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

 Previous Article  |  Next Article 

Journal of Virology, September 2006, p. 9331-9335, Vol. 80, No. 18
0022-538X/06/$08.00+0     doi:10.1128/JVI.01160-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the Receptor-Binding Protein Head Domain from Lactococcus lactis Phage bIL170

Stefano Ricagno,1 Valérie Campanacci,1 Stéphanie Blangy,1 Silvia Spinelli,1 Denise Tremblay,2,3 Sylvain Moineau,2,3,4 Mariella Tegoni,1 and Christian Cambillau1*

Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités Aix-Marseille I & II, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France,1 Groupe de Recherche en Écologie Buccale (GREB), Faculté de Médecine Dentaire,2 Félix d'Hérelle Reference Center for Bacterial Viruses,3 Département de Biochimie et de Microbiologie, Faculté des Sciences et de Génie, Université Laval, Québec City, Québec, Canada G1K 7P44

Received 5 June 2006/ Accepted 21 June 2006

Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry, is subject to lytic phage infections. In the first step of infection, phages recognize the host saccharidic receptor using their receptor binding protein (RBP). Here, we report the 2.30-Å-resolution crystal structure of the RBP head domain from phage bIL170. The structure of the head monomer is remarkably close to those of other lactococcal phages, p2 and TP901-1, despite any sequence identity with them. The knowledge of the three-dimensional structures of three RBPs gives a better insight into the module exchanges which have occurred among phages.

* Corresponding author. Mailing address: Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités Aix-Marseille I & II, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France. Phone: 33 491 825 590. Fax: 33 491 266 720. E-mail: cambillau{at}afmb.univ-mrs.fr.

Journal of Virology, September 2006, p. 9331-9335, Vol. 80, No. 18
0022-538X/06/$08.00+0     doi:10.1128/JVI.01160-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Siponen, M., Spinelli, S., Blangy, S., Moineau, S., Cambillau, C., Campanacci, V. (2009). Crystal Structure of a Chimeric Receptor Binding Protein Constructed from Two Lactococcal Phages. J. Bacteriol. 191: 3220-3225 [Abstract] [Full Text]  
  • Siponen, M., Sciara, G., Villion, M., Spinelli, S., Lichiere, J., Cambillau, C., Moineau, S., Campanacci, V. (2009). Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone. J. Bacteriol. 191: 728-734 [Abstract] [Full Text]  
  • 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]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»