Isolation and Characterization of a Generalized Transducing Bacteriophage for Acinetobacter

Author:

Herman Norma J.1,Juni Elliot1

Affiliation:

1. Department of Microbiology, The University of Michigan, Ann Arbor, Michigan 48104

Abstract

A series of bacteriophages which grow in various strains of Acinetobacter have been isolated. One of these, phage P78, which forms turbid plaques on Acinetobacter strain 78 is specific for this particular host and fails to attack 389 other independently isolated strains of Acinetobacter . Phage P78 appears to be a temperate phage which lysogenizes its host. Various agents such as N -methyl- N ′-nitro- N -nitrosoguanidine, diethyl sulfate, mitomycin C, and ultraviolet light are effective inducers of the lysogen. Phage lysates of wild-type cells are capable of transducing auxotrophs of strain 78 to prototrophy at frequencies ranging from 0.3 × 10 −7 to 34 × 10 −7 per plaque-forming unit adsorbed. To date, no linkage has been detected between any of the markers studied in two-factor crosses. Donor phage grown in one particular mutant, strain 78 ( arg-1 ), has been shown to give rise to significantly higher transduction frequencies than when phage is grown on wild-type or other auxotrophic strains. Phage P78 is rapidly adsorbed to its bacterial host and has a latent period of 25 min, and infection results in a burst size of approximately 50. Some of the physical properties of phage P78 and its DNA are described.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference20 articles.

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3. A study of the Moraxella group. II. Oxidative-negative species (genus Acinetobacter);Baumann P.;J. Bacteriol.,1968

4. Clowes R. C. and W. Hayes. 1968. Amino acid vitamins and purine/pyrimidine pools used in the determination of auxotrophic requirements p. 228-229. In R. C. Clowes and W. Hayes (ed.) Experiments in microbial genetics. Blackwell Scientific Publications Oxford.

5. Eigner J. 1968. Molecular weight and conformation of DNA p. 386-429. In L. Grossman and K. Moldave (ed.) Methods in enzymology vol. 12 part B. Academic Press Inc. New York.

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