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Vaccine. 2015 Dec 8;33(49):7002-7. doi: 10.1016/j.vaccine.2015.08.095. Epub 2015 Sep 19.

S-acylation of influenza virus proteins: Are enzymes for fatty acid attachment promising drug targets?

Author information

1
Institute of Virology, Veterinary Medicine, Free University Berlin, Robert von Ostertag-Str. 7-13, Building 35, 14163 Berlin, Germany. Electronic address: mveit@zedat.fu-berlin.de.
2
Institute of Virology, Veterinary Medicine, Free University Berlin, Robert von Ostertag-Str. 7-13, Building 35, 14163 Berlin, Germany.

Abstract

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.

KEYWORDS:

DHHC-protein; Drug target; HA; Influenza virus; M2; Palmitoylation

PMID:
26387429
DOI:
10.1016/j.vaccine.2015.08.095
[Indexed for MEDLINE]

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