Characterization of Low-molecular-weight Peptides in Human Parotid Saliva

Perinpanayagam, Hiran; VanWuyckhuyse, B.C.; Ji, Ziyu; Tabak, Lawrence A.

doi:10.1177/00220345950740011001

Cited by 63 publications

(49 citation statements)

References 24 publications

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“…Other biofilm regulatory effects besides adhesion may thus be released upon proteolysis of statherin. Notably, statherin-derived peptides (due to endogenous or bacterial proteolysis) are present in saliva (22). The different statherin interaction modes may (to various degrees) reflect statherin-mimicking epitopes in other tissue components, as previously suggested for epithelial adhesion sites for C. albicans colonization (14).…”

Section: Discussionmentioning

confidence: 79%

Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious Actinomyces spp. Delineated by a Hybrid Peptide Construct

Niemi

Johansson

2004

Infect Immun

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Adhesion of microorganisms to host receptor molecules such as salivary statherin molecules is a common event in oral microbial colonization. Here we used a hybrid peptide construct (with both a hydroxyapatitebinding portion and a test peptide portion) to map the interaction of Actinomyces species (and Candida albicans) with statherin. Adhesion to hybrid peptides and truncated statherin variants revealed three binding types, types I to III. (i) Type I strains of rat, hamster, and human infection origins bound C-terminal-derived QQYTF and PYQPQY peptides. The QQYTF peptide inhibited statherin binding for some strains but not for others.(ii) Type II strains of human and monkey tooth origins bound middle-region-derived YQPVPE and QPLYPQ peptides. Neither strain was inhibited by soluble peptides. (iii) Type III strains of human infection origins (and C. albicans) did not bind to either statherin-derived peptides or truncated statherin. Moreover, the type I strains inhibited by QQYTF were also inhibited by TF and QAATF peptides and were detached from statherin by the same peptides. In conclusion, it is suggested that commensal and potentially infectious microorganisms bind middle or C-terminal statherin differently and that other microbes might require discontinuous epitopes.

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Section: Discussionmentioning

confidence: 79%

Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious Actinomyces spp. Delineated by a Hybrid Peptide Construct

Niemi

Johansson

2004

Infect Immun

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“…Proteins were depleted over night with 80 % chilled-ethanol (v/v) at -20°C [24]. Subsequently, the samples were centrifuged at 20.000 x g for 30 min at 4 °C and the residual protein concentration in the supernatant was determined using the Bradford assay (BCA Protein Assay Kit, Pierce, Rockford, IL).…”

Section: Sample Collection and Protein Depletionmentioning

confidence: 99%

Analysis of the Human Salivary Peptidome by Differential Peptide Display and LC-MS/MS Overview Sequencing

Yondre¹,

Tammen²,

Hess³

et al. 2008

TOPROTJ

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Abstract:In recent years interest in the characterization of the human salivary proteome has increased in order to explore its diagnostic potential. Major constituents of human saliva are highly polymorphic proteins that may have biological roles in oral lubrication and protection, e.g. proline-rich proteins (PRPs), statherins, histatins and cystatins. Interestingly, many of theses proteins are rapidly degraded in the oral cavity by host-and bacteria-or viral-derived proteases. Thus, comprehensive analysis of peptides up to 15 kDa (peptidomics) of whole saliva may yield basic information on proteolytic patterns. By employing a LC-ESI-MS/MS approach a total of 107 native peptides from 17 distinct protein precursors was identified from whole saliva. Subsequently the catalog of peptides was used to analyze inter-individual differences in saliva samples from four donors by differential peptide display technology. Genetic polymorphisms were found in peptides from the PRB4M_HUMAN and PROL4_HUMAN precursors. Analysis of the proposed N-and C-termini of the peptides revealed frequent cleavage after Lys or Arg which is characteristic for salivary kallikrein enzymes. Furthermore, we highlight the cleavage motif Gln/Gly in the PRP-C precursor, which suggests a new proteolytic pattern in saliva.

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“…Similar situations may exist with other proteins. Histatins and statherin are rapidly degraded in whole saliva, but less is known about how this process may vary from person to person, or how proteolysis may affect the function of those proteins (Oppenheim et al, 1988;Jensen etal, 1992;Xu et al, 1993;Perinpanayagam et al, 1995). From the standpoint of study design, the issue of polymorphism suggests that the important question may not always be how much of a particular protein but rather how much of the intact or degraded products of particular alleles a person has.…”

Section: (C) Protein Polymorphismsmentioning

confidence: 99%

Does Variability in Salivary Protein Concentrations Influence Oral Microbial Ecology and Oral Health?

Rudney

1995

Critical Reviews in Oral Biology & Medicine

114

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Salivary protein interactions with oral microbes in vitro include aggregation, adherence, cell-killing, inhibition of metabolism, and nutrition. Such interactions might be expected to influence oral ecology. However, inconsistent results have been obtained from in vivo tests of the hypothesis that quantitative variation in salivary protein concentrations will affect oral disease prevalence. Results may have been influenced by choices made during study design, including saliva source, stimulation status, control for flow rate, and assay methods. Salivary protein concentrations also may be subject to circadian variation. Values for saliva collected at the same time of day tend to remain consistent within subjects, but events such as stress, inflammation, infection, menstruation, or pregnancy may induce short-term changes. Long-term factors such as aging, systemic disease, or medication likewise may influence salivary protein concentrations. Such sources of variation may increase the sample size needed to find statistically significant differences. Clinical studies also must consider factors such as human population variation, strain and species differences in protein-microbe interactions, protein polymorphism, and synergistic or antagonistic interaction between proteins. Salivary proteins may form heterotypic complexes with unique effects, and different proteins may exert redundant effects. Patterns of protein-microbe interaction also may differ between oral sites. Future clinical studies must take those factors into account. Promising approaches might involve meta-analysis or multi-center studies, retrospective and prospective longitudinal designs, short-term measurement of salivary protein effects, and consideration of individual variation in multiple protein effects such as aggregation, adherence, and cell-killing.

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Characterization of Low-molecular-weight Peptides in Human Parotid Saliva

Cited by 63 publications

References 24 publications

Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious Actinomyces spp. Delineated by a Hybrid Peptide Construct

Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious Actinomyces spp. Delineated by a Hybrid Peptide Construct

Analysis of the Human Salivary Peptidome by Differential Peptide Display and LC-MS/MS Overview Sequencing

Does Variability in Salivary Protein Concentrations Influence Oral Microbial Ecology and Oral Health?

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