Transglutaminase-mediated modification of ovomucoid: effects on its trypsin inhibitory activity and antigenic properties.

Abstract

Hen egg can cause food hypersensitivity in infants and young children, and ovomucoid is the most allergenic factor among proteins contained in egg white. Since proteinase treatment, a well-recognized strategy in reducing food allergenicity, is ineffective when applied to ovomucoid because of its ability to act as trypsin inhibitor, we investigated the possibility of reducing the ovomucoid antiprotease activity and antigenic properties by covalently modifying its structure. The present paper reports data showing the ability of the Gln115 residue of ovomucoid to act as an acyl donor substrate for the enzyme transglutaminase and, as a consequence, to give rise to a covalent monodansylcadaverine conjugate of the protein in the presence of both enzyme and the diamine dansylated derivative. Moreover, we demonstrated that the obtained structural modification of ovomucoid significantly reduced the capability of the protein to inhibit trypsin activity, also having impact on its anti-ovomucoid serum-binding properties.

• Authors: Raffaele Porta, Concetta Valeria L Giosafatto, Prospero di Pierro, Angela Sorrentino, Loredana Mariniello
• Journal: Amino acids (Amino Acids) Vol. 44 Issue 1 Pg. 285-92 (Jan 2013) ISSN: 1438-2199 [Electronic] Austria
• PMID: 22105613 (Publication Type: Journal Article)

Chemical References

• Antigens
• Bacterial Proteins
• Immune Sera
• Plant Proteins
• Trypsin Inhibitors
• phaseolin protein, Phaseolus vulgaris
• Ovomucin
• Transglutaminases
• Trypsin

Topics

• Animals
• Antigens (chemistry, immunology, pharmacology)
• Bacterial Proteins (chemistry)
• Egg Hypersensitivity (immunology)
• Immune Sera (chemistry)
• Ovomucin (chemistry, immunology, pharmacology)
• Plant Proteins (chemistry)
• Protein Binding
• Proteolysis
• Streptomyces (enzymology)
• Transglutaminases (chemistry)
• Trypsin (chemistry)
• Trypsin Inhibitors (chemistry, immunology, pharmacology)