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Updated: May 22, 2026

Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
Published on: February 25, 2021
CCHFV GP38 and GP85 interact with cell-surface glycosaminoglycans
Olivier Reynard1,2, Romain R Vivès3, Olga Makshakova4
1ImmunoBiology of Viral Infection, CIRI, Centre International de Recherche en Infectiologie, INSERM U1111, CNRS, UMR5308, Univ Lyon, Université Claude Bernard Lyon, Lyon, France. olivier.reynard@inserm.fr.
Abstract:
Crimean Congo Hemorrhagic Fever Virus (CCHFV) is a negative-strand segmented RNA virus responsible for severe hemorrhagic fever in humans. The M genomic segment of CCHFV encodes a polyprotein precursor that is processed by cellular proteases into several structural and non-structural proteins. Among them, GP38 and its precursor GP85 are known to be secreted into the extracellular environment. We investigated their abilities to bind cells and we identified that they strongly bind to the cell plasma membrane through interaction with glycosaminoglycans (GAGs). This interaction was mapped to a surface-exposed basic cluster that combines both a prototypical GAG-binding domain and linearly distant amino acids. The present study describes for the first time the interaction between CCHFV GP38/85 proteins and host cell GAGs and characterizes the interaction domain.
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