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Journal of Biochemistry Advance Access published online on October 30, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm201
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© 2007 The Japanese Biochemical Society

Isolation, characterization and structure-elicitor activity relationships of hibernalin and its two oxidized forms from Phytophthora hibernalis Carne 1925

Renato Capasso1,§,*, Antimo Di Maro2,*, Gennaro Cristinzio3, Antonio De Martino1, Angela Chambery2, Addolorata Daniele2, Filomena Sannino4, Antonino Testa3,5 and Augusto Parente2

1Dipartimento di Scienze del Suolo, della Pianta, dell'Ambiente e delle Produzioni Animali, Facoltà di Agraria, Università degli Studi di Napoli "Federico II", I-80055 Portici (NA), Italy
2Dipartimento di Scienze della Vita, Facoltà di Scienze Matematiche, Fisiche e Naturali, Seconda Università di Napoli, 81100 Caserta, Italy
3Dipartimento di Arboricoltura, Botanica e Patologia Vegetale, Facoltà di Agraria, Università degli Studi di Napoli ‘‘Federico II'', 80055 Portici, Italy
4Dipartimento di Scienze del Suolo della Pianta dell'Ambiente e delle Produzioni Animali, Facoltà di Scienze Biotecnologiche, Università degli Studi di Napoli "Federico II" 80055 Portici, Italy
5Istituto di Biotecnologie Biochimiche, Facoltà di Agraria, Università Politecnica delle Marche, Ancona, Italy

§Corresponding author: Prof. Renato Capasso, Tel.: +39 081 2539173 office-183 lab; Fax. +39 081 2539186; E-mail: renato.capasso{at}unina.it

Received August 3, 2007; Accepted October 14, 2007


  Abstract

Three {alpha}-elicitins, named hibernalin1, hibernalin2 and hibernalin3 (hib1, hib2 and hib3, respectively), were isolated by reverse phase-low pressure liquid chromatography from culture filtrates of Phytophthora hibernalis Carne 1925, the causal agent of citrus lemon brown rot. Hib1 proved to be identical to syringicin previously isolated from culture filtrates of Phytophthora syringae. Hib2 and hib3 shared the same primary structure with hib1, but contained, at position 50, Met sulphoxide or sulphone, respectively. By SDS-PAGE, the three proteins showed the same electrophoretic mobility, corresponding to about 10 kDa. Exact Mr values were obtained by MALDI-TOF-MS (10,194.82 for hib1, 10,209.33 for hib2 and 10,223.80 for hib3), while by ESI-MS an Mr value of 10,194.90 was found for hib1 and no results for hib2 and hib3. The hibernalin forms showed a high propensity to self–association, after exposure to acetonitrile. Hib1 showed to be active in both the hypersensitivity response and electrolytes leakage assays; the sample containing hib1 and hib2 was only weakly active in the first assay and inactive in the second assay, while the sample containing all three hibernalin forms proved to be inactive in both tests. It is proposed that the different activities of the three hibernalin samples could be very likely attributed to both Met50 oxidation and aggregation.

Key Words: Amino acid sequence, Biological activity, Citrus lemon, Hibernalins, Phytophthora hibernalis

*R. Capasso and A. Di Maro contributed equally to the research work.


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