Amsacta moorei entomopoxvirus encodes a functional heparin-binding glycosyltransferase (AMV248)


VIRUS GENES, vol.54, no.3, pp.438-445, 2018 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 54 Issue: 3
  • Publication Date: 2018
  • Doi Number: 10.1007/s11262-018-1561-4
  • Journal Name: VIRUS GENES
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.438-445
  • Keywords: Amsacta moorei entomopoxvirus, Glycosyltransferase, amv248, Heparin binding, Virus attachment, H3L ENVELOPE PROTEIN, CELL ENTRY, VIRUS, GENOME, GLYCOSAMINOGLYCANS, SULFATE, MORPHOGENESIS, REPLICATION, SEQUENCES, FUSION
  • Karadeniz Technical University Affiliated: Yes


Amsacta moorei entomopoxvirus (AMEV) infects certain lepidopteran and orthopteran insects and is the most studied member of the genus Betaentomopoxvirus. It has been considered as a potential vector for gene therapy, a vector to express exogenous proteins and a biological control agent. One of its open reading frames, amv248, encodes a putative glycosyltransferase and is the only known attachment protein conserved in AMEV and chordopoxviruses. The ORF was successfully expressed and the protein was shown to bind soluble heparin, both in silico and in vitro. Our results also showed that, while viral infection was inhibited by soluble glycosaminoglycans (GAGs), GAG-deficient cells were more resistant to the virus. Finally, we revealed that amv248 encodes an active heparin-binding glycosyltransferase which is likely to have a key role in the initiation of infection by AMEV.