Mass spectrometric analysis of host cell proteins interacting with dengue virus nonstructural protein 1 in dengue virus-infected HepG2 cells

2016 ◽  
Vol 1864 (9) ◽  
pp. 1270-1280 ◽  
Author(s):  
Thanyaporn Dechtawewat ◽  
Atchara Paemanee ◽  
Sittiruk Roytrakul ◽  
Pucharee Songprakhon ◽  
Thawornchai Limjindaporn ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Host Cell ◽  
Hepg2 Cells ◽  
Nonstructural Protein ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Host Cell Proteins ◽  
Nonstructural Protein 1

The dengue virus nonstructural protein 1 (NS1) increases NF-κB transcriptional activity in HepG2 cells

2011 ◽  
Vol 156 (7) ◽  
pp. 1275-1279 ◽  
Author(s):  
Breno M. Silva ◽  
Lirlândia P. Sousa ◽  
Alessandra C. Gomes-Ruiz ◽  
Flávia G. G. Leite ◽  
Mauro M. Teixeira ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Hepg2 Cells ◽  
Transcriptional Activity ◽  
Nonstructural Protein ◽  
Nonstructural Protein 1

A Questionnaire Survey on General Status and Opinions about Clinical Mass Spectrometric Analysis in Korea (2018)

2019 ◽  
Vol 9 (3) ◽  
pp. 161
Author(s):  
Sung-Eun Cho ◽  
Hyojin Chae ◽  
Hyung-Doo Park ◽  
Sail Chun ◽  
Yong-Wha Lee ◽  
...  
Keyword(s):  
Questionnaire Survey ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
General Status

Mechanisms of Dopant Depth Profile Modification During Mass Spectrometric Analysis of Multilayer Structure

2015 ◽  
Vol 60 (6) ◽  
pp. 511-520 ◽  
Author(s):  
A.A. Efremov ◽  
◽  
V.G. Litovchenko ◽  
V.P. Melnik ◽  
O.S. Oberemok ◽  
...  
Keyword(s):  
Depth Profile ◽  
Multilayer Structure ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Profile Modification

Mass Spectrometric Analysis of Porcine Rhodopsin¶

2002 ◽  
Vol 75 (3) ◽  
pp. 316 ◽  
Author(s):  
Zsolt Ablonczy ◽  
Patrice Goletz ◽  
Daniel R. Knapp ◽  
Rosalie K. Crouch
Keyword(s):  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis

MASS SPECTROMETRIC ANALYSIS OF OPIOID PEPTIDE-CONTAINING PROTEINS

Analgesia ◽  
1995 ◽  
Vol 1 (4) ◽  
pp. 390-393 ◽  
Author(s):  
Dominic M. Desiderio ◽  
Lin Yan ◽  
Genevieve Fridland ◽  
Jih-Lie Tseng
Keyword(s):  
Opioid Peptide ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis

scholarly journals Potential Phosphorylation of Viral Nonstructural Protein 1 in Dengue Virus Infection

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1393
Author(s):  
Thanyaporn Dechtawewat ◽  
Sittiruk Roytrakul ◽  
Yodying Yingchutrakul ◽  
Sawanya Charoenlappanit ◽  
Bunpote Siridechadilok ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Nonstructural Protein ◽  
Antiviral Drug ◽  
Denv Infection ◽  
Site Directed Mutagenesis ◽  
Phosphorylation Sites ◽  
Post Translational Modification ◽  
Multifunctional Protein ◽  
Nonstructural Protein 1 ◽  
Underlying Mechanisms

Dengue virus (DENV) infection causes a spectrum of dengue diseases that have unclear underlying mechanisms. Nonstructural protein 1 (NS1) is a multifunctional protein of DENV that is involved in DENV infection and dengue pathogenesis. This study investigated the potential post-translational modification of DENV NS1 by phosphorylation following DENV infection. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS), 24 potential phosphorylation sites were identified in both cell-associated and extracellular NS1 proteins from three different cell lines infected with DENV. Cell-free kinase assays also demonstrated kinase activity in purified preparations of DENV NS1 proteins. Further studies were conducted to determine the roles of specific phosphorylation sites on NS1 proteins by site-directed mutagenesis with alanine substitution. The T27A and Y32A mutations had a deleterious effect on DENV infectivity. The T29A, T230A, and S233A mutations significantly decreased the production of infectious DENV but did not affect relative levels of intracellular DENV NS1 expression or NS1 secretion. Only the T230A mutation led to a significant reduction of detectable DENV NS1 dimers in virus-infected cells; however, none of the mutations interfered with DENV NS1 oligomeric formation. These findings highlight the importance of DENV NS1 phosphorylation that may pave the way for future target-specific antiviral drug design.

Sign in / Sign up

Export Citation Format

Share Document