Mucins have a polypeptide backbone, oligosaccharide side‐chains and peripheral structures that include sialic acids. Several pathogens have specific receptors for sialic acids, including human strains of influenza A virus which preferentially recognise and bind α2‐6 linked rather than α2‐3 linked sialic acids.1 The aim of this study was to identify possible disease‐related changes in the expression of sialic acids in nasal mucins.
Nasal mucosal samples were placed in organ culture. Metabolically‐labelled mucins were purified by gel filtration, blotted on to nitrocellulose membranes and probed with the sialic acid‐binding lectins Sambucus nigra and Maackia amurensis.
Ninety‐five mucosal samples were collected (49 turbinates, 31 nasal polyps, 15 samples from FESS). Lectin binding, expressed as optical density, showed significantly increased binding of S. nigra to cellular (P = 0.02; Kruskal–Wallis) and secreted (P = 0.045) mucin from allergic mucosa compared to non‐allergic mucosa. No significant differences were found in the binding patterns of M. amurensis.
This study has demonstrated increased expression of α2‐6 linked sialic acids in the mucins synthesised and secreted by allergic compared to non‐allergic nasal mucosa. This may cause a change in the way mucins and pathogens interact in allergic rhinitis, leading to altered susceptibility to upper respiratory tract infection.
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