TiO<sub>2</sub>‑Based
Phosphoproteomic Analysis
of Schistosomes: Characterization of Phosphorylated Proteins in the
Different Stages and Sex of <i>Schistosoma japonicum</i>
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Abstract
Protein phosphorylation is an important posttranslational
modification
in many organisms that regulates numerous cellular processes. However,
it remains poorly characterized in schistosomes, the causative agent
of schistosomiasis in humans and related animals. In the present study,
we characterized phosphorylated proteins in different stages and sex
of <i>Schistosoma japonicum</i> (<i>S. japonicum</i>) including schistosomula (14 days), adult females (35 days), and
adult males (35 days) by a titanium dioxide (TiO<sub>2</sub>) based
phosphoproteomic method. A total of 180 phosphopeptides were identified
in 148 proteins. Our further studies revealed that heat shock protein
90 (Hsp90), one of the phosphoproteins codetected in the different
stage and sex of schistosomes, may play an important role in the regulation
of schistosome development by directly or indirectly interacting with
other codetected signal molecules. Additionally, some phosphoproteins
were shown to be detected in a gender-specific manner, and the expressions
of these proteins were further validated either by immunohistochemistry
or by real-time reverse transcription polymerase chain reaction (RT-PCR)
at transcript levels between male and female schistosomes. In summary,
these findings as well as the providing of an inventory of phosphoproteins
are expected to provide new insights into schistosome development
and sexual maturation and then may result in the development of novel
interventions against schistosomiasis
