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María Desamparados Ferrer,1,2,
Elisa Maiques,1,2
Carles Úbeda,3
Laura Selva,1,2
Íñigo Lasa,4
Juan J. Calvete,5
Richard P. Novick,3 and
José R. Penadés1,2*
Centro de Investigación y Tecnología Animal, Instituto Valenciano de Investigaciones Agrarias, Apdo. 187, 12.400 Segorbe, Castellón, Spain,1 Departamento de Química, Bioquímica y Biología Molecular, Universidad Cardenal Herrera-CEU, 46113 Moncada, Valencia, Spain,2 Skirball Institute, New York University Medical Center, 540 First Avenue, New York, New York 10016,3 Instituto de Agrobiotecnología, CSIC-Universidad Pública de Navarra-Gobierno de Navarra, 31006 Pamplona, Navarra, Spain,4 Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas, 46010 Valencia, Spain5
Received 17 August 2007/ Accepted 17 January 2008
Staphylococcus aureus pathogenicity islands (SaPIs) have an intimate relationship with temperate staphylococcal phages. During phage growth, SaPIs are induced to replicate and are efficiently encapsidated into special small phage heads commensurate with their size. We have analyzed by amino acid sequencing and mass spectrometry the protein composition of the specific SaPI particles. This has enabled identification of major capsid and tail proteins and a putative portal protein. As expected, all these proteins were phage encoded. Additionally, these analyses suggested the existence of a protein required for the formation of functional phage but not SaPI particles. Mutational analysis demonstrated that the phage proteins identified were involved only in the formation and possibly the function of SaPI or phage particles, having no role in other SaPI or phage functions.
Published ahead of print on 25 January 2008.
Supplemental material for this article may be found at http://jb.asm.org/.
María Ángeles Tormo and María Desamparados Ferrer contributed equally to this work.
| Appl. Environ. Microbiol. | Infect. Immun. | Eukaryot. Cell |
|---|---|---|
| Mol. Cell. Biol. | J. Virol. | Microbiol. Mol. Biol. Rev. |
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