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J. Bacteriol. doi:10.1128/JB.01349-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

SaPI DNA is packaged in particles composed of phage proteins

Centro de Investigación y Tecnología Animal, Instituto Valenciano de Investigaciones Agrarias (CITA-IVIA), Apdo. 187, 12.400 Segorbe, Castellón, Spain; Departamento de Química, Bioquímica y Biología Molecular, Universidad Cardenal Herrera-CEU, 46113 Moncada, Valencia, Spain; Skirball Institute, New York University Medical Center, 540 First Avenue, New York, NY 10016, USA; Instituto de Agrobiotecnología, CSIC-Universidad Pública de Navarra-Gobierno de Navarra, 31006 Pamplona, Navarra, Spain; Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas, 46010 Valencia, Spain

^* To whom correspondence should be addressed. Email: jpenades{at}ivia.es.

	Abstract

Staphylococcus aureus pathogencity 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 function of SaPI or phage particles, having no role in other SaPI or phage functions.

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