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Journal of Bacteriology, June 2005, p. 4187-4197, Vol. 187, No. 12
0021-9193/05/$08.00+0     doi:10.1128/JB.187.12.4187-4197.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Structural Characterization and Assembly of the Distal Tail Structure of the Temperate Lactococcal Bacteriophage TP901-1

Christina S. Vegge,1 Lone Brøndsted,2 Horst Neve,3 Stephen Mc Grath,4 Douwe van Sinderen,4,5 and Finn K. Vogensen1*

Department of Food Science, The Royal Veterinary and Agricultural University, Frederiksberg C, Denmark,1 Department of Veterinary Pathobiology, The Royal Veterinary and Agricultural University, Frederiksberg C, Denmark,2 Institute for Microbiology, Federal Research Centre for Nutrition and Food, Kiel, Germany,3 National Food Biotechnology Centre and Department of Microbiology, National University of Ireland, Cork, Ireland,4 Alimentary Pharmabiotic Centre, University College Cork, Cork, Ireland5

Received 4 January 2005/ Accepted 10 March 2005

The tail structures of bacteriophages infecting gram-positive bacteria are largely unexplored, although the phage tail mediates the initial interaction with the host cell. The temperate Lactococcus lactis phage TP901-1 of the Siphoviridae family has a long noncontractile tail with a distal baseplate. In the present study, we investigated the distal tail structures and tail assembly of phage TP901-1 by introducing nonsense mutations into the late transcribed genes dit (orf46), talTP901-1 (orf47), bppU (orf48), bppL (orf49), and orf50. Transmission electron microscopy examination of mutant and wild-type TP901-1 phages showed that the baseplate consisted of two different disks and that a central tail fiber is protruding below the baseplate. Evaluation of the mutant tail morphologies with protein profiles and Western blots revealed that the upper and lower baseplate disks consist of the proteins BppU and BppL, respectively. Likewise, Dit and TalTP901-1 were shown to be structural tail proteins essential for tail formation, and TalTP901-1 was furthermore identified as the tail fiber protein by immunogold labeling experiments. Determination of infection efficiencies of the mutant phages showed that the baseplate is fundamental for host infection and the lower disk protein, BppL, is suggested to interact with the host receptor. In contrast, ORF50 was found to be nonessential for tail assembly and host infection. A model for TP901-1 tail assembly, in which the function of eight specific proteins is considered, is presented.

* Corresponding author. Mailing address: Department of Food Science, The Royal Veterinary and Agricultural University, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark. Phone: 45 35 28 32 11. Fax: 45 35 28 32 14. E-mail: fkv{at}kvl.dk.

Journal of Bacteriology, June 2005, p. 4187-4197, Vol. 187, No. 12
0021-9193/05/$08.00+0     doi:10.1128/JB.187.12.4187-4197.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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