Structure of Bovine CD46 Ectodomain

Author:

Aitkenhead Hazel123ORCID,Stuart David I.12,El Omari Kamel13ORCID

Affiliation:

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

2. Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford OX37BN, UK

3. The Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell, Didcot OX110FA, UK

Abstract

CD46, or membrane cofactor protein, is a type-one transmembrane protein from the complement regulatory protein family. Alongside its role in complement activation, CD46 is involved in many other processes, from T-cell activation to reproduction. It is also referred to as a pathogen magnet, because it is used as a receptor by multiple bacteria and viruses. Bovine CD46 (bovCD46) in particular is involved in bovine viral diarrhoea virus entry, an economically important disease in cattle industries. This study presents the X-ray crystallographic structure of the extracellular region of bovCD46, revealing a four-short-consensus-repeat (SCR) structure similar to that in human CD46. SCR1-3 are arranged linearly, while SCR 4 has a reduced interface angle, resulting in a hockey stick-like appearance. The structure also reveals the bovine viral diarrhoea virus interaction site in SCR1, which is likely to confer pestivirus specificity for their target host, CD46. Insights gained from the structural information on pestivirus receptors, such as CD46, could offer valuable guidance for future control strategies.

Funder

Biotechnology and Biological Sciences Research Council

Publisher

MDPI AG

Subject

Virology,Infectious Diseases

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