Jesse S. Wright
New York University
5 Papers
126 Citations
Jesse S. Wright is an academic researcher from New York University. The author has contributed to research in topics: Quorum sensing & Receptor. The author has an hindex of 5, co-authored 5 publications.
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Papers
Key determinants of receptor activation in the agr autoinducing peptides of Staphylococcus aureus.
TL;DR: Characterization of the unique AIPs from the four known agr specificity groups of Staphylococcus aureus has been completed, along with analysis of cross-group inhibition of AgrC activation by each of the four A IPs, which suggest a model in which activation and inhibition involves different binding orientations within the ligand binding pocket of each receptor.
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The agr Radiation: an Early Event in the Evolution of Staphylococci
Jesse S. Wright,Katrina E. Traber,Rebecca M. Corrigan,Sarah A. Benson,James M. Musser,James M. Musser,Richard P. Novick +6 more
TL;DR: Evidence is presented, using a newly developed, luciferase-based agr typing scheme, that the evolutionary divergence of the agr system was an early event in the evolution of the staphylococci and long preceded the development of the nucleotide polymorphisms presently used for genotyping.
133
Transient interference with staphylococcal quorum sensing blocks abscess formation.
TL;DR: It is confirmed that a sterile agr+ supernatant causes a sterile abscess similar to the septic abscess caused by live bacteria, which may provide a biological rationale for regulation of virulence factor expression by quorum sensing rather than by response to specific host signals.
Hydrophobic interactions drive ligand-receptor recognition for activation and inhibition of staphylococcal quorum sensing
TL;DR: Testing of these chimeric receptors against a battery of AIP analogs revealed that the AIPs bind primarily to a putative hydrophobic pocket in the receptor, suggesting that this recognition scheme provides the fundamental basis for agr activation and interference.
Reversible and specific extracellular antagonism of receptor-histidine kinase signaling.
TL;DR: The results suggest that molecules designed to compete with natural agonists for binding at receptor- histidine kinase sensor domains could represent a general approach to the inhibition of receptor-histidine Kinase signaling.