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<p>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.</p>

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CCHFV GP38 and GP85 interact with cell-surface glycosaminoglycans

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年5月20日

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  • Olivier Reynard,
  • Romain R. Vivès,
  • Olga Makshakova,
  • Nosylys Gelas,
  • Estelle Gallice,
  • Anna Papa,
  • Christophe Peyrefitte,
  • Viktor E. Volchkov

摘要

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.