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Adhesion of K88ab to guinea pig erythrocytes: effect on membrane enzyme activities

M J Caloca1, J Soler, S Suárez

  • 1Departmento de Bioquimica y Biologia Molecular, Universidad de Leon, Spain.

Infection and Immunity
|August 1, 1996
PubMed

Insights

Nontoxigenic Escherichia coli K88 fimbriae adhere to host cells, inhibiting Mg2+-dependent ATPase but not Na/K ATPase. This study reveals specific cellular alterations caused by K88ab fimbriae adherence.

Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Nontoxigenic Escherichia coli strains carrying K88 fimbriae are linked to piglet diarrhea.
  • Understanding the interaction between K88 fimbriae and host cells is crucial for addressing enteric diseases.

Purpose of the Study:

  • To investigate the cellular alterations in host cells upon adherence of purified K88ab fimbriae.
  • To determine the effect of K88ab fimbriae on specific cellular enzymes, including ATPases.

Main Methods:

  • Utilized guinea pig erythrocytes as a model host cell system.
  • Studied cellular alterations following the adherence of purified K88ab fimbriae.
  • Assessed the activity of Mg2+-dependent ATPase, Na/K ATPase, and metabolic enzymes.

Main Results:

  • Adherence of purified K88ab fimbriae led to significant inhibition of Mg2+-dependent ATPase activity (up to 61%).
  • Na/K ATPase activity remained unaffected by K88ab fimbriae adherence.
  • No significant impact was observed on the activity of key metabolic enzymes.

Conclusions:

  • K88ab fimbriae adherence induces specific cellular changes, primarily affecting Mg2+-dependent ATPase.
  • The selective inhibition of Mg2+-dependent ATPase suggests a targeted mechanism of action by K88ab fimbriae.
  • These findings contribute to understanding the pathogenesis of Escherichia coli-associated diarrhea.

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