@article{TEXTUAL,
      recid = {10482},
      author = {Zaborina, Olga and Holbrook, Christopher and Chen, Yimei  and Long, Jason and Zaborin, Alexander and Morozova, Irina  and Fernandez, Hoylan and Wang, Yingmin and Turner, Jerrold  R and Alverdy, John C},
      title = {Structure–Function Aspects of PstS in Multi-Drug–Resistant  <i>Pseudomonas aeruginosa</i>},
      journal = {PLOS Pathology},
      address = {2008-02-15},
      number = {TEXTUAL},
      abstract = {<p>The increasing prevalence of multi-drug–resistant (MDR)  strains of <span class="genus-species">Pseudomonas  aeruginosa</span> among critically ill humans is of  significant concern. In the current study, we show that MDR  clinical isolates of <span class="genus-species">P.  aeruginosa</span> representing three distinct genotypes  that display high virulence against intestinal epithelial  cells, form novel appendage-like structures on their cell  surfaces. These appendages contain PstS, an extracellular  phosphate binding protein. Using anti-PstS antibodies, we  determined that the PstS-rich appendages in MDR strains are  involved in adherence to and disruption of the integrity of  cultured intestinal epithelial cell monolayers. The outer  surface–expressed PstS protein was also identified to be  present in <span class="genus-species">P. aeruginosa</span>  MPAO1, although to a lesser degree, and its role in  conferring an adhesive and barrier disruptive phenotype  against intestinal epithelial cells was confirmed using an  isogenic ΔPstS mutant. Formation of the PstS rich  appendages was induced during phosphate limitation and  completely suppressed in phosphate-rich media. Injection of  MDR strains directly into the intestinal tract of  surgically injured mice, a known model of phosphate  limitation, caused high mortality rates (60%–100%).  Repletion of intestinal phosphate in this model completely  prevented mortality. Finally, significantly less outer  surface PstS was observed in the MPAO1 mutant ΔHxcR thus  establishing a role for the alternative type II secretion  system Hxc in outer surface PstS expression. Gene  expression analysis performed by RT-PCR confirmed this  finding and further demonstrated abundant expression of  <em>pstS</em> analogous to <em>pa5369</em>, <em>pstS</em>  analogous to <em>pa0688/pa14–55410</em>, and <em>hxcX</em>  in MDR strains. Taken together, these studies provide  evidence that outer surface PstS expression confers a  highly virulent phenotype of MDR isolates against the  intestinal epithelium that alters their adhesive and  barrier disrupting properties against the intestinal  epithelium.</p>},
      url = {http://knowledge.uchicago.edu/record/10482},
}