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 earthwormEisenia 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 wildtypeE. fetidawere isolated and assigned to fetidin and lysenin using mass spectrometry and bioinformatic tools. Glycosylation was found for H1.In silicoanalyses of the hemolysins revealed two hemolysin isoforms and consensus sites for N-glycosylation and peroxidases proximal heme-binding ligand.
Highlights
Earthworms, and, all annelids, are interesting immunological study objects
Abbreviations CF, coelomic fluid; CL, coelomocyte lysate; CL39,41, 39 and 41 kDa hemolysins isolated from coelomocyte lysate; H1−3, three hemolytic CF proteins; LRP, lysenin-related protein; MS, mass spectrometry
Guanine 621 in fetidin is replaced by adenine 672 in LPR1
Summary
Earthworms, and, all annelids, are interesting immunological study objects. They are capable of defending themselves from pathogens and of recognizing degenerated self tissue. Abbreviations CF, coelomic fluid; CL, coelomocyte lysate; CL39,41, 39 and 41 kDa hemolysins isolated from coelomocyte lysate; H1−3, three hemolytic CF proteins; LRP, lysenin-related protein; MS, mass spectrometry. Hemolytic proteins are the most striking humoral defense molecules in the earthworm Eisenia fetida. Hemolytical and agglutinating proteins in E. fetida were originally described by DuPasquier and Duprat [3].
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