Label-Free Quantitative Analysis of the Salivary Pellicle’s Proteome

ABSTRACT: The salivary pellicle, covering natural as well as restored tooth surfaces in the oral cavity as an immobilized protein-rich layer, acts as an important biological mediator at the tooth-saliva-interface. Going beyond previous non-quantitative analyses on pooled samples, we here analyzed the pellicle’s proteome of four individuals, separately on three consecutive days, and determined the relative protein abundance by a label-free quantitative nano-LC-MS/MS approach. We identified 72 major proteins in the initial pellicles formed after 3 min intraorally on ceramic specimens with high inter-individual and inter-day consistency, while significant differences in protein abundance were evident between subjects exhibiting unique individual pellicle profiles. Furthermore, we compared the relative protein abundance with corresponding saliva samples of the same individuals and provide first data on significantly enriched and depleted salivary proteins (p < 0.05) within the salivary pellicle. Our findings reveal the initial adsorption of salivary proteins to solid substrates to be a rapid, highly selective, and reproducible process leading to the immobilization of a broad range of protective proteins and enzymes on the substratum surface within a few minutes. This provides evidence that the pellicle layer might be physiologically functional even without further maturation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Saliva

SUBMITTER: Guillaume Médard  

LAB HEAD: Bernhard Kuster

PROVIDER: PXD004123 | Pride | 2022-03-01

REPOSITORIES: Pride