title: Mg2+ binding affects the structure and activity of ovomucin.
abstract: Metal-protein interaction for regulating the function and structure of proteins is of major interest. We demonstrate here that the addition of 9 μmol Mg2+ per mg ovomucin resulted in a 2.0-fold increase in the adhesion capacity of ovomucin to New Disease Virus (NDV) using ELISA method. The hemagglutinin inhibition rate of 100 μg/mL ovomucin-Mg2+ mixture (9 μmol Mg2+ per mg ovomucin) to NDV increased to 55.61%, which is significantly higher than that of the pure ovomucin (P<0.01). Binding characteristics of ovomucin to Mg2+ were then evident by fluorescence and FT-IR spectroscopy as well as dynamic light scattering (DLS) technology. Fluorescence and FT-IR spectroscopy results suggest that Mg2+ prefers to interact with the carbohydrate moiety of ovomucin without significant changes in the secondary structure when Mg2+ concentration is less than 9 μmol/mg ovomucin. When Mg2+ increases to 16 μmol/mg ovomucin, it gives rise to changes in secondary structure, and forms a more compact configuration. This is supported by the hydrodynamic radius of ovomucin with and without Mg2+ binding as examined by DLS. The Mg2+ bound in regulating the structure and activity of ovomucin provided important insight into the effect of metal ions on ovomucin binding to pathogens.
authors.affiliation: College of Food Science and Engineering, Northwest A&F University, Yangling 712100, PR China; National R&D Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, PR China. Electronic address: shanyy2013@163.com.
authors.forename: Yuanyuan
authors.initials: Y
authors.lastname: Shan
authors.affiliation: National R&D Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, PR China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Xu
authors.affiliation: National R&D Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, PR China. Electronic address: mameihuhn@163.com.
authors.forename: Meihu
authors.initials: M
authors.lastname: Ma
mesh_terms: D000998:Antiviral Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D008274:Magnesium / Q000737:chemistry* / Q000378:metabolism; D010059:Ovomucin / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D013329:Structure-Activity Relationship
chemical_list: D000998:Antiviral Agents; D010059:Ovomucin; D008274:Magnesium
keywords: Magnesium chloride; Ovomucin; Spectroscopy