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The cytoplasmic membrane is a primary target for the staphylocidal action of thrombin-induced platelet microbicidal

S P Koo1, M R Yeaman, C C Nast

  • 1Department of Medicine, St. John's Cardiovascular Research Center, Los Angeles County-Harbor UCLA Medical Center, Torrance, California 90509, USA. KOO@AFP76.HUMC.EDU

Infection and Immunity
|November 14, 1997
PubMed

Insights

Thrombin-induced platelet microbicidal protein (tPMP-1) directly targets and damages the bacterial cytoplasmic membrane, leading to Staphylococcus aureus death. This membrane disruption is dependent on bacterial growth phase and voltage, indicating a direct mechanism of action for tPMP-1.

Area of Science:

  • Antimicrobial Peptides
  • Bacterial Pathogenesis
  • Membrane Biophysics

Background:

  • Thrombin-induced platelet microbicidal protein (tPMP-1) is a cationic peptide with broad-spectrum antimicrobial activity.
  • tPMP-1 exhibits efficacy against Staphylococcus aureus, a significant human pathogen.
  • Previous studies suggested tPMP-1 disrupts the bacterial cytoplasmic membrane, but the directness of this interaction was unclear.

Purpose of the Study:

  • To investigate whether the staphylococcal cytoplasmic membrane is a direct or indirect target of tPMP-1.
  • To determine the influence of bacterial growth phase and cell wall on tPMP-1 activity.
  • To characterize the biophysical mechanism of tPMP-1-induced membrane damage.

Main Methods:

  • In vitro activity of tPMP-1 against protoplasts from logarithmic (LOG) and stationary (STAT) phase Staphylococcus aureus strains (susceptible 19S and resistant 19R).
  • Monitoring protoplast lysis via optical density and ultrastructural changes using transmission electron microscopy (TEM).
  • Electrophysiological studies using anionic planar lipid bilayers to assess tPMP-1 interaction under varying voltages.

Main Results:

  • tPMP-1 caused significant lysis and membrane disruption in LOG-phase protoplasts of susceptible S. aureus (19S), but not stationary-phase protoplasts.
  • tPMP-1 activity was independent of the bacterial cell wall, as evidenced by protoplast lysis.
  • tPMP-1 permeabilized lipid bilayers in a voltage-dependent manner, increasing conductance at -90 mV but not -30 mV.

Conclusions:

  • tPMP-1 directly targets the staphylococcal cytoplasmic membrane as a primary mechanism of action.
  • The antimicrobial activity of tPMP-1 is influenced by the bacterial growth phase.
  • tPMP-1 induces bacterial death, at least partly, by voltage-dependent membrane permeabilization.

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