Publikationsdatenbank

S-acylation of influenza virus proteins: Are enzymes for fatty acid attachment promising drug targets? (2015)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Veit, Michael (WE 5)

Siche, Stefanie (WE 5)

Quelle

Vaccine; 33(49) — S. 7002–7007

ISSN: 0264-410x

Verweise

DOI: 10.1016/j.vaccine.2015.08.095

Pubmed: 26387429

Kontakt

Institut für Virologie

Robert-von-Ostertag-Str. 7-13
Gebäude 35
14163 Berlin
+49 30 838 51833
viro@zedat.fu-berlin.de

Abstract / Zusammenfassung

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.