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Related Concept Videos

Cryptococcal Meningitis01:27

Cryptococcal Meningitis

Cryptococcal meningitis is a life-threatening opportunistic infection predominantly associated with HIV/AIDS, accounting for over 100,000 deaths annually worldwide. However, it also affects individuals with other forms of immunosuppression, including those undergoing immunosuppressive therapy, organ transplant recipients, patients with innate immunodeficiencies, and individuals with hematological disorders. The infection is caused mainly by Cryptococcus neoformans and Cryptococcus gattii,...

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Related Experiment Video

Updated: May 28, 2026

Biolistic Transformation of a Fluorescent Tagged Gene into the Opportunistic Fungal Pathogen Cryptococcus neoformans
07:32

Biolistic Transformation of a Fluorescent Tagged Gene into the Opportunistic Fungal Pathogen Cryptococcus neoformans

Published on: March 19, 2015

Expression and characterization of Cryptococcus neoformans recombinant App1.

Asfia Qureshi1, Virginia Williams, Maurizio Del Poeta

  • 1Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.

Mycopathologia
|October 6, 2011
PubMed
Summary

Cryptococcus neoformans antiphagocytic protein 1 (App1) can form amyloid fibrils due to its cysteines. This study explored its properties and in vivo localization, aiding in understanding fungal pathogenesis.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Cryptococcus neoformans is an opportunistic fungal pathogen.
  • The antiphagocytic protein 1 (App1) is a key virulence factor.
  • Understanding App1's structure and function is crucial for developing antifungal strategies.

Purpose of the Study:

  • To characterize the biophysical properties of recombinant App1 (rApp1).
  • To investigate the potential for rApp1 to form amyloid fibrils.
  • To explore alternative expression systems for rApp1 and examine its in vivo localization.

Main Methods:

  • SDS-PAGE and gel filtration chromatography for protein characterization.
  • Circular dichroism and fluorescence spectroscopy for structural analysis.
  • Recombinant protein expression in insect cells and lentiviral systems.
  • In vivo localization studies in Cryptococcus neoformans.

Main Results:

  • rApp1 was characterized using multiple biophysical techniques.
  • The presence of an odd number of cysteines in rApp1 facilitates intermolecular disulfide bridge formation.
  • rApp1 demonstrated the ability to form amyloid fibrils in vitro under specific conditions.
  • Successful exploration of alternative expression methods for rApp1.
  • In vivo localization of App1 was examined in relation to the fungal capsule.

Conclusions:

  • rApp1 possesses unique structural properties enabling amyloid fibril formation.
  • These findings provide insights into the role of App1 in Cryptococcus neoformans pathogenesis.
  • The study offers potential avenues for therapeutic intervention targeting App1.