Sequence analysis of earthworm hemolysins

Issue title: Second International Conference on Biomedical Spectroscopy: From the Bench to the Clinic, London, UK, 5–8 July, 2003

Article type: Research Article

Authors: König, Simone^; | Wagner, Frank | Kauschke, Ellen | Eue, Ines

Affiliations: Integrated Functional Genomics, IZKF University of Münster, Germany | Zoological Institute, University of Greifswald, Germany | Institute of Anatomy, University of Greifswald, Germany | In den Wolfseichen 5, Lohmar, Germany

Note: [] Corresponding author: Dr. Simone König, Integrated Functional Genomics, Von‐Esmarch‐Str. 56, 48149 Muenster, Germany. Tel.: +49 (0)251 835 7164; Fax: +49 (0)251 835‐5651; E‐mail: koenigs@uni‐muenster.de.

Abstract: Annelids are capable of defending themselves from pathogens and of recognizing degenerated self tissue. These reactions require specialized immune mechanisms that are effected by proteins and cellular reactions. Hemolytic proteins are the most striking humoral defense molecules in the earthworm Eisenia fetida. Beside their hemolytic activity these proteins possess agglutinating, antibacterial, cytotoxic, and clotting properties. Hemolytic proteins both from coelomocytes (CL39,41) and coelomic fluid (H1−3) of wildtype E. fetida were isolated and assigned to fetidin and lysenin using mass spectrometry and bioinformatic tools. Glycosylation was found for H1. In silico analyses of the hemolysins revealed two hemolysin isoforms and consensus sites for N‐glycosylation and peroxidases proximal heme‐binding ligand.

Keywords: Eisenia fetida, hemolysins, mass spectrometry, isoforms, glycosylation, hydrogen peroxide

Journal: Spectroscopy, vol. 18, no. 2, pp. 347-353, 2004