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The Shigella flexneri OmpA amino acid residues 188EVQ190 are essential for the interaction with the virulence factor

Daniela Scribano1,2, Rosanna Damico2, Cecilia Ambrosi2

  • 1Dip. Scienze Mediche, Orali e Biotecnologiche, Università "G. D'Annunzio" di Chieti, Chieti, Italy.

Biochemistry and Biophysics Reports
|September 29, 2017
PubMed

Insights

Shigella flexneri outer membrane protein A (OmpA) interacts with apyrase (PhoN2). Specific OmpA residues (188-190) are crucial for this interaction, impacting bacterial virulence.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • Shigella flexneri is an intracellular pathogen.
  • Outer membrane protein A (OmpA) is vital for Gram-negative bacteria.
  • OmpA plays roles in structural integrity and virulence.

Purpose of the Study:

  • To identify specific residues in S. flexneri OmpA involved in PhoN2 interaction.
  • To understand the structural basis of OmpA-PhoN2 interaction.

Main Methods:

  • Yeast two-hybrid technology.
  • In silico 3D modeling of S. flexneri OmpA.

Main Results:

  • The OmpA residues 188-190 (EVQ) are essential for PhoN2-OmpA interaction.
  • These residues are located in a flexible region of OmpA, potentially acting as a protein-protein interaction scaffold.

Conclusions:

  • The OmpA 188-190 region is critical for PhoN2 binding.
  • This interaction is important for Shigella flexneri virulence.
Keywords:
IcsAOmpAPhoN2 (apyrase)Protein-protein interactionShigella flexneriYeast two-hybrid

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