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Structural basis for the recognition of LDL-receptor family members by VSV glycoprotein

Jovan Nikolic1, Laura Belot1, Hélène Raux1

  • 1Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.

Nature Communications
|March 14, 2018
PubMed

Insights

Vesicular stomatitis virus (VSV) uses its glycoprotein G to bind low-density lipoprotein receptor (LDL-R) family members. Specific residues on VSV G are crucial for this interaction, guiding viral entry and potential gene therapy applications.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Vesicular stomatitis virus (VSV), an oncolytic rhabdovirus, utilizes its glycoprotein G (VSV G) for viral entry and is employed in gene therapy.
  • Low-density lipoprotein receptor (LDL-R) is a primary cellular receptor for VSV entry.

Purpose of the Study:

  • To elucidate the structural basis of VSV G interaction with LDL-R domains.
  • To identify key residues on VSV G essential for receptor binding and viral infectivity.

Main Methods:

  • X-ray crystallography to determine the structures of VSV G in complex with LDL-R CR2 and CR3 domains.
  • Site-directed mutagenesis to assess the role of specific VSV G residues in receptor interaction and viral infectivity.

Main Results:

  • Two crystal structures revealed identical binding sites for LDL-R CR2 and CR3 on VSV G.
  • Two basic residues on VSV G were identified as critical for binding to LDL-R CR2 and CR3.
  • Mutagenesis of these residues abolished VSV infectivity, suggesting all VSV receptors belong to the LDL-R family.

Conclusions:

  • VSV G has evolved specific interactions with the cysteine-rich domains of LDL-R family receptors.
  • Structural insights provide a foundation for engineering recombinant viruses with modified tropism for therapeutic purposes.

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