Abstract
Plaquing of a newly isolated phage of Bacillus subtilis, phage 41c, is only 2% efficient in agar containing 200 μg of deoxyribonuclease per ml. Timed deoxyribonuclease addition experiments showed that phage development is blocked in 90% of the cells if deoxyribonuclease is present during adsorption (zero-time samples), whereas 10 min after adsorption the enzyme has little effect (10-min samples). The fate of 32P-deoxyribonucleic acid label of phage 41c in zero-time samples was compared to that in 10-min samples. In both, about 80% of the label remained with the phage-bacterium complex on initial centrifugation. However, four successive washings removed 90% of the 32P from the zero-time samples but only 25% from the 10-min samples. In both samples, most of the washed-out label was of low molecular weight. When the time course of interruption of infection by blending was compared with interruption by deoxyribonuclease treatment, the two processes exhibited similar kinetics. It is postulated that both processes block injection at the same site, namely, the point of contact between phage tail and cell wall surface. Partitioning of 32P label during protoplasting of zero-time and 10-min samples was similar to that observed during washing. For the protoplasting experiments, a quantitative method for plaquing protoplasts was developed. A single bacillus made of several cells can give rise to several protoplast plaque-forming units. Strain 41c was the only phage of seven tested to be inhibited by deoxyribonuclease. No other deoxyribonuclease-sensitive phages have been described.
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Selected References
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- BRENNER S., HORNE R. W. A negative staining method for high resolution electron microscopy of viruses. Biochim Biophys Acta. 1959 Jul;34:103–110. doi: 10.1016/0006-3002(59)90237-9. [DOI] [PubMed] [Google Scholar]
- BROCK T. D., MOSSER J., PEACHER B. THE INHIBITION BY STREPTOMYCIN OF CERTAIN STREPTOCOCCUS BACTERIOPHAGES, USING HOST BACTERIA RESISTANT TO THE ANTIBIOTIC. J Gen Microbiol. 1963 Oct;33:9–22. doi: 10.1099/00221287-33-1-9. [DOI] [PubMed] [Google Scholar]
- Haas M., Yoshikawa H. Defective bacteriophage PBSH in Bacillus subtilis. II. Intracellular development of the induced prophage. J Virol. 1969 Feb;3(2):248–260. doi: 10.1128/jvi.3.2.248-260.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kawakami M., Landman O. E. Nature of the carrier state of bacteriophage SP-10 in Bacillus subtilis. J Bacteriol. 1968 May;95(5):1804–1812. doi: 10.1128/jb.95.5.1804-1812.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LANDMAN O. E., HALLE S. ENZYMICALLY AND PHYSICALLY INDUCED INHERITANCE CHANGES IN BACILLUS SUBTILIS. J Mol Biol. 1963 Dec;7:721–738. doi: 10.1016/s0022-2836(63)80119-9. [DOI] [PubMed] [Google Scholar]
- LURIA S. E., STEINER D. L. The role of calcium in the penetration of bacteriophage T5 into its host. J Bacteriol. 1954 Jun;67(6):635–639. doi: 10.1128/jb.67.6.635-639.1954. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lanni Y. T. DNA transfer from phage T5 to host cells: dependence on intercurrent protein synthesis. Proc Natl Acad Sci U S A. 1965 May;53(5):969–973. doi: 10.1073/pnas.53.5.969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MARMUR J., DOTY P. Determination of the base composition of deoxyribonucleic acid from its thermal denaturation temperature. J Mol Biol. 1962 Jul;5:109–118. doi: 10.1016/s0022-2836(62)80066-7. [DOI] [PubMed] [Google Scholar]
- Paranchych W. Stages in phage R17 infection: the role of divalent cations. Virology. 1966 Jan;28(1):90–99. doi: 10.1016/0042-6822(66)90309-6. [DOI] [PubMed] [Google Scholar]
- REITER H. EFFECTS OF ANTISERUM ON ADSORBED PHAGE. J Bacteriol. 1963 Oct;86:637–641. doi: 10.21236/ad0415723. [DOI] [PMC free article] [PubMed] [Google Scholar]
- REITER H. THE LOCATION OF THE INHIBITORY ACTION OF KCN AND SEVERAL POLYAMINES ON BACTERIOPHAGE REPLICATION. Virology. 1963 Dec;21:636–641. doi: 10.1016/0042-6822(63)90237-x. [DOI] [PubMed] [Google Scholar]
- SALTON M. R., MCQUILLEN K. Bacterial protoplasts. II. Bacteriophage multiplication in protoplasts of sensitive and lysogenic strains of Bacillus megaterium. Biochim Biophys Acta. 1955 Aug;17(4):465–472. doi: 10.1016/0006-3002(55)90408-x. [DOI] [PubMed] [Google Scholar]
- SCHILDKRAUT C. L., MARMUR J., DOTY P. Determination of the base composition of deoxyribonucleic acid from its buoyant density in CsCl. J Mol Biol. 1962 Jun;4:430–443. doi: 10.1016/s0022-2836(62)80100-4. [DOI] [PubMed] [Google Scholar]
- SCHINDLER J. INHIBITION OF REPRODUCTION OF THE F2 BACTERIOPHAGE BY STREPTOMYCIN. Folia Microbiol (Praha) 1964 Sep;89:269–276. doi: 10.1007/BF02873305. [DOI] [PubMed] [Google Scholar]
- Silverman P. M., Valentine R. C. The RNA injection step of bacteriophage f2 infection. J Gen Virol. 1969 Jan;4(1):111–124. doi: 10.1099/0022-1317-4-1-111. [DOI] [PubMed] [Google Scholar]
- THORNE C. B. Transduction in Bacillus subtilis. J Bacteriol. 1962 Jan;83:106–111. doi: 10.1128/jb.83.1.106-111.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tichy P., Landman O. E. Transformation in quasi spheroplasts of Bacillus subtilis. J Bacteriol. 1969 Jan;97(1):42–51. doi: 10.1128/jb.97.1.42-51.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Valentine R. C., Wedel H. The extracellular stages of RNA bacteriophage infection. Biochem Biophys Res Commun. 1965 Oct 26;21(2):106–112. doi: 10.1016/0006-291x(65)90094-x. [DOI] [PubMed] [Google Scholar]