Related Experiment Video

Updated: Jul 20, 2025

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

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Structure of Bovine CD46 Ectodomain

Hazel Aitkenhead1,2,3, David I Stuart1,2, Kamel El Omari1,3

  • 1Diamond Light Source (United Kingdom), Harwell Science and Innovation Campus, Didcot OX110DE, UK.

Viruses
|July 29, 2023
PubMed

Insights

Bovine CD46 (bovCD46), a complement regulatory protein, acts as a viral entry receptor. Its structure reveals the bovine viral diarrhea virus binding site, aiding pestivirus control strategies.

Area of Science:

  • Structural Biology
  • Immunology
  • Virology

Background:

  • CD46 (membrane cofactor protein) is a complement regulatory protein involved in immune responses and pathogen binding.
  • Bovine CD46 (bovCD46) serves as a receptor for the bovine viral diarrhea virus (BVDV), a significant cattle pathogen.
  • Understanding CD46-virus interactions is crucial for controlling economically important diseases in livestock.

Purpose of the Study:

  • To determine the X-ray crystallographic structure of the extracellular region of bovine CD46.
  • To identify the interaction site between bovCD46 and the bovine viral diarrhea virus.
  • To provide structural insights for developing pestivirus control strategies.

Main Methods:

  • X-ray crystallography
  • Protein structure determination
  • Structural analysis of protein-ligand interactions

Main Results:

  • The extracellular region of bovCD46 adopts a four-short-consensus-repeat (SCR) structure, similar to human CD46.
  • SCR domains 1-3 exhibit a linear arrangement, while SCR 4 shows a reduced interface angle, creating a 'hockey stick' conformation.
  • The bovine viral diarrhea virus interaction site was localized to SCR1, suggesting host and pestivirus specificity.

Conclusions:

  • The determined structure of bovCD46 provides a molecular basis for its role as a pestivirus receptor.
  • Structural insights into the bovCD46-BVDV interaction can guide the development of targeted antiviral therapies and vaccines.
  • This research contributes to understanding pathogen-host interactions and disease control in cattle.

Keywords:
BVDVCD46X-ray structurebovine viral diarrhoea viruspestivirustype I membrane proteinvirus receptor

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