Lysis Inhibition in Escherichia coli Infected with Bacteriophage T4

Author:

Bode Werner1

Affiliation:

1. Department of Physics, Kansas State University, Manhattan, Kansas 66502

Abstract

A technique of continuous filtration of T4-infected Escherichia coli has been devised to study the phenomenon of lysis inhibition. Studies using this technique revealed that the length of the lysis delay caused by superinfection can attain only certain discrete values, which for low average multiplicity of superinfection is thought to be a reflection of the actual number of superinfecting particles per cell. The time interval between primary and superinfection had little effect on the length of lysis delay. With increasing rate of superinfection, the length of lysis delay decreased. In superinfected cells, the concentration of endolysin exceeded the final concentration in nonsuperinfected cells. Superinfection of a lysing culture induced lysis inhibition immediately. Temperature-shift experiments, with cells primarily infected by a temperature-sensitive endolysin mutant, revealed that after the normal latent period superinfection was unable to induce lysis inhibition. Amber-restrictive cells, which were primarily infected by an endolysin negative amber mutant, released adenosine triphosphate (ATP) at the end of the normal latent period although lysis did not occur. Superinfection reduced the loss of ATP markedly. The hypothetical role of the cytoplasmic membrane in lysis inhibition is discussed.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference9 articles.

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2. Lysis and Iysis inhibition with Escherichia coli bacteriophage;DOERMANN A. H.;J. Bacteriol.,1948

3. Studies on the relationship between virus and host cell. III. The breakdown of p3alabelled T2r+ bacteriophage adsorbed to E. coli previously infected by other coliphages of the T group;FRENCH R. C.;Can. J. Med. Sci.,1951

4. LEHNINGER A. L. 1965. The mitochondrion. W. A. Benjamin Inc. New York.

5. McELRoY W. D. 1963. Crystalline firefly Iuciferase p. 445-448. In S. P. Colowick and N. 0. Kaplan [ed.] Methods in enzymology vol. 6. Academic Press Inc. New York.

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