The C-terminal portion of the tail fiber protein of bacteriophage lambda is responsible for binding to LamB, its receptor at the surface of Escherichia coli K-12.

Abstract:

:Bacteriophage lambda adsorbs to its Escherichia coli K-12 host by interacting with LamB, its cell-surface receptor. We fused C-terminal portions of J, the tail fiber protein of lambda, to maltose-binding protein. Solid-phase binding assays demonstrated that a purified fusion protein comprising only the last 249 residues of J could bind to LamB trimers and inhibited recognition by anti-LamB antibodies. Electron microscopy further demonstrated that the fusion protein could also bind to LamB at the surface of intact cells. This interaction prevented lambda adsorption but affected only partially maltose uptake.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Wang J,Hofnung M,Charbit A

doi

10.1128/jb.182.2.508-512.2000

keywords:

subject

Has Abstract

pub_date

2000-01-01 00:00:00

pages

508-12

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

182

pub_type

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