4.2 Article

Differential proteomics analysis of female and male adults of Angiostrongylus cantonensis

Journal

EXPERIMENTAL PARASITOLOGY
Volume 131, Issue 2, Pages 169-174

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.exppara.2012.03.019

Keywords

Angiostrongylus cantonensis; Differential proteomics; Two-dimensional fluorescence difference gel electrophoresis; Matrix-assisted laser desorption ionization time-of-flight mass spectrometry

Categories

Funding

  1. The National Natural Science Foundation of China [30972575, 30800963]
  2. The Natural Science Foundation of Zhejiang Provincial Key Project [Z2100950]

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In this study, we identified the differentially expressed proteins of female and male adults of Angiostrongylus cantonensis through differential proteomics. We extracted and purified total proteins from male and female adults, separated proteins by two-dimensional difference gel electrophoresis (2D-DIGE) in pH 47, analyzed the gel images by DeCyder 7.0 software, and sacrificed the infected rats to count the number of male and female adults. It was found 28 protein spots that were differentially expressed; seven protein spots were then identified by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). Five proteins were up-regulated and two proteins down-regulated in male adults compared with female adults. Three of the five up-regulated proteins with known functions ascribed to them were identified as galectin-1, proteasome alpha subunit and peroxiredoxin. The two down-regulated proteins were identified as indoleamine dioxygenase like-myoglobin and galectin. Furthermore, the female was significantly greater than male adults (P < 0.01) in the rats. The findings demonstrate the differences in protein expression profiles and the ability to survive in the final host between female and male adults of A. cantonensis, and may provide a theoretical basis to study their developmental biology further. (C) 2012 Elsevier Inc. All rights reserved.

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