P1
cinC(+) mutants were isolated from a P1CM
clr100 lysogen based on the criterion that the
cin mutation cannot restore flagellar phase variation of the
hin pin strain, and a P1
cinC(-) mutant was isolated from a P1
cinC(+) lysogen of the
hin+ pin+ strain by utilizing the difference in colonial types at 41°C. The
hin+ pin+/P1
cinC(-) strain yielded P1
cinC(+) lysogens at a rate of 10
-2 per bacterium while the
hin pin/P1
cinC(-) strain was considerably stable. Anti-P1
cinC(+) serum neutralized both the P1
cinC(-) and MuG(+) particles to 16% the rate of the homologous combination whereas anti-P1
cinC(-) serum neutralized the P1
cinC(+) particles to 45% the rate of the homologous combination. This indicates that P1
cinC(+) and P1
cinC(-) bear antigenically distinct polypeptides concerned with host specificity and that P1
cinC(+) shares some antigen (s) involved in infectivity with MuG(+). The analysis of whole phage proteins revealed that P1
cinC(+) had a 105kd polypeptide, and P1
cinC(-) had 101kd instead of 105kd.
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