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The Shigella flexneri OmpA amino acid residues (188)EVQ(190) are essential for the interaction with the virulence factor PhoN2
Shigella flexneri is an intracellular pathogen that deploys an arsenal of virulence factors promoting host cell invasion, intracellular multiplication and intra- and inter-cellular dissemination. We have previously reported that the interaction between apyrase (PhoN2), a periplasmic ATP-diphosphohyd...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5613738/ https://www.ncbi.nlm.nih.gov/pubmed/28955953 http://dx.doi.org/10.1016/j.bbrep.2016.08.010 |
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author | Scribano, Daniela Damico, Rosanna Ambrosi, Cecilia Superti, Fabiana Marazzato, Massimiliano Conte, Maria Pia Longhi, Catia Palamara, Anna Teresa Zagaglia, Carlo Nicoletti, Mauro |
author_facet | Scribano, Daniela Damico, Rosanna Ambrosi, Cecilia Superti, Fabiana Marazzato, Massimiliano Conte, Maria Pia Longhi, Catia Palamara, Anna Teresa Zagaglia, Carlo Nicoletti, Mauro |
author_sort | Scribano, Daniela |
collection | PubMed |
description | Shigella flexneri is an intracellular pathogen that deploys an arsenal of virulence factors promoting host cell invasion, intracellular multiplication and intra- and inter-cellular dissemination. We have previously reported that the interaction between apyrase (PhoN2), a periplasmic ATP-diphosphohydrolase, and the C-terminal domain of the outer membrane (OM) protein OmpA is likely required for proper IcsA exposition at the old bacterial pole and thus for full virulence expression of Shigella flexneri (Scribano et al., 2014). OmpA, that is the major OM protein of Gram-negative bacteria, is a multifaceted protein that plays many different roles both in the OM structural integrity and in the virulence of several pathogens. Here, by using yeast two-hybrid technology and by constructing an in silico 3D model of OmpA from S. flexneri 5a strain M90T, we observed that the OmpA residues (188)EVQ(190) are likely essential for PhoN2-OmpA interaction. The (188)EVQ(190) amino acids are located within a flexible region of the OmpA protein that could represent a scaffold for protein-protein interaction. |
format | Online Article Text |
id | pubmed-5613738 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-56137382017-09-27 The Shigella flexneri OmpA amino acid residues (188)EVQ(190) are essential for the interaction with the virulence factor PhoN2 Scribano, Daniela Damico, Rosanna Ambrosi, Cecilia Superti, Fabiana Marazzato, Massimiliano Conte, Maria Pia Longhi, Catia Palamara, Anna Teresa Zagaglia, Carlo Nicoletti, Mauro Biochem Biophys Rep Research Article Shigella flexneri is an intracellular pathogen that deploys an arsenal of virulence factors promoting host cell invasion, intracellular multiplication and intra- and inter-cellular dissemination. We have previously reported that the interaction between apyrase (PhoN2), a periplasmic ATP-diphosphohydrolase, and the C-terminal domain of the outer membrane (OM) protein OmpA is likely required for proper IcsA exposition at the old bacterial pole and thus for full virulence expression of Shigella flexneri (Scribano et al., 2014). OmpA, that is the major OM protein of Gram-negative bacteria, is a multifaceted protein that plays many different roles both in the OM structural integrity and in the virulence of several pathogens. Here, by using yeast two-hybrid technology and by constructing an in silico 3D model of OmpA from S. flexneri 5a strain M90T, we observed that the OmpA residues (188)EVQ(190) are likely essential for PhoN2-OmpA interaction. The (188)EVQ(190) amino acids are located within a flexible region of the OmpA protein that could represent a scaffold for protein-protein interaction. Elsevier 2016-08-12 /pmc/articles/PMC5613738/ /pubmed/28955953 http://dx.doi.org/10.1016/j.bbrep.2016.08.010 Text en © 2016 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article Scribano, Daniela Damico, Rosanna Ambrosi, Cecilia Superti, Fabiana Marazzato, Massimiliano Conte, Maria Pia Longhi, Catia Palamara, Anna Teresa Zagaglia, Carlo Nicoletti, Mauro The Shigella flexneri OmpA amino acid residues (188)EVQ(190) are essential for the interaction with the virulence factor PhoN2 |
title | The Shigella flexneri OmpA amino acid residues (188)EVQ(190) are essential for the interaction with the virulence factor PhoN2 |
title_full | The Shigella flexneri OmpA amino acid residues (188)EVQ(190) are essential for the interaction with the virulence factor PhoN2 |
title_fullStr | The Shigella flexneri OmpA amino acid residues (188)EVQ(190) are essential for the interaction with the virulence factor PhoN2 |
title_full_unstemmed | The Shigella flexneri OmpA amino acid residues (188)EVQ(190) are essential for the interaction with the virulence factor PhoN2 |
title_short | The Shigella flexneri OmpA amino acid residues (188)EVQ(190) are essential for the interaction with the virulence factor PhoN2 |
title_sort | shigella flexneri ompa amino acid residues (188)evq(190) are essential for the interaction with the virulence factor phon2 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5613738/ https://www.ncbi.nlm.nih.gov/pubmed/28955953 http://dx.doi.org/10.1016/j.bbrep.2016.08.010 |
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