Complexity and Diversity of the Mammalian Sialome Revealed by Nidovirus Virolectins
By M. Langereis, M. Bakkers, Lingquan Deng, V. Padler-Karavani, S. Vervoort, R. Hulswit, Arno L. W. van Vliet, G. Gerwig, Stefanie A H de Poot, W. Boot and 10 more. 2015
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SUMMARY 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.
Subfields: Ecology, Genetics, Molecular Biology
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Citations in the corpus
- Biological roles of glycans (2016, background): “There are other examples of even more exquisite sialic acid specificity of viruses, based on the presence of O-acetyl esters at specific positions: while a 4-O-acetyl ester on sialic acid targets is required for mouse hepatitis virus infection (754-756), a 9-O-acetyl ester on the sialic acid side ch”
- Human coronaviruses OC43 and HKU1 bind to 9-O-acetylated sialic acids via a conserved receptor-binding site in spike protein domain A (2019, methodology): “Conventional sp-LBAs were performed using twofold serial dilutions of CoV S1–Fc proteins, as described previously (20, 47).”
- Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein (2017, unknown): “Our data indicate that MERS-CoV has evolved a binding site of low affinity but high selectivity for Neu5Ac that excludes Neu5Gc.”