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Citation: WANG Zi-Jian, GAO Xiang, YANG Jing-Bo, SUN Wan-Chun, WU Dong-Lin, PENG Qi-Sheng, LIU Ning. Mass Spectrometric Analysis of S-Palmitoylation of Hemagglutinin from Influenza A Virus[J]. Chinese Journal of Analytical Chemistry, ;2016, 44(10): 1521-1527. doi: 10.11895/j.issn.0253-3820.160361 shu

Mass Spectrometric Analysis of S-Palmitoylation of Hemagglutinin from Influenza A Virus

1.
Central Laboratory, the Second Hospital of Jilin University, Changchun 130041, China;
2.
Key Laboratory of Zoonosis, Ministry of Education, Jilin University, Changchun 130062, China;
3.
Center for Disease Control and Prevention, Changchun 130025, China

Received Date: 11 May 2016
Revised Date: 14 July 2016

Fund Project: This work was supported by Natural Science Foundation of China (Nos. 21175055, 81673168, 31372409), the Jilin Province Science and Technology Department (No. 20110739, 20150204001YY), the Jilin University Bethune Project B (No. 2012210), and the Health and Family Planning Commission of Jilin Province (No.2015Z041).

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S-Palmitoylation in protein is one of the most important kinds of lipid modification and plays a vital role in cell signal transduction, metabolism and other processes, which is formed by covalent binding of palmitic acid with the sulfhydryl group of cysteine residue in protein through thioester bond. In the present study, acyl-biotin exchange reaction was performed to convert S-palmitic acid on the hemagglutinin protein from influenza A virus into biotin-labeled tag. The biotin-labeled protein was then enriched by streptavidin beads and further purified by electrophoresis, followed by in-gel digestion. The results showed that the ratio of biotin concentration of the sample with hydroxylamine treatment (+HA) to that of the sample without hydroxylamine treatment (-HA) was larger than 3. Mass spectrometric analysis of the digestion mixture of the enriched hemagglutinin protein from influenza A virus identified two s-palmitoylation modification sites that were located on carboxyl terminal region of hemagglutinin protein such as Cys₅₆₂ and Cys₅₆₅, respectively. This research offers a specific and effective method for large-scale analysis of S-palmitoylated proteins.
- Influenza virus,
- Hemagglutinin protein,
- Acyl-biotin exchange,
- S-Palmitoylation
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