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Licensed Unlicensed Requires Authentication Published by De Gruyter August 3, 2021

The extracellular region of bovine milk butyrophilin exhibits closer structural similarity to human myelin oligodendrocyte glycoprotein than to immunological BTN family receptors

  • Andreas Eichinger ORCID logo , Irmgard Neumaier and Arne Skerra ORCID logo EMAIL logo
From the journal Biological Chemistry

Abstract

Bovine butyrophilin (BTN1A1) is an abundant type I transmembrane glycoprotein exposed on the surface of milk fat globules. We have solved the crystal structure of its extracellular region via multiple wavelength anomalous dispersion after incorporation of selenomethionine into the bacterially produced protein. The butyrophilin ectodomain exhibits two subdomains with immunoglobulin fold, each comprising a β-sandwich with a central disulfide bridge as well as one N-linked glycosylation. The fifth Cys residue at position 193 is unpaired and prone to forming disulfide crosslinks. The apparent lack of a ligand-binding site or receptor activity suggests a function predominantly as hydrophilic coat protein to prevent coagulation of the milk fat droplets. While there is less structural resemblance to members of the human butyrophilin family such as BTN3A, which play a role as immune receptors, the N-terminal bovine butyrophilin subdomain shows surprising similarity to the human myelin oligodendrocyte glycoprotein, a protein exposed on the surface of myelin sheaths. Thus, our study lends structural support to earlier hypotheses of a correlation between the consumption of cow milk and prevalence of neurological autoimmune diseases and may offer guidance for the breeding of cattle strains that express modified butyrophilin showing less immunological cross-reactivity.


Corresponding author: Arne Skerra, Lehrstuhl für Biologische Chemie, Technische Universität München, Emil-Erlenmeyer-Forum 5, D-85354 Freising, Germany, E-mail:

Funding source: Helmholtz-Zentrum Berlin für Materialien und Energie

Acknowledgments

The authors wish to thank Dr. Carolin Farke and Prof. Heinrich H.D. Meyer (TUM Lehrstuhl für Physiologie) for the donation of cDNA, Walter Stelzer (TUM Lehrstuhl für Chemie der Biopolymere) for MS analysis, Ina Theobald (TUM Lehrstuhl für Biologische Chemie) for experimental assistance and Dr. Manfred S. Weiss (Helmholtz-Zentrum Berlin, Germany) for technical support at BESSY beamline 14.1.

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: This work was financially supported by the Helmholtz-Zentrum Berlin.

  3. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

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Supplementary Material

The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2021-0122).


Received: 2021-01-24
Accepted: 2021-06-17
Published Online: 2021-08-03
Published in Print: 2021-09-27

© 2021 Walter de Gruyter GmbH, Berlin/Boston

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