Defining the role of Hmu and Hus systems in Porphyromonas gingivalis heme and iron homeostasis and virulence.

Iron and heme are essential nutrients for all branches of life. Pathogenic members of the Bacteroidota phylum, including Porphyromonas gingivalis, do not synthesize heme and rely on host hemoproteins for heme as a source of iron and protoporphyrin IX. P.

Comparative analysis of A7436 and ATCC 33277 strains reveals differences in the expression of heme acquisition systems.

Unlabelled: strains exhibit different phenotypes , different virulence potential in animal models, and different associations with human diseases, with strains classified as virulent/more virulent (e.g., A7436 and W83) or as less virulent/avirulent (e.

Interplay between Porphyromonas gingivalis Hemophore-Like Protein HmuY and Kgp/RgpA Gingipains Plays a Superior Role in Heme Supply.

To acquire heme as a source of iron and protoporphyrin IX, Porphyromonas gingivalis uses gingipains, Hmu, and Hus systems. The aim of this study was to assess the correlation between the production and function of the most important virulence factors of P. gingivalis involved in heme supply, namely, hemophore-like proteins (HmuY and HusA) and gingipains.

Glycation of Host Proteins Increases Pathogenic Potential of .

The non-enzymatic addition of glucose (glycation) to circulatory and tissue proteins is a ubiquitous pathophysiological consequence of hyperglycemia in diabetes. Given the high incidence of periodontitis and diabetes and the emerging link between these conditions, it is of crucial importance to define the basic virulence mechanisms employed by periodontopathogens such as in mediating the disease process. The aim of this study was to determine whether glycated proteins are more easily utilized by to stimulate growth and promote the pathogenic potential of this bacterium.

HmuY and GAPDH-Novel Heme Acquisition Strategy in the Oral Microbiome.

The oral cavity of healthy individuals is inhabited by commensals, with species of being the most abundant and prevalent in sites not affected by periodontal diseases. The development of chronic periodontitis is linked with the environmental shift in the oral microbiome, leading to the domination of periodontopathogens. Structure-function studies showed that employs a "moonlighting" protein glyceraldehyde-3-phosphate dehydrogenase (SgGAPDH) to bind heme, thus forming a heme reservoir for exchange with other proteins.

Prevotella intermedia produces two proteins homologous to Porphyromonas gingivalis HmuY but with different heme coordination mode.

As part of the infective process, Porphyromonas gingivalis must acquire heme which is indispensable for life and enables the microorganism to survive and multiply at the infection site. This oral pathogenic bacterium uses a newly discovered novel hmu heme uptake system with a leading role played by the HmuY hemophore-like protein, responsible for acquiring heme and increasing virulence of this periodontopathogen. We demonstrated that Prevotella intermedia produces two HmuY homologs, termed PinO and PinA.