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Interaction of bacteriophage K10 with its receptor, the lamB protein of Escherichia coli
Abstract:
The lamB protein of Escherichia coli was initially recognized as the receptor for bacteriophage lambda. It is now shown also to constitute the receptor for phage K10. The lamB protein interacts with phage K10 in vitro, but this interaction does not lead to phage inactivation. Most lambda-resistant labB mutants are also resistant to K10, and vice versa. However, a significant proportion of the mutants resistant to one of the phages is sensitive to the other. Nineteen K10-resistant lambda-sensitive mutants have been studied. Only six of them produce a lamB protein which seems totally unimpaired in its ihe same deletion interval of the lamB gene. The corresponding region of the lamB polypeptide must be specifically involved in the interaction with phage K10. An unusual pattern of K10 host range mutants has been obtained; two calsses of such mutants could be defined, growing on two distinct classes of K10-resistant lamB mutants.
Insights
The Escherichia coli lamB protein serves as a receptor for both bacteriophage lambda and phage K10. Mutations affecting lamB can confer resistance to one or both phages, revealing specific interaction sites for K10.
Area of Science:
- Microbiology
- Molecular Biology
- Virology
Background:
- The lamB protein in Escherichia coli is a known receptor for bacteriophage lambda.
- The role of lamB in bacteriophage K10 infection has not been fully elucidated.
Purpose of the Study:
- To investigate the role of the lamB protein as a receptor for bacteriophage K10.
- To identify specific regions of the lamB protein involved in phage K10 interaction.
Main Methods:
- Bacteriophage resistance assays using lamB mutants.
- In vitro interaction studies between lamB protein and phage K10.
- Analysis of host range mutants of phage K10.
Main Results:
- Escherichia coli lamB protein functions as a receptor for both bacteriophage lambda and phage K10.
- Most lambda-resistant lamB mutants are also resistant to K10, but a significant proportion shows differential resistance.
- Specific regions within the lamB polypeptide are crucial for phage K10 interaction, distinct from lambda interaction sites.
- Phage K10 exhibits unusual host range mutant patterns, correlating with specific lamB mutations.
Conclusions:
- The lamB protein mediates entry for both bacteriophage lambda and K10.
- Distinct domains of the lamB protein are involved in binding and/or entry for each phage.
- Further characterization of K10 host range mutants can refine our understanding of lamB-phage interactions.