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Changes in the Cytoplasmic Composition of Amino Acids and Proteins Observed in Staphylococcus aureus during Growth under Variable Growth Conditions Representative of the Human Wound Site

Artikel i vetenskaplig tidskrift
Författare M. M. Alreshidi
R. H. Dunstan
Johan Gottfries
M. M. Macdonald
M. J. Crompton
C. S. Ang
N. A. Williamson
T. K. Roberts
Publicerad i Plos One
Volym 11
Nummer/häfte 7
ISSN 1932-6203
Publiceringsår 2016
Publicerad vid Institutionen för kemi och molekylärbiologi
Språk en
Länkar dx.doi.org/10.1371/journal.pone.015...
Ämnesord small-colony variants, proteomic analysis, escherichia-coli, osmotic-stress, responses, skin, proline, osmoregulation, temperature, metabolome, Science & Technology - Other Topics
Ämneskategorier Biologiska vetenskaper

Sammanfattning

Staphylococcus aureus is an opportunistic pathogen responsible for a high proportion of nosocomial infections. This study was conducted to assess the bacterial responses in the cytoplasmic composition of amino acids and ribosomal proteins under various environmental conditions designed to mimic those on the human skin or within a wound site: pH6-8, temperature 35-37 degrees C, and additional 0-5% NaCl. It was found that each set of environmental conditions elicited substantial adjustments in cytoplasmic levels of glutamic acid, aspartic acid, proline, alanine and glycine (P < 0.05). These alterations generated characteristic amino acid profiles assessed by principle component analysis (PCA). Substantial alterations in cytoplasmic amino acid and protein composition occurred during growth under conditions of higher salinity stress implemented via additional levels of NaCl in the growth medium. The cells responded to additional NaCl at pH 6 by reducing levels of ribosomal proteins, whereas at pH 8 there was an upregulation of ribosomal proteins compared with the reference control. The levels of two ribosomal proteins, L32 and S19, remained constant across all experimental conditions. The data supported the hypothesis that the bacterium was continually responding to the dynamic environment by modifying the proteome and optimising metabolic homeostasis.

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