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PMID:10629200
| Citation |
Wang, J, Hofnung, M and Charbit, A (2000) 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. J. Bacteriol. 182:508-12 |
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| 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. |
| Links | |
| Keywords |
ATP-Binding Cassette Transporters; Bacterial Proteins/metabolism; Bacteriophage lambda/metabolism; Blotting, Western; Carrier Proteins/metabolism; Enzyme-Linked Immunosorbent Assay; Escherichia coli/metabolism; Escherichia coli/virology; Escherichia coli Proteins; Maltose/metabolism; Maltose-Binding Proteins; Membrane Proteins/metabolism; Monosaccharide Transport Proteins; Protein Sorting Signals/metabolism; Surface Properties; Viral Tail Proteins/metabolism |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0019062: virion attachment to host cell |
ECO:0000314: |
P |
Figure 4 shows that the when the Tail Fiber Protein in Phage Lambda was inhibited, binding to LamB, the receptor at the surface of Escherichia coli K-12, was greatly reduced. |
complete | ||||
| GO:0046813: receptor-mediated virion attachment to host cell |
ECO:0000315: |
P |
Figure 4 shows that the when the Tail Fiber Protein in Phage Lambda was inhibited, binding to LamB, the receptor at the surface of Escherichia coli K-12, was greatly reduced. |
complete | ||||
Notes
See also
References
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