PrM- and cell-binding domains of the dengue virus E protein

J Virol. 1999 Mar;73(3):2547-51. doi: 10.1128/JVI.73.3.2547-2551.1999.

Abstract

The E-prM proteins of flaviviruses are unusual complexes which play important roles in virus assembly and fusion modulation and in potential immunity-inducing vaccines. Despite their importance, little is known about the biogenesis and structural organization of E-prM complexes. Pulse-chase radiolabeling of dengue virus-infected Vero cells demonstrated a rapid interassociation of E and prM proteins, and sucrose gradient sedimentation analysis suggested that E-prM complexes progressed from simple heteromers to more densely sedimenting structures indicating increased multimerization. E-prM heteromers of even higher complexity were observed in virus particles, suggesting an intracellular assembly process which results in the networking of E-prM subunits into a lattice-like structure found in virus particles. Trypsin cleavage of E-prM-containing virus particles resulted in the release of a soluble 45-kDa fragment of the E protein which retained cell-binding activity. The results suggest that E-prM interactions in dengue virus particles are largely mediated by domains in the carboxy-terminal anchoring domain of E, while cell-binding activity is retained in a trypsin-releasable ectodomain of the E protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Chlorocebus aethiops
  • Dengue Virus / physiology*
  • Receptors, Virus / physiology*
  • Trypsin / pharmacology
  • Vero Cells
  • Viral Proteins / physiology*
  • Virion / physiology

Substances

  • Receptors, Virus
  • Viral Proteins
  • Trypsin