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Journal of Bacteriology, July 2008, p. 4989-4996, Vol. 190, No. 14
0021-9193/08/$08.00+0     doi:10.1128/JB.00349-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Phage SPP1 Reversible Adsorption to Bacillus subtilis Cell Wall Teichoic Acids Accelerates Virus Recognition of Membrane Receptor YueB{triangledown} ,{dagger}

Catarina Baptista, Mário A. Santos, and Carlos São-José*

Instituto de Ciência Aplicada e Tecnologia and Departamento de Biologia Vegetal, Faculdade de Ciências da Universidade de Lisboa, Ed. ICAT, 1749-016 Lisbon, Portugal

Received 10 March 2008/ Accepted 8 May 2008

Bacteriophage SPP1 targets the host cell membrane protein YueB to irreversibly adsorb and infect Bacillus subtilis. Interestingly, SPP1 still binds to the surface of yueB mutants, although in a completely reversible way. We evaluated here the relevance of a reversible step in SPP1 adsorption and identified the receptor(s) involved. We show that reversible adsorption is impaired in B. subtilis mutants defective in the glucosylation pathway of teichoic acids or displaying a modified chemical composition of these polymers. The results indicate that glucosylated poly(glycerolphosphate) cell wall teichoic acid is the major target for SPP1 reversible binding. Interaction with this polymer is characterized by a fast adsorption rate showing low-temperature dependence, followed by a rapid establishment of an equilibrium state between adsorbed and free phages. This equilibrium is basically determined by the rate of phage dissociation, which exhibits a strong dependence on temperature compatible with an Arrhenius law. This allowed us to determine an activation energy of 22.6 kcal/mol for phage release. Finally, we show that SPP1 reversible interaction strongly accelerates irreversible binding to YueB. Our results support a model in which fast SPP1 adsorption to and desorption from teichoic acids allows SPP1 to scan the bacterial surface for rapid YueB recognition.

* Corresponding author. Mailing address: Instituto de Medicina Molecular, Av. Prof. Egas Moniz, Ed. Egas Moniz, 1649-028 Lisbon, Portugal. Phone: 351217999411, ext. 47230. Fax: 351217999412. E-mail: cjose{at}fm.ul.pt

{triangledown} Published ahead of print on 16 May 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, July 2008, p. 4989-4996, Vol. 190, No. 14
0021-9193/08/$08.00+0     doi:10.1128/JB.00349-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kaneko, J., Narita-Yamada, S., Wakabayashi, Y., Kamio, Y. (2009). Identification of ORF636 in Phage {phi}SLT Carrying Panton-Valentine Leukocidin Genes, Acting as an Adhesion Protein for a Poly(Glycerophosphate) Chain of Lipoteichoic Acid on the Cell Surface of Staphylococcus aureus. J. Bacteriol. 191: 4674-4680 [Abstract] [Full Text]  


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