Journal
VACCINE
Volume 33, Issue 49, Pages 7002-7007Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.vaccine.2015.08.095
Keywords
Influenza virus; HA; M2; Palmitoylation; DHHC-protein; Drug target
Categories
Funding
- Deutsche Forschungsgemeinschaft (DFG) [740 (TP C3), Ve 141/10-1]
Ask authors/readers for more resources
Covalent attachment of saturated fatty acids (palmitate and stearate) to hemagglutinin (HA) of influenza virus is a protein modification essential for viral replication. The enzymes catalysing acylation of viral proteins have not been identified, but likely candidates that acylate cellular substrates are members of a protein family that contain a DHHC (Asp-His-His-Cys) cysteine-rich domain. Since 23 DHHC-proteins with distinct, only partly overlapping substrate specificities are present in humans, only a few of them might acylate HA in airway cells of the lung. We argue here that these DHHC-proteins might be promising drug targets since their blockade should result in suppression of viral replication, while acylation of cellular proteins will not be (or very little) compromised. (C) 2015 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available