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iTRAQ‐based quantitative proteomic analysis of a toxigenic dinoflagellate Alexandrium catenella and its non‐toxic mutant
Author(s) -
Zhang ShuFei,
Zhang Yong,
Xie ZhangXian,
Zhang Hao,
Lin Lin,
Wang DaZhi
Publication year - 2015
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.201500156
Subject(s) - dinoflagellate , mutant , biology , marine toxin , computational biology , proteomics , microbiology and biotechnology , toxin , biochemistry , ecology , gene
Paralytic shellfish toxins (PSTs) are a group of potent neurotoxic alkaloids produced by cyanobacteria and dinoflagellates. The PST biosynthesis gene cluster and several toxin‐related proteins have been unveiled in cyanobacteria, yet little is known about dinoflagellates. Here, we compared the protein profiles of a toxin‐producing dinoflagellate Alexandrium catenella (ACHK‐T) and its non‐toxic mutant (ACHK‐NT), and characterized differentially displayed proteins using a combination of the iTRAQ‐based proteomic approach and the transcriptomic database. Totally 3488 proteins were identified from A. catenella , and proteins involved in carbohydrate, amino acid and energy metabolism were the most abundant. Among them, 185 proteins were differentially displayed: proteins involved in amino acid biosynthesis, protein and carbohydrate metabolism and bioluminescence were more abundant in ACHK‐T, while proteins participating in photosynthesis, fatty acid biosynthesis, and the processes occurring in peroxisome displayed higher abundances in ACHK‐NT. Seven toxin‐related proteins were identified but they varied insignificantly between the two strains. Different carbon and energy utilization strategies were potentially related to the toxin producing ability, and the regulation mechanism of PST biosynthesis was more complex in dinoflagellates. Our study provides the first comprehensive dataset on the dinoflagellate proteome and lays the groundwork for future proteomic study.