Professor
Supervisor of Doctorate Candidates
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DOI number:10.1002/pmic
Key Words:glycosylation; intact glycopeptide; mass spectrometry; neuraminidase.
Abstract:Influenza H1N1 virus has posed a serious threat to human health. The glycosylation of neuraminidase (NA) could affect the infectivity and virulence of the influenza virus, but detailed site-specific glycosylation information of NA is still missing. In this study, intact glycopeptide analysis is performed on an influenza NA (A/H1N1/California/2009) that is expressed in human 293T and insect Hi-5 cells. The data indicate that three of four potential N-linked glycosylation sites are glycosylated, including one partial glycosylation site from both cell lines. The NA expressed in human cells has more complex glycans than that of insect cells, suggesting the importance of selecting an appropriate expression system for the production of functional glycoproteins. Different types of glycans are identified from different glycosites of NA expressed in human cells, which implies the site-dependence of glycosylation on NA. This study provides valuable information for the research of influenza virus as well as the functions of viral protein glycosylation.
Indexed by:Journal paper
Discipline:Natural Science
First-Level Discipline:Biology
Document Type:J
Translation or Not:no
Date of Publication:2019-02-19
Included Journals:SCI
Pre One:37. Shisheng Sun*, Yingwei Hu, Minghui Ao, Punit Shah, Jing Chen, Weiming Yang, Xingwang Jia, Yuan Tian, Stefani Thomas, Hui Zhang*. N-GlycositeAtlas: a database resource for mass spectrometry-based human N-linked glycoprotein and glycosylation site mapping. Clinical Proteomics. 2019, 16 (1): 1-11.
Next One:35. Jingchao Li, Zhonghua Li, Xiaotao Duan, Ke Qin, Liuyi Dang, Shisheng Sun, Li Cai, Linda C Hsieh-Wilson, Liming Wu, Wen Yi*. An Isotope-Coded Photocleavable Probe for Quantitative Profiling of Protein O-GlcNAcylation. ACS Chemical Biology. 2019, 14(1): 4-10.
