Dengue Virus Assembly, prM Protein Cleavage and Entry17 October 2014
The precursor membrane (prM) protein of dengue virus (DENV) is present on the surface of immature virions. The role of nine highly conserved residues in the alpha-helical domain (MH) of the prM protein in DENV replication was investigated by alanine-substitution mutagenesis. Five mutants affected the production of virus-like particles and replicon particles; eight mutants affected the entry, which correlated with the impairment in prM cleavage. Taken together, these MH domain residues can modulate prM cleavage, maturation and virus entry. The highly conserved nature of these residues suggests potential targets of antiviral strategy.
Hsieh SC, Wu YC, Zou G, Nerurkar VR, Shi PY, Wang WK. Highly conserved residues in the helical domain of dengue virus type 1 precursor membrane protein are involved in assembly, prM protein cleavage and entry. Journal of Biological Chemistry 2014 Oct 17. [Epub ahead of print]