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Lysenin family proteins in earthworm coelomocytes - Comparative approach
Bianka Swiderska1, Sylwia Kedracka-Krok1, Tomasz Panz2
1Department of Physical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland; Laboratory of Proteomics and Mass Spectrometry, Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.
Abstract:
Sphingomyelin-binding proteins of the lysenin family were originally identified in earthworms belonging to the genus Eisenia comprised of at least two distinct species, E. andrei and E. fetida, until recently considered subspecies or morphotypes of E. foetida (sic). In the present study the presence of lysenin and lysenin-related protein 2 (LRP-2, known also as fetidin) was detected in coelomocytes retrieved from all investigated adult specimens of E. andrei, and E. fetida. They were accompanied by LRP-3 and LRP-1 in some specimens of E. andrei and E. fetida, respectively. Lysenins were not observed in a third composting lumbricid species, Dendrobaena veneta, which served as a convenient negative reference for techniques and procedures used in the study. The pore-forming potential of soluble and cellular fractions of coelomic fluid was studied towards sheep red blood cells and sphingomyelin-rich liposomes. After experimental depletion the potential was restored in parallel with restoration of chloragocyte-derived eleocytes in both E. andrei and E. fetida.
