4.7 Article

MG2 and lactoferrin form a heteropic complex in salivary secretions

Journal

JOURNAL OF DENTAL RESEARCH
Volume 82, Issue 6, Pages 471-475

Publisher

INT AMER ASSOC DENTAL RESEARCHI A D R/A A D R
DOI: 10.1177/154405910308200613

Keywords

protein-protein interactions; saliva; salivary proteins

Funding

  1. NIDCR NIH HHS [DE 14080, DE 44619, DE 07652, DE 11691] Funding Source: Medline

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Protein-protein interactions are necessary for homeostasis to be maintained and for biological systems to be integrated. Heterotypic complexes occur in saliva, and a complex between MG2 and SIgA has been suggested to promote microbial clearance from the oral cavity. In this study, we used a peptide display library to investigate previously unrecognized heterotypic complexes involving MG2 and other proteins. The library was panned with MG2 12 times, and analyses of clones identified the sequence Ala-Leu-Leu-Cys-, which occurs in salivary lactoferrin. Blotting experiments confirmed that MG2 and lactoferrin form a heterotypic complex in viro and in vivo. Periodate treatment of MG2 did not affect the interaction. A synthetic lactoferrin peptide containing the motif Ala-Leu-Leu-Cys- blocked the interaction between MG2 and lactoferrin, confirming the specificity of the interaction identified by panning. This complex may enhance the properties of these salivary components in the oral environment.

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