Destabilization of phospholipid model membranes by YplA, a phospholipase A2 secreted by Yersinia enterocolitica

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Erin Berring1, Sam Brancato, Katherine Grant

  • 1Department of Chemistry, Saint Louis University, Monsanto Hall 125, 3501 Laclede Avenue, St. Louis, MO 63103-2010, USA.

Chemistry and Physics of Lipids
|September 8, 2004
PubMed

Insights

Yersinia enterocolitica's phospholipase A2 (YplA) interacts differently with cell membranes depending on its N-terminus. This N-terminus is crucial for YplA's initial interaction with compact cellular membranes.

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Yersinia enterocolitica possesses a virulence factor, phospholipase A2 (YplA).
  • YplA is secreted through the flagellar type-III secretion system.
  • The N-terminal region of YplA influences its enzymatic activity and membrane interaction.

Purpose of the Study:

  • To investigate the physical properties and membrane association of Yersinia enterocolitica phospholipase A2 (YplA).
  • To determine the role of YplA's N-terminus in its interaction with biological membranes.

Main Methods:

  • Utilized Langmuir phospholipid monolayers to study YplA and its truncated form (YplA(S)) association.
  • Employed fluorescent phospholipid substrates to analyze phospholipase activity.
  • Spectroscopic analysis of fluorescein-labeled YplA interaction with liposomes.

Main Results:

  • Both YplA and YplA(S) associate with phospholipid monolayers.
  • YplA(S) shows better interaction at low lipid densities, while YplA prefers higher densities.
  • Fluorescein-labeled YplA interacts more readily with the nonpolar region of liposomes compared to YplA(S).

Conclusions:

  • The N-terminus of YplA plays a significant role in mediating its initial interaction with cellular membranes.
  • Differential binding affinities suggest a specific function for the N-terminus in membrane recognition.
  • Findings provide insights into the mechanism of YplA's virulence and membrane targeting.

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