Salivary micelles: identification of complexes containing MG2, sIgA, lactoferrin, amylase, glycosylated proline-rich protein and lysozyme

Abstract

Micelles represent macromolecular structures in saliva and the aim of this study was to identify salivary proteins that occur in these globular particles. Micelles were isolated from whole saliva (WS) collected from three individuals and analysed in different experiments. Samples were subjected to polyacrylamide gel electrophoreses, hydrolysed to determine their amino acid composition and total protein concentration, examined by scanning electron microscopy and examined on Western blots probed with a panel of antibodies directed against salivary proteins. On Coomassie Brilliant Blue stained gels, the banding pattern of whole saliva and micelles was similar but the intensity of bands was quite different. Amino acid analysis confirmed that the amino acid composition of micelles was distinct from that of whole saliva. Scanning electron microscopy showed that micelles exhibit a complex pattern consisting of individual particles or clusters of particles with different sizes and shapes. Micelles contain proteins with high (MG2 and secretory IgA), intermediate (lactoferrin, amylase and glycosylated proline-rich protein (PRP)) and low (lysozyme) molecular weight that were immuno-detected on blots probed with specific antibodies. Micelles represent particulate multicomponent structures in whole saliva that contain a subset of salivary proteins known to be important components of the innate immune system and are likely to play an important role in the maintenance of homeostasis in the oral environment.