Porin flexibility in Providencia stuartii: cell-surface-exposed loops L5 and L7 are markers of Providencia porin OmpPst1
| Autor: | Tommaso D'Agostino, Que-Tien Tran, Jean-Marie Pagès, Mathias Winterhalter, Anne Davin-Regli, Matteo Ceccarelli, Laure Maigre |
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| Přispěvatelé: | Tran, Que-Tien, Maigre, Laure, D'Agostino, Tommaso, Ceccarelli, Matteo, Winterhalter, Mathia, Pagès, Jean-Marie, Davin-Regli, Anne |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Antibiotic resistance 030106 microbiology Cell Porins Microbial Sensitivity Tests Providencia beta-Lactams Microbiology 03 medical and health sciences medicine Humans Amino Acid Sequence Overproduction Molecular Biology chemistry.chemical_classification Membrane transport biology Providencia stuartii Porin Enterobacteriaceae Infections Genetic Variation General Medicine biochemical phenomena metabolism and nutrition biology.organism_classification Amino acid Anti-Bacterial Agents 030104 developmental biology medicine.anatomical_structure chemistry Cell permeabilization bacteria Bacterial outer membrane Sequence Alignment Bacterial Outer Membrane Proteins |
| Popis: | Epidemiologically unrelated Providencia stuartii strains isolated in hospitals in the south of France were investigated for their porin sequences and profiles. Noticeable resistance to β-lactams was found to be associated with production of extended spectrum β-lactamases or AmpC overproduction, but not metallo-β-lactamases. At the same time, the expression level of outer membrane porins was unmodified in these isolates. The identity of the amino acid sequences of the major porin OmpPst1 was less than 90% in the tested clinical strains, whereas sequences of the second major porin OmpPst2 were found to be identical in all isolates. Sequence diversity identified in the OmpPst1 porins was mainly located in two cell-surface-exposed loops (L5 and L7): these loops were found to be responsible for 80% of the main movements of the protein. Parallel tempering MD simulations indicated possible coordinated movement of these loops that might affect the electrostatic interaction of the porin with membrane components (e.g. LPS) or with external molecules/surfaces. This suggests that such flexibility of surface-exposed domains of OmpPst1 may participate in bacterial adaptation to the environment. |
| Databáze: | OpenAIRE |
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