This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Vegge, C. S. Articles by Vogensen, F. K. Search for Related Content PubMed PubMed Citation Articles by Vegge, C. S. Articles by Vogensen, F. K.

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

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), tal_TP901-1 (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 Tal_TP901-1 were shown to be structural tail proteins essential for tail formation, and Tal_TP901-1 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.

This article has been cited by other articles:

• Sciara, G., Blangy, S., Siponen, M., Mc Grath, S., van Sinderen, D., Tegoni, M., Cambillau, C., Campanacci, V. (2008). A Topological Model of the Baseplate of Lactococcal Phage Tuc2009. J. Biol. Chem. 283: 2716-2723 [Abstract] [Full Text]  
• Labrie, S. J., Moineau, S. (2007). Abortive Infection Mechanisms and Prophage Sequences Significantly Influence the Genetic Makeup of Emerging Lytic Lactococcal Phages. J. Bacteriol. 189: 1482-1487 [Abstract] [Full Text]  
• Vegge, C. S., Neve, H., Brondsted, L., Heller, K. J., Vogensen, F. K. (2006). Analysis of the Collar-Whisker Structure of Temperate Lactococcal Bacteriophage TP901-1.. Appl. Environ. Microbiol. 72: 6815-6818 [Abstract] [Full Text]  
• Deveau, H., Labrie, S. J., Chopin, M.-C., Moineau, S. (2006). Biodiversity and classification of lactococcal phages.. Appl. Environ. Microbiol. 72: 4338-4346 [Abstract] [Full Text]  
• Mc Grath, S., Neve, H., Seegers, J. F. M. L., Eijlander, R., Vegge, C. S., Brondsted, L., Heller, K. J., Fitzgerald, G. F., Vogensen, F. K., van Sinderen, D. (2006). Anatomy of a Lactococcal Phage Tail. J. Bacteriol. 188: 3972-3982 [Abstract] [Full Text]  
• Spinelli, S., Campanacci, V., Blangy, S., Moineau, S., Tegoni, M., Cambillau, C. (2006). Modular Structure of the Receptor Binding Proteins of Lactococcus lactis Phages: THE RBP STRUCTURE OF THE TEMPERATE PHAGE TP901-1. J. Biol. Chem. 281: 14256-14262 [Abstract] [Full Text]  
• Vegge, C. S., Vogensen, F. K., Mc Grath, S., Neve, H., van Sinderen, D., Brondsted, L. (2006). Identification of the Lower Baseplate Protein as the Antireceptor of the Temperate Lactococcal Bacteriophages TP901-1 and Tuc2009. J. Bacteriol. 188: 55-63 [Abstract] [Full Text]