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Biol. Bull. 215: 63-72. (August 2008)
© 2008 Marine Biological Laboratory

Cyclophilin and the Regulation of Symbiosis in Aiptasia pallida

S. Perez* and V. Weis

Department of Zoology, Oregon State University, Corvallis, Oregon 97331

* To whom correspondence should be addressed, at 300 Pasteur Drive, M-322 Alway Bldg., Stanford University Medical Center, Stanford, CA 94305-5120. E-mail: perezs{at}stanford.edu

The sea anemone Aiptasia pallida, symbiotic with intracellular dinoflagellates, expresses a peptydyl-prolyl cis-trans isomerase (PPIase) belonging to the conserved family of cytosolic cyclophilins (ApCypA). Protein extracts from A. pallida exhibited PPIase activity. Given the high degree of conservation of ApCypA and its known function in the cellular stress response, we hypothesized that it plays a similar role in the cnidarian-dinoflagellate symbiosis. To explore its role, we inhibited the activity of cyclophilin with cyclosporin A (CsA). CsA effectively inhibited the PPIase activity of protein extracts from symbiotic A. pallida. CsA also induced the dose-dependent release of symbiotic algae from host tissues (bleaching). Laser scanning confocal microscopy using superoxide and nitric oxide-sensitive fluorescent dyes on live specimens of A. pallida revealed that CsA strongly induced the production of these known mediators of bleaching. We tested whether the CsA-sensitive isomerase activity is important for maintaining the activity of the antioxidant enzyme superoxide dismutase (SOD). SOD activity of protein extracts was not affected by pre-incubation with CsA in vitro.

Abbreviations: ApCypA, Aiptasia pallida cyclophilin A • CsA, cyclosporine A • DAF-FM-DA, 4-amino-5-methylamino-2',7'-difluorofluorescein diacetate • DHEt, dihydroethidium • DTT, dithiothreitol • Et, ethidium • PPIase, peptydyl-prolyl cis-trans isomerase • SOD, superoxide dismutase • TBP, tert-butyl hydroperoxide






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