Specific cell components of Bacteroides gingivalis mediate binding and degradation of human fibrinogen

Journal Article · Tue Jan 01 04:00:00 EST 1991 · Journal of Bacteriology; (USA)

OSTI ID:5474046

Lantz, M S; Allen, R D; Vail, T A; Switalski, L M; Hook, M ^[1]

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1. Univ. of Alabama at Birmingham (USA)

Bacteroides (Porphyromonas) gingivalis, which has been implicated as an etiologic agent in human periodontal diseases, has been shown to bind and degrade human fibrinogen. B. gingivalis strains bind fibrinogen reversibly and with high affinity and bind to a specific region of the fibrinogen molecule that appears to be located between the D and E domains. The authors now report that human fibrinogen is bound and then degraded by specific B. gingivalis components that appear to be localized at the cell surface. Fibrinogen binding to bacterial cells occurred at 4, 22, and 37{degree}C. A functional fibrinogen-binding component (M{sub r}, 150 000) was identified when sodium dodecyl sulfate-solubilized bacteria were fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, transferred to nitrocellulose membranes, and probed with {sup 125}I-fibrinogen. Fibrinogen degradation did not occur at 4{degree}C but did occur at 22 and 37{degree}C. When bacteria and iodinated fibrinogen were incubated at 37{degree}C, two major fibrinogen fragments (M{sub r}, 97 000 and 50 000) accumulated in incubation mixture supernatant fractions. Two major fibrinogen-degrading components (M{sub r}, 120 000 and 150 000) have been identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in substrate-containing gels. Fibrinogen degradation by the M{sub r}-120 000 and -150 000 proteases was enhanced by reducing agents, completely inhibited by N-{alpha}-p-tosyl-L-lysyl chloromethyl ketone, and partially inhibited by n-ethyl maleimide, suggesting that these enzymes are thiol-dependent proteases with trypsinlike substrate specificity. The fibrinogen-binding component could be separated from the fibrinogen-degrading components by selective solubilization of bacteria in sodium deoxycholate.

• OSTI ID: 5474046
• Journal Information: Journal of Bacteriology; (USA), Journal Name: Journal of Bacteriology; (USA) Vol. 173:2; ISSN JOBAA; ISSN 0021-9193
• Country of Publication: United States
• Language: English

Related Subjects

550901* -- Pathology-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
BACTERIA
BACTERIAL DISEASES
BETA DECAY RADIOISOTOPES
BIODEGRADATION
BLOOD COAGULATION FACTORS
CHEMICAL REACTIONS
COAGULANTS
DAYS LIVING RADIOISOTOPES
DECOMPOSITION
DISEASES
DRUGS
ELECTRON CAPTURE RADIOISOTOPES
ELECTROPHORESIS
ENZYMES
FIBRINOGEN
GLOBULINS
HEMATOLOGIC AGENTS
HEMOSTATICS
HYDROLASES
INFECTIOUS DISEASES
INTERMEDIATE MASS NUCLEI
INTERNAL CONVERSION RADIOISOTOPES
IODINE 125
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
MAMMALS
MAN
MICROORGANISMS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PATHOGENESIS
PATHOGENS
PEPTIDE HYDROLASES
PHYSIOLOGY
PRIMATES
PROTEINS
PROTEOLYSIS
RADIOISOTOPES
TRACER TECHNIQUES
VERTEBRATES