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C3bi-binding protein on Candida albicans: temperature-dependent expression and relationship to human complement
A Eigentler1, T F Schulz, C Larcher
1Institute for Hygiene, Innsbruck, Austria.
Infection and Immunity
|February 1, 1989
Summary
Candida albicans pseudohyphae bind C3-coated particles via a temperature-dependent C3bi receptor. This receptor is heat labile, trypsin sensitive, and antigenically related but not identical to human complement receptor type 3 (CR3).
Area of Science:
- Mycology
- Immunology
- Microbiology
Background:
- Candida albicans forms pseudohyphae, a morphological transition implicated in host-pathogen interactions.
- Previous studies suggested C. albicans pseudohyphae can bind complement-coated particles.
Purpose of the Study:
- To investigate the capacity of C. albicans pseudohyphae to bind C3-coated particles.
- To characterize the C. albicans C3bi receptor and compare it to human complement receptor type 3 (CR3).
Main Methods:
- Culturing C. albicans at different temperatures (30°C vs. 38.5°C).
- Assessing binding of EAC1423bi (complement-coated particles).
- Using monoclonal antibodies (e.g., OKM-1) against human CR3.
- Enzyme treatments (trypsin) and heat lability assays.
- Immunoprecipitation of C. albicans surface proteins.
Main Results:
- C. albicans grown at 30°C strongly bound EAC1423bi, while cells grown at 38.5°C did not.
- The binding molecule was heat labile and trypsin sensitive.
- Monoclonal antibodies to human CR3 alpha-chain showed temperature-dependent reactivity with C. albicans.
- Binding to C. albicans did not require divalent cations, unlike human CR3.
- OKM-1 antibody recognized a 130 kDa protein on C. albicans.
Conclusions:
- The C3bi receptor on C. albicans pseudohyphae is temperature-dependent and distinct from yeast cells.
- C. albicans C3bi receptors are antigenically related to human CR3 but possess different functional properties.
- These findings highlight temperature-regulated immune evasion strategies in C. albicans.