absence of OmpC, can adsorb to a specific LPS which has only one or two glucose residues without a branch. These results strengthen the idea that T4 adsorbs to E. coli via two distinct modes, OmpC‐dependent and OmpC‐independent, suggested by previous reports (Prehm et al. 1976; Yu and Mizushima 1982). Isolation and characterization of the T4 mutants Nik ( N o i nfection to K ‐12 strain), Nib ( N o i nfection to B strain), and Arl ( a ltered r ecognition of L PS ) identified amino acids of the long tail fiber that play important roles in the interaction with OmpC or LPS , suggesting that the top surface of the distal tip head domain of T4 long tail fibers interacts with LPS and its lateral surface interacts with OmpC.