Interaction of bacteriophage K10 with its receptor, the lamB protein of Escherichia coli
نویسندگان
چکیده
منابع مشابه
Interaction of Bacteriophage λ with Its E. coli Receptor, LamB
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 λ and its host Esch...
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The majority of bacterial viruses are bacteriophages bearing a tail that serves to recognise the bacterial surface and deliver the genome into the host cell. Infection is initiated by the irreversible interaction between the viral receptor binding protein (RBP) and a receptor at the surface of the bacterium. This interaction results ultimately in the phage DNA release in the host cytoplasm. Pha...
متن کاملThe protein interaction network of bacteriophage lambda with its host, Escherichia coli.
Although most of the 73 open reading frames (ORFs) in bacteriophage λ have been investigated intensively, the function of many genes in host-phage interactions remains poorly understood. Using yeast two-hybrid screens of all lambda ORFs for interactions with its host Escherichia coli, we determined a raw data set of 631 host-phage interactions resulting in a set of 62 high-confidence interactio...
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Background and Aims: Bacteriophages are mandatory bacterial parasites that are harmless to human and animal, which are used by dipping or spraying in food as natural antimicrobial agents. The use of these methods leads to wasting or trapping of phage in food, but its immobilization on the polymer surface facilitates the contact of phage with the host cell at the food surface. Therefore, the aim...
متن کاملThe 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.
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 anti...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1979
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.140.2.680-686.1979