Complexity and Diversity of the Mammalian Sialome Revealed by Nidovirus Virolectins

Martijn A. Langereis, Mark J G Bakkers, Lingquan Deng, Vered Padler-Karavani, Stephin J. Vervoort, Ruben J G Hulswit, Arno L W van Vliet, Gerrit J. Gerwig, Stefanie A H de Poot, Willemijn Boot, Anne Marie van Ederen, Balthasar A. Heesters, Chris M. van der Loos, Frank J M van Kuppeveld, Hai Yu, Eric G. Huizinga, Xi Chen, Ajit Varki, Johannis P. Kamerling, Raoul J. de Groot*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

3 Citations (Scopus)


Sialic acids (Sias), 9-carbon-backbone sugars, are among the most complex and versatile molecules of life. As terminal residues of glycans on proteins and lipids, Sias are key elements of glycotopes of both cellular and microbial lectins and thus act as important molecular tags in cell recognition and signaling events. Their functions in such interactions can be regulated by post-synthetic modifications, the most common of which is differential Sia-O-acetylation (O-Ac-Sias). The biology of O-Ac-Sias remains mostly unexplored, largely because of limitations associated with their specific in situ detection. Here, we show that dual-function hemagglutinin-esterase envelope proteins of nidoviruses distinguish between a variety of closely related O-Ac-Sias. By using soluble forms of hemagglutinin-esterases as lectins and sialate-O-acetylesterases, we demonstrate differential expression of distinct O-Ac-sialoglycan populations in an organ-, tissue- and cell-specific fashion. Our findings indicate that programmed Sia-O-acetylation/de-O-acetylation may be critical to key aspects of cell development, homeostasis, and/or function.

Original languageEnglish
Pages (from-to)1966-1978
Number of pages13
JournalCell Reports [E]
Issue number12
Publication statusPublished - 30 Jun 2015


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