tetano
Editor, Senior Moderator
Proteomics. 2018 Dec 21:e1800202. doi: 10.1002/pmic.201800202. [Epub ahead of print]
[h=1]Intact glycopeptide analysis of influenza A/H1N1/09 neuraminidase revealing the effects of host and glycosite location on site-specific glycan structures.[/h] Zhu B[SUP]1[/SUP], Shen J[SUP]1[/SUP], Zhao T[SUP]1[/SUP], Jiang H[SUP]2[/SUP], Ma T[SUP]1[/SUP], Zhang J[SUP]3[/SUP], Dang L[SUP]1[/SUP], Gao N[SUP]1[/SUP], Hu Y[SUP]4[/SUP], Shi Y[SUP]2[/SUP], Sun S[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza H1N1 virus has posed serious threat to human health. The glycosylation of neuraminidase (NA) could affect the infectivity and virulence of influenza virus, but detailed site-specific glycosylation information of NA is still missing. In this study, intact glycopeptide analysis was performed on an influenza NA (A/H1N1/California/2009) that was expressed in human 293T and insect Hi-5 cells. Our data indicated that three of four potential N-linked glycosylation sites were glycosylated, including one partial glycosylation site from both cell lines. The NA expressed in human cells had 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 were identified from different glycosites of NA expressed in human cells, which implied 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. This article is protected by copyright. All rights reserved.
[h=4]KEYWORDS:[/h] glycosylation; intact glycopeptide; mass spectrometry; neuraminidase
PMID: 30578591 DOI: 10.1002/pmic.201800202
[h=1]Intact glycopeptide analysis of influenza A/H1N1/09 neuraminidase revealing the effects of host and glycosite location on site-specific glycan structures.[/h] Zhu B[SUP]1[/SUP], Shen J[SUP]1[/SUP], Zhao T[SUP]1[/SUP], Jiang H[SUP]2[/SUP], Ma T[SUP]1[/SUP], Zhang J[SUP]3[/SUP], Dang L[SUP]1[/SUP], Gao N[SUP]1[/SUP], Hu Y[SUP]4[/SUP], Shi Y[SUP]2[/SUP], Sun S[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza H1N1 virus has posed serious threat to human health. The glycosylation of neuraminidase (NA) could affect the infectivity and virulence of influenza virus, but detailed site-specific glycosylation information of NA is still missing. In this study, intact glycopeptide analysis was performed on an influenza NA (A/H1N1/California/2009) that was expressed in human 293T and insect Hi-5 cells. Our data indicated that three of four potential N-linked glycosylation sites were glycosylated, including one partial glycosylation site from both cell lines. The NA expressed in human cells had 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 were identified from different glycosites of NA expressed in human cells, which implied 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. This article is protected by copyright. All rights reserved.
[h=4]KEYWORDS:[/h] glycosylation; intact glycopeptide; mass spectrometry; neuraminidase
PMID: 30578591 DOI: 10.1002/pmic.201800202