HET0016 Ginger derived glycoproteins contain a variety

Ginger-derived HET0016 contain a variety of functional components, including specific phenolic compounds, purine compounds, and bioactive polysaccharides. Moreover, glycoproteins belong to the glycoconjugates, which combine some of the properties of polysaccharides and proteins. It has been reported that glycoproteins support various biological functions and activities, such as the maintenance of protein conformation and stability, hypolipidemic functions, and antioxidation (Ivashchenko et al., 2017).
Materials and methods
Results and discussion
Conclusion
Acknowledgement This paper was supported by The National Natural Science Funds of China (No. 31601479).
Introduction Natural honey is valued in traditional medicine all over the world since ancient times. The antimicrobial and antinematodal properties of honey are useful for the defense of honey bee against pathogenic microbes and parasitic nematodes (Glinski and Buczek, 2003; Zaghloul et al., 2001; Azim and Sajid, 2009). Parasitic nematodes cause a variety of infections in domestic animals, livestock, and humans (Kumar and Clark, 2005). Nematode infections of animals and plants result in enormous economic burden. Common parasitic nematodes for humans are ascarids (Ascaris), pinworms (Enterobius), whipworms (Trichuris trichiura), filarids, and hookworms (Bethony et al., 2006). These nematodes are common in developing countries causing high morbidity and mortality in both humans and domestic animals (Chan, 1997). Previously, we reported nematicidal activity of honey using C. elegans as a model nematode (Sajid and Azim, 2012; Azim and Sajid, 2009). We characterized potent growth inhibitory effect of different types of honey on all developmental stages of C. elegans (Azim and Sajid, 2009). The nematicidal activity of honey was found to be due to an abnormality in reproduction as demonstrated by defects in egg-laying and -hatching by C. elegans. Microscopic analysis revealed apoptosis in C. elegans gonads and intestinal lumen (Azim and Sajid, 2009). Amongst the less abundant components of honey, glycoproteins and glycopeptides were found to be involved in nematicidal activity instead of major carbohydrate components of honey (i.e. fructose, glucose, sucrose, and maltose) (Azim and Sajid, 2009). Natural honey contains an array of glycoproteins and glycopeptides with molecular masses of up to hundreds of kilodaltons (Mesaik et al., 2015; Won et al., 2009; Rossano et al., 2012; Mohammed and Azim, 2012; Marshall and Williams, 1987). Honey proteins originate from the hypopharyngeal gland of honey bees (Apis mellifera, Apis cerana, Apis florae and Apis dorsata) as well as from nectars and pollens of flowers (Won et al., 2009; Rossano et al., 2012). Honey proteins include enzymes involved in carbohydrate metabolism and immune response like glucose oxidase, catalase, invertase (saccharase), diastase (amylase) and glucosidases (Sajid and Azim, 2012; Babacan et al., 2002; Pontoh and Low, 2002). Natural honey contains ‘major royal jelly proteins’ (MRJPs) which are also found in other bee products particularly in royal jelly (Albert and Klauding, 2004). MRJPs are secretory proteins synthesized with signal peptides of 16–20 amino acid residues (Buttstedt et al., 2014). Mature MRJPs have theoretical molecular masses in the range of 45–70 kDa and composed of 400–578 amino acid residues. Pairwise sequence identities between MRJPs are in the range of 47–74% (Buttstedt et al., 2014). In royal jelly, MRJP1 is present in oligomeric form(s) (Simúth, 2001; Nozaki et al., 2012). MRJPs have a multimodal mechanism of actions other than their role as a nutritional element in the development of honey bee larvae (Buttstedt et al., 2013). Members of MRJP family included MRJP1 which is a weak acidic glycoprotein with growth factor-like properties (Buttstedt et al., 2013; Okamoto et al., 2003; Schmitzová et al., 1998). Some MRJPs are reported to affect biosynthesis of a variety of cytokines (Buttstedt et al., 2014). MRJP1 and MRJP2 were found to be major allergens in royal jelly allergy (Babacan et al., 2002). The MRJP3 has been reported to possess potent immunomodulatory activity while MRJP4 and MRJP5 have been considered to provide essential amino acids (Buttstedt et al., 2014; Okamoto et al., 2003; Schmitzová et al., 1998; Ferguson et al., 2011). Honey MRJP1 produced an immuno-stimulatory effect by increasing the production of TNFα in mice peritoneal macrophages and the protein moiety of this glycoprotein was found responsible for this property of honey (Hayashi et al., 2011). The MRJP1 has a high affinity for IgE and deglycosylation of N-linked sugars markedly reduced the binding of MRJP1 to IgE hence inhibited the allergic reaction (Hayashi et al., 2011; Tamura et al., 2009a; b). MRJPs have moderate sequence similarity (20%) with ‘Yellow’ or ‘Yellow-like’ proteins found throughout insects (Kumar and Clark, 2005; Buttstedt et al., 2014).