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Journal of Bacteriology, August 2006, p. 5925-5934, Vol. 188, No. 16
0021-9193/06/$08.00+0     doi:10.1128/JB.00107-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Entry Mechanism of Membrane-Containing Phage Bam35 Infecting Bacillus thuringiensis

Ausra Gaidelyte,1,2,{ddagger} Virginija Cvirkaite-Krupovic,1,2,{ddagger} Rimantas Daugelavicius,1,2 Jaana K. H. Bamford,1,{dagger} and Dennis H. Bamford1*

Department of Biological and Environmental Sciences and Institute of Biotechnology, Biocenter 2, P.O. Box 56 (Viikinkaari 5), 00014 University of Helsinki, Finland,1 Department of Biochemistry and Biophysics, Vilnius University, M. K. Ciurlionio 21, 03101 Vilnius, Lithuania2

Received 20 January 2006/ Accepted 31 May 2006

The temperate double-stranded DNA bacteriophage Bam35 infects gram-positive Bacillus thuringiensis cells. Bam35 has an icosahedral protein coat surrounding the viral membrane that encloses the linear 15-kbp DNA genome. The protein coat of Bam35 uses the same assembly principle as that of PRD1, a lytic bacteriophage infecting gram-negative hosts. In this study, we dissected the process of Bam35 entry into discrete steps: receptor binding, peptidoglycan penetration, and interaction with the plasma membrane (PM). Bam35 very rapidly adsorbs to the cell surface, and N-acetyl-muramic acid is essential for Bam35 binding. Zymogram analysis demonstrated that peptidoglycan-hydrolyzing activity is associated with the Bam35 virion. We showed that the penetration of Bam35 through the PM is a divalent-cation-dependent process, whereas adsorption and peptidoglycan digestion are not.

* Corresponding author. Mailing address: P.O. Box 56 (Viikinkaari 5), FIN-00014, University of Helsinki, Finland. Phone: 358 9 191 59100. Fax: 358 9 191 59098. E-mail: dennis.bamford{at}helsinki.fi.

{dagger} Present address: Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Jyväskylä, Finland.

{ddagger} A. Gaidelytë and V. Cvirkaitë-Krupoviè contributed equally to this work.

Journal of Bacteriology, August 2006, p. 5925-5934, Vol. 188, No. 16
0021-9193/06/$08.00+0     doi:10.1128/JB.00107-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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