Premium
Proteomic analysis of differentially expressed proteins between the male and female worm of Schistosoma japonicum after pairing
Author(s) -
Cheng GuoFeng,
Lin JiaoJiao,
Feng XinGang,
Fu ZhiQiang,
Jin YaMei,
Yuan ChunXiu,
Zhou YuanCong,
Cai YouMin
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200400953
Subject(s) - proteome , biology , schistosoma japonicum , peptide mass fingerprinting , proteomics , two dimensional gel electrophoresis , spots , gel electrophoresis , tandem mass tag , microbiology and biotechnology , genetics , gene , immunology , quantitative proteomics , helminths , schistosomiasis , botany
Identification of differentially expressed proteins between the male and female worm of Schistosoma japonicum may provide new insights into the development of schistosomes, especially the molecular mechanism of female worm maturation induced by the male worm after pairing. Comparative two‐dimensional gel electrophoresis (2‐DE) and mass spectrometry were employed to separate and identify differentially expressed proteins between the male and female worm after pairing. Soluble and hydrophobic proteins from egg, schistosomulum (14 days), and female and male worms at adult stage (42 days) were separated by a sequential extraction method followed by 2‐DE and 2‐DE images were constructed. There were 1016 ± 67, 1808 ± 89, 1142 ± 45 and 1288 ± 32 spots detected for soluble proteins and 1425 ± 108, 952 ± 59, 847 ± 75 and 965 ± 69 spots for hydrophobic proteins from egg, schistosomulum, and adult stage female and male worms, respectively. The differentially and uniquely expressed proteins from male and female worms after pairing (42 days) include 41 ± 4 and 23 ± 2 unique spots for soluble proteins, and 11 ± 1 and 26 ± 3 unique spots for hydrophobic proteins, respectively. Matrix‐assisted laser desorption/ionization‐time of flight and electrospray ionization‐tandem mass spectrometry were employed to analyze 12 unique spots from the female worm and 16 unique spots from the male worm for peptide mass fingerprinting and sequencing. The results showed that the main functions of these differentially expressed proteins were in signal transduction, metabolism and transcriptional regulation etc . Comparison of the schistosomes proteome between male and female worms may permit the identification of protein candidates for the development of vaccines or new targets for drug development against schistosomiasis.