Wild and domestic animals variably display Neu5Ac and Neu5Gc sialic acids

Author:

Nemanichvili Nikoloz12,Spruit Cindy M3,Berends Alinda J12,Gröne Andrea12,Rijks Jolianne M42,Verheije Monique H12,de Vries Robert P3ORCID

Affiliation:

1. Division of Pathology , Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, , Yalelaan 1, 3584 CL Utrecht, The Netherlands

2. Utrecht University , Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, , Yalelaan 1, 3584 CL Utrecht, The Netherlands

3. Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University , Universiteitsweg 99, 3584 CG Utrecht, The Netherlands

4. Dutch Wildlife Health Centre , Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, , Yalelaan 1, 3584 CL Utrecht, The Netherlands

Abstract

Abstract Sialic acids are used as a receptor by several viruses and variations in the linkage type or C-5 modifications affect the binding properties. A species barrier for multiple viruses is present due to α2,3- or α2,6-linked sialic acids. The C-5 position of the sialic acid can be modified to form N-acetylneuraminic acid (Neu5Ac) or N-glycolylneuraminic acid (Neu5Gc), which acts as a determinant for host susceptibility for pathogens such as influenza A virus, rotavirus, and transmissible gastroenteritis coronavirus. Neu5Gc is present in most mammals such as pigs and horses but is absent in humans, ferrets, and dogs. However, little is known about C-5 content in wildlife species or how many C-5 modified sialic acids are present on N-linked glycans or glycolipids. Using our previously developed tissue microarray system, we investigated how 2 different lectins specific for Neu5Gc can result in varying detection levels of Neu5Gc glycans. We used these lectins to map Neu5Gc content in wild Suidae, Cervidae, tigers, and European hedgehogs. We show that Neu5Gc content is highly variable among different species. Furthermore, the removal of N-linked glycans reduces the binding of both Neu5Gc lectins while retention of glycolipids by omitting methanol treatment of tissues increases lectin binding. These findings highlight the importance of using multiple Neu5Gc lectins as the rich variety in which Neu5Gc is displayed can hardly be detected by a single lectin.

Funder

European Commission

Beijerinck Premium of the Royal Dutch Academy of Sciences

Publisher

Oxford University Press (OUP)

Subject

Biochemistry

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