Maturation of DENV proteins

Summary
Organism
Homo sapiens (human)
Reactome
R-HSA-9918432
PubChem
R-HSA-9918432
Description
  • Dengue virus (DENV) uses the host to fold and cleave its polyprotein, and mature the resulting fragments. The individual steps are highly conserved in all flaviviruses. The proteins prM, E, and NS1 are glycosylated with complex glycans or high-mannose sugars (reviewed in Yap et al., 2017; Feng et al., 2022). Dengue proteins can undergo further modifications like phosphorylation, sumoylation, ubiquitination, myristoylation or hydroxyprolylation (Aviner et al., 2021; reviewed in Kumar et al., 2020; Boytz & Rolle, 2024). C and NS5 also localize to the nucleus, and NS1 is secreted to extracellular space, where they interact with host factors. NS1, NS2A, NS2B, NS3, NS4A, NS4B, NS5 form the replication complex at foci near the ER membrane which later supports budding of virions into the ER lumen (reviewed in Cleaves, 1985; Roby et al., 2015).
Click on a node on the pathway to see its details. Glycoproteins are marked with a glycoprotein icon in their name.
Displaying all 6 entries
GlyCosmos Lectin UniProt ID Lectin Name Pathway Viewer
GL_000249 P27824 Calnexin view
GL_000272 P27797 Calreticulin view
GL_004645 O60762 Dolichol-phosphate mannosyltransferase subunit 1 view
GL_005149 O15460 Prolyl 4-hydroxylase subunit alpha-2 view
GL_005207 P13674 Prolyl 4-hydroxylase subunit alpha-1 view
GL_005280 Q7Z4N8 Prolyl 4-hydroxylase subunit alpha-3 view

About Release Notes Help Feedback

Click here to visit the beta site.


International Collaboration

GlyCosmos is a member of the GlySpace Alliance together with GlyGen and Glycomics@ExPASy.

Acknowledgements

Supported by JST NBDC Grant Number JPMJND2204

Partly supported by NIH Common Fund Grant #1U01GM125267-01


Logo License Policies Site Map

Contact: [email protected]

This work is licensed under Creative Commons Attribution 4.0 International


GlyCosmos Portal v4.5.0

Last updated: April 6, 2026