Haemin binding as a factor in the virulence ofPorphyromonas gingivalis
Autor: | John W. Smalley, Andrew J. Birss, Philip Marsh, Ailsa S. McKee |
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Rok vydání: | 1996 |
Předmět: |
Hemeproteins
Virulence Microbiology Heme-Binding Proteins chemistry.chemical_compound Genetics Molecular Biology Bacteroidaceae Porphyromonas gingivalis biology Strain (chemistry) Binding protein Cooperative binding biology.organism_classification Molecular Weight chemistry Hemin Carrier Proteins Bacterial outer membrane Oxidation-Reduction Bacterial Outer Membrane Proteins Protein Binding |
Zdroj: | FEMS Microbiology Letters. 141:65-70 |
ISSN: | 1574-6968 0378-1097 |
DOI: | 10.1111/j.1574-6968.1996.tb08364.x |
Popis: | Haemin (iron protoporphyrin IX) is an essential growth factor for the periodontal pathogen. Porphyromonas gingivalis. Iron protoporphyrin IX (IPP IX) binding to the avirulent P. gingivalis beige variant (W50/BE1) and the black-pigmenting parent wild-type strain W50 was quantified. W50/BE1 grown in a chemostat under haemin excess-bound IPP IX under both oxidising and reducing conditions but with both lower capacity and avidity than either the haemin-limited- and haemin-excess-grown parent strain W50. Rosenthal plots for W50/BE1 indicated cooperative binding. W50/BE1 cells expressed a 32 kDa outer membrane haemin-binding protein when grown under conditions of haemin excess, and this strain might serve as a useful source from which to isolate this protein. The reduced IPP IX binding ability of W50/BE1 may be the rate-limiting factor for haem uptake and explain the reduced virulence and slower rate of pigmentation of this strain. |
Databáze: | OpenAIRE |
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