Unknown

Dataset Information

0

Staphylococcus aureus pathogenicity island DNA is packaged in particles composed of phage proteins.


ABSTRACT: 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.

SUBMITTER: Tormo MA 

PROVIDER: S-EPMC2293202 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Staphylococcus aureus pathogenicity island DNA is packaged in particles composed of phage proteins.

Tormo María Angeles MA   Ferrer María Desamparados MD   Maiques Elisa E   Ubeda Carles C   Selva Laura L   Lasa Iñigo I   Calvete Juan J JJ   Novick Richard P RP   Penadés José R JR  

Journal of bacteriology 20080125 7


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  ...[more]

Similar Datasets

| S-EPMC2168463 | biostudies-literature
| S-EPMC7611864 | biostudies-literature
| S-EPMC1964853 | biostudies-other
| S-EPMC2562889 | biostudies-literature
| S-EPMC10541612 | biostudies-literature
| S-EPMC4402969 | biostudies-literature
| S-EPMC4907134 | biostudies-literature
| S-EPMC94850 | biostudies-literature
| S-EPMC4936726 | biostudies-literature
| S-EPMC5784253 | biostudies-literature