Neofunctionalization of the α1,2fucosyltransferase Paralogue in Leporids Contributes to Glycan Polymorphism and Resistance to Rabbit Hemorrhagic Disease Virus

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There are three members of the α1,2fucosyltransferases gene family in mammalian genomes, Fut1, Fut2 and Sec1. The encoded fucosyltransferases are key enzymes for the synthesis of glycans that can be used as ligands by pathogens. However, the polymorphism of expression of these fucosylated glycans on epithelial cell types contributes to protection at the species level. In most mammalian species Sec1 is a pseudogene and in humans, genetic variation of α1,2fucosylated glycans is provided by FUT2 polymorphisms. Rabbit haemorrhagic disease virus (RHDV) uses α1,2fucosylated glycans as attachment factors. It induces an acute disease with very high mortalities in rabbit populations. We now confirm an association between genetic markers in the rabbit Sec1-Fut2 genomic region and survival to RHDV. We show that the Fut1 gene is the main contributor to the synthesis of RHDV binding sites although individual variation is not achieved by Fut1 polymorphisms but by variation in levels of Sec1 transcription. The Sec1 protein acting as a dominant-negative of Fut1, high Sec1 expression leads to a decreased number of RHDV binding sites. Thus, unlike in other mammals, in rabbits Sec1 underwent neofunctionalization. It contributes to generate diversity of fucosylated glycans, a key mechanism for escaping pathogens such as RHDV.

Vyšlo v časopise: Neofunctionalization of the α1,2fucosyltransferase Paralogue in Leporids Contributes to Glycan Polymorphism and Resistance to Rabbit Hemorrhagic Disease Virus. PLoS Pathog 11(4): e32767. doi:10.1371/journal.ppat.1004759
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004759

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