Cumulative Correlations of Lysozyme, Lactof errin, Peroxidase, S-IgA, Amylase, and Total Protein Concentrations with Adherence of Oral Viridans Streptococci to Microplates Coated with Human Saliva

Joel D Rudney, K. L. Hickey, Z. Ji

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Abstract

Redundancy refers to the observation that many salivary proteins exhibit similar properties in vitro. It is possible that bacterial adherence to salivary pellicle occurs as a cumulative effect of multiple proteins. This study determined the joint and individual contributions of salivary amylase, S-IgA, lysozyme, salivary peroxidase, lactoferrin, and total protein concentrations to adherence by oral viridans streptococci in microplates coated with whole saliva from 123 persons. Strains used were: Streptococcus gordonii Blackburn, 10558, Streptococcus mitis 10712,903, Streptococcus oralis 10557, 9811, and Streptococcus sanguis 10556, 13379. Rabbit antibody against 13379 was used for the detection of adherence. This antibody cross-reacted with all strains. Absorbance was standardized against saliva pooled from five donors. All saliva samples had been previously assayed for amylase, lactoferrin, lysozyme, secretory IgA, peroxidase, and total protein. Adherence scores for all strains except 13379 were significantly and positively correlated. Salivas binding high or low levels of one strain tended to bind others correspondingly. Multiple regression indicated significant contributions to 10558 adherence from total protein and lactoferrin (positive), and peroxidase and lysozyme (negative). Similar results were obtained for Blackburn and 903. Significant individual correlations were seen for 9811 and total protein (positive), 10557 and peroxidase (negative), and 13379 and lactoferrin (negative). Salivas with high adherence scores contained significantly more protein and lactoferrin, and significantly less peroxidase, than salivas with low adherence scores. These findings support the hypothesis that multiple proteins contribute to the adherence of streptococcal strains HI vivo.

Original languageEnglish (US)
Pages (from-to)759-768
Number of pages10
JournalJournal of dental research
Volume78
Issue number3
DOIs
StatePublished - Jan 1 1999

Fingerprint

Viridans Streptococci
Amylases
Muramidase
Saliva
Immunoglobulin A
Peroxidase
Lactoferrin
Proteins
Dental Pellicle
Streptococcus oralis
Streptococcus gordonii
Streptococcus mitis
Streptococcus sanguis
Salivary Proteins and Peptides
Secretory Immunoglobulin A
Antibodies
Joints
Rabbits

Keywords

  • Amylase
  • Lactoferrin
  • Lysozyme
  • Peroxidase
  • S-IgA
  • Saliva, adherence
  • Streptococcus gordonii
  • Streptococcus mitis
  • Streptococcus oralis
  • Streptococcus sanguis
  • Total protein
  • Viridans streptococci

Cite this

@article{3ebae6cb9b8642e4a733c8e609ab2008,
title = "Cumulative Correlations of Lysozyme, Lactof errin, Peroxidase, S-IgA, Amylase, and Total Protein Concentrations with Adherence of Oral Viridans Streptococci to Microplates Coated with Human Saliva",
abstract = "Redundancy refers to the observation that many salivary proteins exhibit similar properties in vitro. It is possible that bacterial adherence to salivary pellicle occurs as a cumulative effect of multiple proteins. This study determined the joint and individual contributions of salivary amylase, S-IgA, lysozyme, salivary peroxidase, lactoferrin, and total protein concentrations to adherence by oral viridans streptococci in microplates coated with whole saliva from 123 persons. Strains used were: Streptococcus gordonii Blackburn, 10558, Streptococcus mitis 10712,903, Streptococcus oralis 10557, 9811, and Streptococcus sanguis 10556, 13379. Rabbit antibody against 13379 was used for the detection of adherence. This antibody cross-reacted with all strains. Absorbance was standardized against saliva pooled from five donors. All saliva samples had been previously assayed for amylase, lactoferrin, lysozyme, secretory IgA, peroxidase, and total protein. Adherence scores for all strains except 13379 were significantly and positively correlated. Salivas binding high or low levels of one strain tended to bind others correspondingly. Multiple regression indicated significant contributions to 10558 adherence from total protein and lactoferrin (positive), and peroxidase and lysozyme (negative). Similar results were obtained for Blackburn and 903. Significant individual correlations were seen for 9811 and total protein (positive), 10557 and peroxidase (negative), and 13379 and lactoferrin (negative). Salivas with high adherence scores contained significantly more protein and lactoferrin, and significantly less peroxidase, than salivas with low adherence scores. These findings support the hypothesis that multiple proteins contribute to the adherence of streptococcal strains HI vivo.",
keywords = "Amylase, Lactoferrin, Lysozyme, Peroxidase, S-IgA, Saliva, adherence, Streptococcus gordonii, Streptococcus mitis, Streptococcus oralis, Streptococcus sanguis, Total protein, Viridans streptococci",
author = "Rudney, {Joel D} and Hickey, {K. L.} and Z. Ji",
year = "1999",
month = "1",
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doi = "10.1177/00220345990780030801",
language = "English (US)",
volume = "78",
pages = "759--768",
journal = "Journal of Dental Research",
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TY - JOUR

T1 - Cumulative Correlations of Lysozyme, Lactof errin, Peroxidase, S-IgA, Amylase, and Total Protein Concentrations with Adherence of Oral Viridans Streptococci to Microplates Coated with Human Saliva

AU - Rudney, Joel D

AU - Hickey, K. L.

AU - Ji, Z.

PY - 1999/1/1

Y1 - 1999/1/1

N2 - Redundancy refers to the observation that many salivary proteins exhibit similar properties in vitro. It is possible that bacterial adherence to salivary pellicle occurs as a cumulative effect of multiple proteins. This study determined the joint and individual contributions of salivary amylase, S-IgA, lysozyme, salivary peroxidase, lactoferrin, and total protein concentrations to adherence by oral viridans streptococci in microplates coated with whole saliva from 123 persons. Strains used were: Streptococcus gordonii Blackburn, 10558, Streptococcus mitis 10712,903, Streptococcus oralis 10557, 9811, and Streptococcus sanguis 10556, 13379. Rabbit antibody against 13379 was used for the detection of adherence. This antibody cross-reacted with all strains. Absorbance was standardized against saliva pooled from five donors. All saliva samples had been previously assayed for amylase, lactoferrin, lysozyme, secretory IgA, peroxidase, and total protein. Adherence scores for all strains except 13379 were significantly and positively correlated. Salivas binding high or low levels of one strain tended to bind others correspondingly. Multiple regression indicated significant contributions to 10558 adherence from total protein and lactoferrin (positive), and peroxidase and lysozyme (negative). Similar results were obtained for Blackburn and 903. Significant individual correlations were seen for 9811 and total protein (positive), 10557 and peroxidase (negative), and 13379 and lactoferrin (negative). Salivas with high adherence scores contained significantly more protein and lactoferrin, and significantly less peroxidase, than salivas with low adherence scores. These findings support the hypothesis that multiple proteins contribute to the adherence of streptococcal strains HI vivo.

AB - Redundancy refers to the observation that many salivary proteins exhibit similar properties in vitro. It is possible that bacterial adherence to salivary pellicle occurs as a cumulative effect of multiple proteins. This study determined the joint and individual contributions of salivary amylase, S-IgA, lysozyme, salivary peroxidase, lactoferrin, and total protein concentrations to adherence by oral viridans streptococci in microplates coated with whole saliva from 123 persons. Strains used were: Streptococcus gordonii Blackburn, 10558, Streptococcus mitis 10712,903, Streptococcus oralis 10557, 9811, and Streptococcus sanguis 10556, 13379. Rabbit antibody against 13379 was used for the detection of adherence. This antibody cross-reacted with all strains. Absorbance was standardized against saliva pooled from five donors. All saliva samples had been previously assayed for amylase, lactoferrin, lysozyme, secretory IgA, peroxidase, and total protein. Adherence scores for all strains except 13379 were significantly and positively correlated. Salivas binding high or low levels of one strain tended to bind others correspondingly. Multiple regression indicated significant contributions to 10558 adherence from total protein and lactoferrin (positive), and peroxidase and lysozyme (negative). Similar results were obtained for Blackburn and 903. Significant individual correlations were seen for 9811 and total protein (positive), 10557 and peroxidase (negative), and 13379 and lactoferrin (negative). Salivas with high adherence scores contained significantly more protein and lactoferrin, and significantly less peroxidase, than salivas with low adherence scores. These findings support the hypothesis that multiple proteins contribute to the adherence of streptococcal strains HI vivo.

KW - Amylase

KW - Lactoferrin

KW - Lysozyme

KW - Peroxidase

KW - S-IgA

KW - Saliva, adherence

KW - Streptococcus gordonii

KW - Streptococcus mitis

KW - Streptococcus oralis

KW - Streptococcus sanguis

KW - Total protein

KW - Viridans streptococci

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U2 - 10.1177/00220345990780030801

DO - 10.1177/00220345990780030801

M3 - Article

VL - 78

SP - 759

EP - 768

JO - Journal of Dental Research

JF - Journal of Dental Research

SN - 0022-0345

IS - 3

ER -