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Updated: Aug 19, 2026
Experimental Human Pneumococcal Carriage
Published on: February 15, 2013
Surface labeling of Pneumocystis carinii from in vitro culture
J A Radding1, M Y Armstrong, M S Bogucki
1Yale MacArthur Center for Molecular Parasitology, Yale University School of Medicine, New Haven, CT 06510.
Abstract:
Pneumocystis carinii is an opportunistic pathogen of man, carried as a commensal in healthy subjects. It frequently causes a fatal pneumonia in the immunosuppressed host. It is a major complication of HIV-1 infection in man (AIDS). Using surface radioiodination of rat-derived P. carinii trophozoites obtained from in vitro culture, a major surface glycoprotein (gp120) has been identified. The glycoprotein exhibits adherent behavior similar to that of the intact organism. Purification of gp120 by conventional methods was unsuccessful as the glycoprotein irreversibly bound to numerous column matrices. A combination of gel chromatography and hydroxyapatite chromatography in sodium dodecylsulfate was utilized to purify the glycoprotein. Some preliminary characterization of the glycoprotein is presented.
Insights
Researchers identified a key surface glycoprotein (gp120) on Pneumocystis carinii, an opportunistic pathogen causing pneumonia in immunocompromised individuals, including those with HIV/AIDS.
Area of Science:
- Medical Mycology
- Immunology
- Virology
Background:
- Pneumocystis carinii is an opportunistic pathogen causing fatal pneumonia in immunosuppressed individuals.
- It is a significant complication in human immunodeficiency virus type 1 (HIV-1) infection, leading to acquired immunodeficiency syndrome (AIDS).
- Understanding P. carinii's surface components is crucial for developing diagnostic and therapeutic strategies.
Purpose of the Study:
- To identify and characterize major surface glycoproteins of Pneumocystis carinii.
- To investigate the role of these glycoproteins in organism adherence.
- To develop effective purification methods for these surface molecules.
Main Methods:
- Surface radioiodination of in vitro cultured rat-derived P. carinii trophozoites.
- Gel chromatography and hydroxyapatite chromatography in sodium dodecyl sulfate for glycoprotein purification.
- Preliminary characterization of the purified glycoprotein.
Main Results:
- A major surface glycoprotein, designated gp120, was identified on P. carinii trophozoites.
- The purified gp120 demonstrated adherent properties, mirroring the intact organism's behavior.
- Conventional purification methods were ineffective due to irreversible binding; a specialized chromatographic approach was successful.
Conclusions:
- Pneumocystis carinii possesses a major surface glycoprotein (gp120) involved in adherence.
- The unique binding properties of gp120 necessitate specific purification techniques.
- Further characterization of gp120 may offer insights into P. carinii pathogenesis and potential therapeutic targets.
