Fulltext

Proteolytic cleavage analysis at the Murray Valley encephalitis virus NS1-2A junction

Addis SN 1 , Lee E 2 , Bettadapura J 3 , Lobigs M 4

Affiliations 

  • 1 John Curtin School of Medical Research, The Australian National University, Canberra, ACT, Australia. khadijah@umt.edu.my
  • 2 Faculty of Education, Science, Technology and Mathematics, University of Canberra, Canberra, ACT, Australia. eva.lee@canberra.edu.au
  • 3 Emerging Viruses & Inflammation Research Group, Institute for Glycomics, Griffith University, Nathan, QLD, Australia. j.bettadapura@griffith.edu.au
  • 4 Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia. m.lobigs@uq.edu.au
Virol J, 2015;12:144.
PMID: 26377679 DOI: 10.1186/s12985-015-0375-4

Abstract

Our understanding of the proteolytic processing events at the NS1-2A junction in the flavivirus polyprotein has not markedly progressed since the early work conducted on dengue virus (DENV). This work identified an octapeptide sequence located immediately upstream of the cleavage site thought to be important in substrate recognition by an as yet unknown, endoplasmic reticulum-resident host protease. Of the eight amino acid recognition sequence, the highly conserved residues at positions P1, P3, P5, P7 and P8 (with respect to N-terminus of NS2A) are particularly sensitive to amino acid substitutions in terms of DENV NS1-NS2A cleavage efficiency; however, the role of the octapeptide in efficient NS1 and NS2A production of other flaviviruses has not been experimentally addressed.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

MeSH terms
Similar publications