Age- and Sex-Associated Differences in the Glycopatterns of Human Salivary Glycoproteins and Their Roles against Influenza A Virus

Abstract

Recent studies have elucidated that expression of certain glycoproteins in human saliva is increased or decreased according to age; meanwhile, human saliva may inhibit viral infection and prevent viral transmission. However, little is known about the age- and sex-associated differences in the glycopatterns of human salivary glycoproteins and their significant roles against influenza A virus (IVA). Here, we investigate the glycopatterns of human salivary glycoproteins with 180 healthy saliva samples divided into six age/sex groups using lectin microarrays and fabricate saliva microarrays to validate the terminal carbohydrate moieties of glycoproteins in individual saliva samples. Furthermore, we assess the inhibiting and neutralizing activity of saliva against two strains of influenza A (H9N2) virus. We find that seven lectins (e.g., MAL-II and SNA) show significant age differences in both females and males, and seven lectins (e.g., WFA and STL) show significant sex differences in children, adults and elderly people. Interestingly, we observe that elderly individuals have strongest resistance to IVA partly by presenting more terminal α2-3/6-linked sialic acid residues in their saliva, which bind with the influenza viral hemagglutinations. We conclude that age- and sex-associated differences in the glycopatterns of human salivary glycoproteins may provide pivotal information to help understand some age related diseases and physiological phenomena.

Comparison of the glycopattern alterations of mitochondrial proteins in cerebral cortex between rat Alzheimer’s disease and the cerebral ischemia model

“…In neurodegenerative diseases, mitochondrial dysfunction has been reported to occur early and to act causally in disease pathogenesis57. Furthermore, in multiple diseases, the glycopattern of proteins is different to that in normal samples394058, and the differentially expressed glycans may play an important role in the pathological process. Many studies have focused on the mitochondrial proteome to explore the pathogenesis of AD46 and ischemic stroke47; however, there has been little focus on the glycopattern of the mitochondrial glycoproteins in these two diseases.…”

“…A lectin microarray was produced to determine whether the mitochondrial protein glycopatterns changed in the SAD or MCAO rat models according to a previous protocol4054. To be specific, 37 lectins (Table S1; 29 from Vector Laboratories, Burlingame, CA, USA; seven from Sigma; one from Calbiochem, San Diego, CA, USA) that bind N - or O -linked glycans were used to produce the lectin microarray.…”

“…There are two major types of protein glycosylation, including N -glycosylation of the asparagine side-chains and O -glycosylation of the serine or threonine side-chains40. Glycosylation increases the diversity of proteins due to its different glycosidic bond, glycan structure, glycan composition, and glycan length40.…”

“…There are two major types of protein glycosylation, including N -glycosylation of the asparagine side-chains and O -glycosylation of the serine or threonine side-chains40. Glycosylation increases the diversity of proteins due to its different glycosidic bond, glycan structure, glycan composition, and glycan length40. Glycoproteins play important roles in cell-cell and cell-matrix interactions, cell adhesion, evasion of the immune response, development and morphogenesis, malignant transformation and metastasis, and other biological functions4142.…”

Glycopatterns of Urinary Protein as New Potential Diagnosis Indicators for Diabetic Nephropathy

“…Lectins were spotted on the homemade epoxysilane-coated slides with Stealth micro spotting pins (SMP-10B) (TeleChem, USA) by a Capital smart microarrayer (CapitalBio, Beijing). Please refer to Qin et al [22] for the sugar-binding specificities of the lectins, and layout of the lectin microarray was showed in Figure 1(a). Each lectin was spotted in triplicate per slide.…”