Processing of flavivirus structural glycoproteins: stable membrane insertion of premembrane requires the envelope signal peptide

Virology
L MarkoffB Falgout

Abstract

The flavivirus structural proteins capsid (C), premembrane (prM), and envelope (E) are cleaved in that order from the N-terminus of the polyprotein by the ER intralumenal enzyme signal peptidase. The prM-E and E-NS1 junctions contain hydrophobic domains with both transmembrane and signal function. These domains reside at the C-termini of prM and E, respectively, after cleavage. We studied the functions of the 37-amino-acid C-terminus of the dengue virus type 4 (DEN4) prM (amino acids 243-279 of the DEN4 polyprotein) in the processing of prM and E. Hydrophobicity in this domain is interrupted by a conserved Arg residue (Arg-264) within a short amphipathic segment. Hydrophobic amino acids upstream from Arg-264 (aa 243-263) were presumed to constitute the membrane anchor for prM (the "tm" segment). Previous results had suggested that sequences downstream from Arg-264 (aa 265-279) constitute the E signal peptide. RNA transcripts prepared from wild-type (wt) and deletion-mutant DEN4 cDNAs encoding the prM signal peptide, prM, E, and the N-terminus of the nonstructural glycoprotein, NS1, were translated in rabbit reticulocyte lysate in the presence of microsomes. Processing of wt prM and E in vitro appeared to mimic processing occurr...Continue Reading

Citations

Aug 17, 2005·Journal of Virology·Carey L MedinAlan L Rothman
Nov 26, 2005·Expert Review of Anti-infective Therapy·Michael S Diamond
Jun 23, 2006·Reviews in Medical Virology·Joshua FinkSubhash G Vasudevan
May 20, 2003·Immunology and Cell Biology·Michael S Diamond
Jan 7, 1998·Journal of Virology·R P Valle, B Falgout
Feb 20, 2021·Virus Research·Debajit DeyS Saif Hasan
Jul 3, 2021·Viruses·Pham-Tue-Hung TranWessam Melik

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