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

tetano

Editor, Senior Moderator
Vaccine. 2015 Sep 17. pii: S0264-410X(15)01277-3. doi: 10.1016/j.vaccine.2015.08.095. [Epub ahead of print]
[h=1]S-acylation of influenza virus proteins: Are enzymes for fatty acid attachment promising drug targets?[/h] Veit M[SUP]1[/SUP], Siche S[SUP]2[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] 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.
Copyright ? 2015. Published by Elsevier Ltd.


[h=4]KEYWORDS:[/h] DHHC-protein; Drug target; HA; Influenza virus; M2; Palmitoylation

PMID: 26387429 [PubMed - as supplied by publisher]
 
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