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Bacteriophage chi sensitivity and motility of Escherichia coli K-12 and Salmonella typhimurium Fla- mutants possessing the hook structure

The production of hook protein and flagellin in 29 Fla- mutants of Escherichia coli K-12 was determined by the complement fixation assay. Six mutants produced hook protein, and four of them also produced flagellin. A flaE mutation was introduced into these fla mutants carrying the hook structure. All of these mutants made polyhooks and were used as hosts for a newly isolated host-range mutant of chi phage that has a high affinity for the hook structure. All except one mutant produced significant amounts of progeny phages. A flaD flaE double mutant was that exception which did not yield significant amounts of progeny by the phage propagation method. All of the flaE double mutants produced comparable amounts of polyhooks, and no qualitative difference was detected between chi-sensitive and chi-insensitive mutants by the complement fixation assay. Accordingly, it was thought that the polyhook of the flaD flaE mutant had a mechanical defect for chi phage infection. This assumption was confirmed by tethered-cell experiments; the flaD flaE mutant did not rotate. These results are well explained by a proposed regulation pathway of flagellar genes. flaE mutants can express other genes which govern the final step of the flagellar morphogenesis, whereas flaD mutants cannot rotate, possibly because the mocha operon is not expressed. The results obtained in E. coli were also found to be applicable to Salmonella typhimurium.