title: The interaction of salivary secretions with the human complement system--a model for the study of host defense systems on inflamed mucosal surfaces.
abstract: When complement first contacts salivary secretions, as when gingival crevicular fluid first meets saliva at the gingival margin, complement function is enhanced. The immediate potentiation of the complement system at equal volume ratios of serum to saliva is due to several factors, including the lower ionic strength of saliva when compared with serum and the presence of certain salivary glyproteins such as the nonimmunoglobulin agglutinins that appear to simultaneously activate C1 and affect (sequester) certain complement control proteins, such as Factor H. This initial potentiation of the complement cascade by saliva may aid in defending the area immediately above the gingival crevice from oral microbiota that are being coated with a combination of serous exudate components and salivary components. As serum becomes much more diluted with saliva (i.e., crevicular fluid moves away from the supragingival area), the acidic proline-rich salivary proteins (APRP) begin to disrupt the unbound C1q-C1r2-C1s2 macromolecular complexes. Thus, the APRP along with other C1 fixing substances in saliva appear to restrict complement function, but only when the ratios of saliva to serum exceed 250:1. Since certain salivary glycoproteins bind to viruses, the potentiation of the complement system by saliva may also play a role in neutralizing certain viral infections on mucosal surfaces where tissue transudates containing complement begin to contact mucosal secretions such as saliva. Again, the ratio of serous fluid to mucosal secretion appears to be an important factor. This article also discusses some of our preliminary data and speculations concerning the binding of the self-associating high-molecular-weight nonimmunoglobulin salivary agglutinins (NIA) with the envelope of the human immunodeficiency virus (HIV) and the possible cooperative role of C1q and fibronectin in aiding neutralization of HIV infectivity.
authors.affiliation: Department of Microbiology and Immunology, College of Dental Medicine, Medical University of South Carolina, Charleston.
authors.forename: R J
authors.initials: RJ
authors.lastname: Boackle
mesh_terms: D003167:Complement Activation / Q000502:physiology; D003165:Complement System Proteins / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D012463:Saliva / Q000276:immunology / Q000502:physiology*; D013280:Stomatitis / Q000276:immunology
chemical_list: D003165:Complement System Proteins