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Isolation and properties of extracellular proteinases of Penicillium marneffei

Jonathan L Moon1, Lindsey N Shaw, John A Mayo

  • 1Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602-7229, USA.

Biological Chemistry
|August 18, 2006
PubMed

Insights

This study identifies and characterizes proteinases secreted by Penicillium marneffei, a fungus causing infections in immunocompromised individuals. Two distinct enzymes, an acid proteinase and a serine proteinase, were found to be differentially expressed.

Area of Science:

  • Mycology
  • Medical Mycology
  • Biochemistry

Background:

  • Penicillium marneffei is a dimorphic fungus endemic to Southeast Asia.
  • Infections caused by P. marneffei have increased due to rising rates of immunocompromised individuals, particularly those with AIDS.
  • Limited research exists on the proteinases secreted by this pathogen.

Purpose of the Study:

  • To identify and characterize proteinases secreted by Penicillium marneffei.
  • To investigate the potential role of these proteinases in P. marneffei pathogenesis.
  • To understand the expression patterns of these enzymes under different culture conditions.

Main Methods:

  • Purification and characterization of proteinases from P. marneffei liquid cultures.
  • Cloning and expression of a gene encoding a third proteinase.
  • Identification of enzyme families (eqolisin, serine proteinase) and assessment of their pH activity and expression.

Main Results:

  • Two secreted proteinases were purified and characterized.
  • One purified enzyme and a recombinant enzyme belong to the eqolisin family (pepstatin-insensitive acid proteinases).
  • A second purified enzyme is a neutral pH-active serine proteinase.
  • Enzyme expression appears to be differentially regulated by culture conditions.

Conclusions:

  • Penicillium marneffei secretes at least two distinct types of proteinases: an acid proteinase and a serine proteinase.
  • These enzymes are potentially involved in P. marneffei pathogenesis and their expression is regulated.
  • Further research into these proteinases could inform therapeutic strategies against P. marneffei infections.

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