1. Two-hybrid analysis of human salivary mucin MUC7 interactions
- Author
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Gwynneth D. Offner, Xiaojing Li, Lucila S Bruno, Robert F. Troxler, Frank G. Oppenheim, Li Wang, Camille C Siqueira, and Rodrigo Villamarim Soares
- Subjects
Saliva ,Proteolysis ,Molecular Sequence Data ,Saccharomyces cerevisiae ,MG2 ,Biology ,Blotting, Far-Western ,Protein–protein interaction ,Two-Hybrid System Techniques ,medicine ,Humans ,Amino Acid Sequence ,Far-western blotting ,Amylase ,Salivary Proteins and Peptides ,Molecular Biology ,Gene Library ,Sequence Homology, Amino Acid ,medicine.diagnostic_test ,Mucin ,Mucins ,Reproducibility of Results ,Cell Biology ,Salivary protein ,Submandibular gland ,Yeast ,medicine.anatomical_structure ,Biochemistry ,biology.protein ,Sequence Alignment ,Protein Binding - Abstract
MUC7 is a low molecular weight monomeric mucin secreted by submandibular, sublingual and minor salivary glands. This mucin has been implicated in the non-immune host defense system in the oral cavity since it binds and agglutinates a variety of oral microbes. To investigate interactions between this mucin and other secretory salivary proteins, a submandibular gland prey library was screened with baits encoding the N- and C-terminal regions of MUC7 in the yeast two-hybrid system. The N-terminal region interacted with several secretory salivary proteins, whereas the C-terminal region did not. Interacting proteins included amylase, acidic proline-rich protein 2, basic proline-rich protein 3, lacrimal proline-rich protein 4, statherin and histatin 1. Formation of complexes between these proteins and the N-terminal region of MUC7 was confirmed in Far Western blotting experiments. Interactions between mucin and non-mucin proteins in saliva could protect complex partners from proteolysis, modulate the biological activity of complexed proteins or serve as a delivery system for distribution of secretory salivary proteins throughout the oral cavity.
- Published
- 2005