Lectin Switching During Dengue Virus Infection

Dejnirattisai, Wanwisa; Webb, Andrew I.; Chan, Vera; Jumnainsong, Amonrat; Davidson, Andrew; Mongkolsapaya, Juthathip; Screaton, Gavin

Virus produced in C6/36 cells bound exclusively to GNA, implying that it contained predominantly high-or pauci-mannose N-glycans consistent with the glycosylation patterns seen in insect cells. Vero-produced virus was bound by 3 of the lectins tested-GNA, SNA, and DSA-suggesting that the virus contained a variety of high-mannose and complex-or hybrid-type N-glycans with or without a2,6-linked sialic acids, possibly on polyNacetyllactosamine outer chains. The DC-produced virus was bound only by SNA and DSA, indicating that there was a lack of high-mannose or hybrid N-glycans and that only complex-type N-glycans were present. All of the lectin binding signals occurred at the same position on the gels as E protein in the region of 60 kDa; we did not see any signal at 19 kDa where prM would be expected to migrate. However, this could be due to a low level of prM on these viruses.