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. 1973 Jan;113(1):198–202. doi: 10.1128/jb.113.1.198-202.1973

Modification of Bacteriophage φ25 Adsorption to Bacillus subtilis by Concanavalin A

D C Birdsell 1, R J Doyle 2
PMCID: PMC251618  PMID: 4631705

Abstract

The phytohemagglutinin, concanavalin A (Con A), interacts specifically and reversibly with the α-d-glucose-substituted polyglycerol phosphate teichoic acids of Bacillus subtilis 168. Teichoic acids from nonglucosylated strains (mutants resistant to phage φ25) interact weakly, if at all, with Con A. Prior treatment of glucosylated cell walls with Con A results in a concentration-dependent inhibition of phage φ25 adsorption. The inhibition of adsorption to glucosylated cell walls occurs immediately upon the formation of the Con A-cell wall complex and is reversed upon dissociation of the complex by addition of α-methyl glucose. Examination of the interaction between Con A and whole cells, cell walls, or wall digests from glucosylated (phage-sensitive) and non-glucosylated (phage-resistant) strains further demonstrates the specificity of the reaction. A conditional phage φ25-resistant mutant only forms complexes with Con A when grown under permissive conditions.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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