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Related Concept Videos

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Amphotericin B is a broad-spectrum antifungal agent that exploits structural differences between fungal and mammalian cell membranes. Its amphipathic structure—featuring a hydrophobic polyene-lactone ring and a hydrophilic region containing mycosamine and carboxylic acid groups—enables selective binding to ergosterol, a sterol predominantly found in fungal plasma membranes. This selective interaction underlies the drug’s antifungal activity, although weak binding to...
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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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Assessing the Putative Anticryptococcal Properties of Crude and Clarified Extracts from Mollusks
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Interaction of surface molecules on Cryptococcus neoformans with plasminogen.

Reiko Ikeda1, Tomoe Ichikawa

  • 1Department of Microbial Science and Host Defense, Meiji Pharmaceutical University, Noshio, Kiyose, Tokyo, Japan.

FEMS Yeast Research
|December 31, 2013
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Cryptococcus neoformans surface polysaccharides bind and activate plasminogen, a key component of the host fibrinolytic system. This interaction may facilitate pathogen invasion by influencing blood clot breakdown.

Keywords:
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Area of Science:

  • Microbiology
  • Biochemistry
  • Immunology

Background:

  • Pathogenic microorganisms often express molecules that interact with host proteins to facilitate invasion.
  • The host fibrinolytic system, involving plasminogen, is a target for microbial exploitation.
  • Staphylococcus aureus triosephosphate isomerase (TPI) is a known moonlighting protein that binds plasminogen.

Purpose of the Study:

  • To investigate the interaction between Cryptococcus neoformans surface polymers and human plasminogen.
  • To determine if C. neoformans surface components can activate plasminogen, potentially aiding in host tissue invasion.

Main Methods:

  • Surface plasmon resonance (SPR) analysis to detect plasminogen binding to soluble polysaccharides.
  • DEAE column chromatography to fractionate C. neoformans surface polysaccharides.
  • Assay to measure plasminogen activation by C. neoformans components in the presence of tissue plasminogen activator.

Main Results:

  • Heat-killed C. neoformans cells activated plasminogen in a dose-dependent manner.
  • Neutral polysaccharides from C. neoformans bound to plasminogen and activated it.
  • The major capsular component, glucuronoxylomannan, showed weak binding and did not activate plasminogen.
  • Neutral polysaccharides contained mannose, galactose, glucose, and xylose.

Conclusions:

  • C. neoformans possesses surface neutral polysaccharides capable of binding and activating plasminogen.
  • These polysaccharides may influence the host fibrinolytic system, potentially contributing to fungal invasion.
  • The primary capsule component, glucuronoxylomannan, does not appear to play a significant role in plasminogen activation.