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Porphyromonas gingivalis as a Model Organism for Assessing Interaction of Anaerobic Bacteria with Host Cells
Published on: December 17, 2015
Characterization of FimA in Porphyromonas gingivalis genotype IV
Young-Suk Choi1, Ji-Hoi Moon, Jae-Hong Park
1Department of Maxillofacial Biomedical Engineering, School of Dentistry, Kyung Hee University, Seoul, Korea.
Abstract:
It has been reported that a large majority of periodontitis patients carry organisms with either type II or IV-fimA, while type I is the most prevalent fimA genotype among Porphyromonas gingivalis-positive healthy adults. Here we report characterization of recombinant fimbrial protein (rFimA) produced in Escherichia coli from genotype IV-fimA. In SDS-PAGE and immunoblot analysis after partial dissociation, type IV-rFimA showed a ladder-like pattern representing oligomeric/polymeric forms of native fimbrial structure. Unlike anti-type I-native fimbriae which can only recognize conformational epitopes of the respective proteins, both anti-type IV-native fimbriae and anti-type IV-rFimA antibodies recognized conformational as well as linear epitopes in type IV-fimbriae. These results suggest that the type IV-rFimA proteins retain the native fimbrial antigenicity and the antigenicity of type IV-fimbriae is different from that of type I-fimbriae.
Insights
Type IV fimA genotype proteins from Porphyromonas gingivalis were characterized. These recombinant fimbrial proteins (rFimA) retain native antigenicity and differ from type I fimbriae, impacting periodontitis patient immunity.
Area of Science:
- Microbiology
- Immunology
- Structural Biology
Background:
- Periodontitis is often associated with specific fimA genotypes of Porphyromonas gingivalis.
- Type I fimA is prevalent in healthy adults, while types II and IV are common in periodontitis patients.
Purpose of the Study:
- To characterize recombinant fimbrial protein (rFimA) from the type IV fimA genotype.
- To compare the antigenicity of type IV fimbriae with type I fimbriae.
Main Methods:
- Production of recombinant type IV-fimA protein in Escherichia coli.
- SDS-PAGE and immunoblot analysis to assess protein structure and antigenicity.
- Antibody recognition of conformational and linear epitopes.
Main Results:
- Type IV-rFimA exhibited oligomeric/polymeric forms similar to native fimbriae.
- Antibodies against type IV fimbriae recognized both conformational and linear epitopes.
- Type IV-rFimA retained native fimbrial antigenicity.
- Antigenicity of type IV fimbriae differed significantly from type I fimbriae.
Conclusions:
- Recombinant type IV-fimbriae proteins accurately represent native fimbrial structure and antigenicity.
- Distinct antigenic properties of type IV fimbriae compared to type I may influence immune responses in periodontitis.
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