NS1-mediated upregulation of ZDHHC22 acyltransferase in influenza a virus infected cells.
A549 Cells
Acylation
Animals
CRISPR-Cas Systems
Carnitine O-Palmitoyltransferase
/ genetics
Cell Line
Dogs
Gene Knockout Techniques
Humans
Influenza A virus
/ physiology
Madin Darby Canine Kidney Cells
Membrane Proteins
/ genetics
Up-Regulation
Viral Nonstructural Proteins
/ genetics
Virus Replication
Hemagglutinin
ZDHHC
acylation
influenza
mass spectrometry
Journal
Cellular microbiology
ISSN: 1462-5822
Titre abrégé: Cell Microbiol
Pays: India
ID NLM: 100883691
Informations de publication
Date de publication:
06 2021
06 2021
Historique:
revised:
19
02
2021
received:
22
09
2020
accepted:
22
02
2021
pubmed:
26
2
2021
medline:
15
12
2021
entrez:
25
2
2021
Statut:
ppublish
Résumé
Influenza A viruses contain two S-acylated proteins, the ion channel M2 and the glycoprotein hemagglutinin (HA). Acylation of the latter is essential for virus replication. Here we analysed the expression of each of the 23 members of the family of ZDHHC acyltransferases in human airway cells, the site of virus replication. RT-PCR revealed that every ZDHHC acyltransferase (except ZDHHC19) is expressed in A549 and Calu cells. Interestingly, expression of one ZDHHC, ZDHHC22, is upregulated in virus-infected cells; this effect is more pronounced after infection with an avian compared to a human virus strain. The viral protein NS1 triggers ZDHHC22 expression in transfected cells, whereas recombinant viruses lacking a functional NS1 gene did not cause ZDHHC22 upregulation. CRISPR/Cas9 technology was then used to knock-out the ZDHHC22 gene in A549 cells. However, acylation of M2 and HA was not reduced, as analysed for intracellular HA and M2 and the stoichiometry of S-acylation of HA incorporated into virus particles did not change according to MALDI-TOF mass spectrometry analysis. Comparative mass spectrometry of palmitoylated proteins in wt and ΔZDHHC22 cells identified 25 potential substrates of ZDHHC22 which might be involved in virus replication.
Substances chimiques
INS1 protein, influenza virus
0
Membrane Proteins
0
Viral Nonstructural Proteins
0
ZDHHC22 protein, human
EC 2.3.1.-
Carnitine O-Palmitoyltransferase
EC 2.3.1.21
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e13322Informations de copyright
© 2021 The Authors. Cellular Microbiology published by John Wiley & Sons Ltd.
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