Backbone ¹H, ¹³C and ¹⁵N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin.

Dengue virus, belongs to Flaviviridae, is an arthropod transmitted virus that threatens millions of people's lives. As with other flaviviruses, a positive single-stranded 11-kilobases RNA in the dengue virus genome encodes three structural proteins (capsid protein C, membrane protein M, and envelope protein E) and seven non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5). The two component protease NS2B-NS3p is essential for viral replication and is believed to be a potential antiviral drug target. Aprotinin, a native inhibitor, is proved to retard the activity of NS2B-NS3p. The backbone assignments of NS2B-NS3p will be essential for determining the high resolution solution structure of NS2B-NS3p and screening new antiviral drugs. Herein, we report the backbone (1)H, (15)N, (13)C resonance assignments of the N terminal fragment of NS2B (4.8 kDa) and NS3p (18.5 kDa) in complex with aprotinin (6.5 kDa) by high resolution NMR.