TITLE:
A two-dimensional electrophoresis reference map of the earthworm Eisenia fetida
AUTHORS:
Xing Wang, Yi Zhang, Zhenjun Sun
KEYWORDS:
2-DE; Invertebrates; Animal Proteomics; Eisenia fetida; MALDI-TOF/TOF-MS
JOURNAL NAME:
Natural Science,
Vol.4 No.11,
November
28,
2012
ABSTRACT: The molecular mechanisms underlying innate immunity in the earthworm E. fetida remain unclear. For the recognition of innate immunity in the earthworm E. fetida, a detailed knowledge of this proteome is a prerequisite. The absence of a high-resolution E. fetida proteome map prompted us to determine E. fetida protein spots that can be visualised on 2-D protein gels. In this study, we present a preliminary description of the whole earthworm E. fetida proteome. A highly detailed two-dimensional gel electrophoresis (2-DE) map of the E. fetida proteome was established and approximately 1500 protein spots were detected from the earthworm sample when applying a 500 μg protein 2-DE in the pH range 3.0 - 10.0. We present a 2-DE proteome map of E. fetida, identifying 76 different proteins by matrix-assisted laser desorption/ionization-tandem time of flight mass spectrometry (MALDI-TOF/ TOF-MS) analysis. These identified proteins, including heat shock protein 90 (Hsp90), chaperonine protein HSP60, caspase-8, fibrinolytic protease 0, gelsolin-like protein, lombricine kinase, coelomic cytolytic factor1 (CCF 1), manganous superoxide dismutase (MnSOD), triosephosphate isomerase, extracellular globin-4, lysenin, and intermediate filament protein, glyceraldehyde-3- phosphate dehydrogenase, et al., are involved in several processes, including transcripttion, translation, the tricarboxylic acid cycle, the cellular amino acid metabolic process, protein amino acid phosphorylation, glycolysis, and the glucose metabolic process. These 2-DE data will enhance future comparisons of immunity, toxicology, biotic processes and other challenges, thereby allowing for further study of the molecular mechanisms in response to environmental stressors, and it will be useful to investigate environmental proteomics in invertebrate earthworms.