title: Interaction of bacteriophage l with its E. coli receptor, LamB.
abstract: The initial step of viral infection is the binding of a virus onto the host cell surface. This first viral-host interaction would determine subsequent infection steps and the fate of the entire infection process. A basic understating of the underlining mechanism of initial virus-host binding is a prerequisite for establishing the nature of viral infection. Bacteriophage &#955; and its host Escherichia coli serve as an excellent paradigm for this purpose. &#955; phages bind to specific receptors, LamB, on the host cell surface during the infection process. The interaction of bacteriophage &#955; with the LamB receptor has been the topic of many studies, resulting in wealth of information on the structure, biochemical properties and molecular biology of this system. Recently, imaging studies using fluorescently labeled phages and its receptor unveil the role of spatiotemporal dynamics and divulge the importance of stochasticity from hidden variables in the infection outcomes. The scope of this article is to review the present state of research on the interaction of bacteriophage &#955; and its E. coli receptor, LamB.
authors.affiliation: Department of Biochemistry and Molecular Pharmacology, NYU Medical School, 550 First Avenue, New York, NY 10016, USA. sujoy.chatterjee@nyumc.org
authors.forename: Sujoy
authors.initials: S
authors.lastname: Chatterjee
authors.forename: Eli
authors.initials: E
authors.lastname: Rothenberg
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010582:Bacteriophage lambda / Q000502:physiology*; D004926:Escherichia coli / Q000378:metabolism* / Q000821:virology*; D008954:Models, Biological; D018272:Porins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D011991:Receptors, Virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D053585:Virus Attachment
chemical_list: D001425:Bacterial Outer Membrane Proteins; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins