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Title: Collagen binding to Staphylococcus aureus

Abstract

Staphylococcus aureus can bind soluble collagen in a specific, saturable manner. We have previously shown that some variability exists in the degree of collagen binding between different strains of heat-killed, formaldehyde-fixed S. aureus which are commercially available as immunologic reagents. The present study demonstrates that live S. aureus of the Cowan 1 strain binds amounts of collagen per organism equivalent to those demonstrated previously in heat-killed, formaldehyde-fixed bacteria but has an affinity over 100 times greater, with Kd values of 9.7 X 10(-11) M and 4.3 X 10(-8) M for live and heat-killed organisms, respectively. Studies were also carried out with S. aureus killed by ionizing radiation, since this method of killing the organism seemed less likely to alter the binding moieties on the surface than did heat killing. Bacteria killed by exposure to gamma radiation bound collagen in a manner essentially indistinguishable from that of live organisms. Binding of collagen to irradiated cells of the Cowan 1 strain was rapid, with equilibrium reached by 30 min at 22 degrees C, and was fully reversible. The binding was not inhibited by fibronectin, fibrinogen, C1q, or immunoglobulin G, suggesting a binding site for collagen distinct from those for these proteins. Collagenmore » binding was virtually eliminated in trypsin-treated organisms, indicating that the binding site has a protein component. Of four strains examined, Cowan 1 and S. aureus ATCC 25923 showed saturable, specific binding, while strains Woods and S4 showed a complete lack of binding. These results suggest that some strains of S. aureus contain high-affinity binding sites for collagen. While the number of binding sites per bacterium varied sixfold in the two collagen-binding strains, the apparent affinity was similar.« less

Authors:
; ;
Publication Date:
Research Org.:
Cleveland Clinic Foundation, OH
OSTI Identifier:
7132994
Resource Type:
Journal Article
Journal Name:
Infect. Immun.; (United States)
Additional Journal Information:
Journal Volume: 2
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; COLLAGEN; CHEMICAL BONDS; STAPHYLOCOCCUS; BIOLOGICAL RADIATION EFFECTS; CELL KILLING; FORMALDEHYDE; GAMMA RADIATION; RECEPTORS; TEMPERATURE EFFECTS; ALDEHYDES; BACTERIA; BIOLOGICAL EFFECTS; ELECTROMAGNETIC RADIATION; IONIZING RADIATIONS; MEMBRANE PROTEINS; MICROORGANISMS; ORGANIC COMPOUNDS; PROTEINS; RADIATION EFFECTS; RADIATIONS; SCLEROPROTEINS; 560130* - Radiation Effects on Microorganisms; 560300 - Chemicals Metabolism & Toxicology

Citation Formats

Holderbaum, D, Hall, G S, and Ehrhart, L A. Collagen binding to Staphylococcus aureus. United States: N. p., 1986. Web.
Holderbaum, D, Hall, G S, & Ehrhart, L A. Collagen binding to Staphylococcus aureus. United States.
Holderbaum, D, Hall, G S, and Ehrhart, L A. 1986. "Collagen binding to Staphylococcus aureus". United States.
@article{osti_7132994,
title = {Collagen binding to Staphylococcus aureus},
author = {Holderbaum, D and Hall, G S and Ehrhart, L A},
abstractNote = {Staphylococcus aureus can bind soluble collagen in a specific, saturable manner. We have previously shown that some variability exists in the degree of collagen binding between different strains of heat-killed, formaldehyde-fixed S. aureus which are commercially available as immunologic reagents. The present study demonstrates that live S. aureus of the Cowan 1 strain binds amounts of collagen per organism equivalent to those demonstrated previously in heat-killed, formaldehyde-fixed bacteria but has an affinity over 100 times greater, with Kd values of 9.7 X 10(-11) M and 4.3 X 10(-8) M for live and heat-killed organisms, respectively. Studies were also carried out with S. aureus killed by ionizing radiation, since this method of killing the organism seemed less likely to alter the binding moieties on the surface than did heat killing. Bacteria killed by exposure to gamma radiation bound collagen in a manner essentially indistinguishable from that of live organisms. Binding of collagen to irradiated cells of the Cowan 1 strain was rapid, with equilibrium reached by 30 min at 22 degrees C, and was fully reversible. The binding was not inhibited by fibronectin, fibrinogen, C1q, or immunoglobulin G, suggesting a binding site for collagen distinct from those for these proteins. Collagen binding was virtually eliminated in trypsin-treated organisms, indicating that the binding site has a protein component. Of four strains examined, Cowan 1 and S. aureus ATCC 25923 showed saturable, specific binding, while strains Woods and S4 showed a complete lack of binding. These results suggest that some strains of S. aureus contain high-affinity binding sites for collagen. While the number of binding sites per bacterium varied sixfold in the two collagen-binding strains, the apparent affinity was similar.},
doi = {},
url = {https://www.osti.gov/biblio/7132994}, journal = {Infect. Immun.; (United States)},
number = ,
volume = 2,
place = {United States},
year = {Sat Nov 01 00:00:00 EST 1986},
month = {Sat Nov 01 00:00:00 EST 1986}
}