Analysis of gene expression in Porphyromonas gingivalis hmuS deletion mutant strain (RNA-seq analysis)
Porphyromonas gingivalis is considered a keystone pathogen responsible for dysbiosis in the oral microbiome, leading to the development of periodontal disease and contributing to various systemic comorbidities. Although P. gingivalis requires heme for growth and virulence, it is unable to synthesize heme de novo and therefore relies on host hemoproteins as its source. To acquire heme, the bacterium utilizes the Hmu system, which is composed of six proteins (HmuYRSTUV). HmuY functions as a hemophore-like protein that sequesters heme from host hemoproteins; HmuR serves as an outer membrane receptor responsible for heme uptake. The remaining four proteins (HmuS, HmuT, HmuU, and HmuV) are uncharacterized. HmuS has been proposed to act as a reverse ferrochelatase, due to its homology with CobN cobaltochelatases; therefore, it could catalyze the removal of iron from heme. The released iron could then be transported into the cytoplasm via the HmuTUV proteins. However, the specific role of HmuS in P. gingivalis has never been studied or confirmed. Therefore, this study aimed to investigate the effect of hmuS gene deletion on global gene expression in P. gingivalis, thereby assessing its role in iron acquisition and overall bacterial fitness.
Porphyromonas gingivalis is considered a keystone pathogen responsible for dysbiosis in the oral microbiome, leading to the development of periodontal disease and contributing to various systemic comorbidities. Although P. gingivalis requires heme for growth and virulence, it is unable to synthesize heme de novo and therefore relies on host hemoproteins as its source. To acquire heme, the bacterium utilizes the Hmu system, which is composed of six proteins (HmuYRSTUV). HmuY functions as a hemophore-like protein that sequesters heme from host hemoproteins; HmuR serves as an outer membrane receptor responsible for heme uptake. The remaining four proteins (HmuS, HmuT, HmuU, and HmuV) are uncharacterized. HmuS has been proposed to act as a reverse ferrochelatase, due to its homology with CobN cobaltochelatases; therefore, it could catalyze the removal of iron from heme. The released iron could then be transported into the cytoplasm via the HmuTUV proteins. However, the specific role of HmuS in P. gingivalis has never been studied or confirmed. Therefore, this study aimed to investigate the effect of hmuS gene deletion on global gene expression in P. gingivalis, thereby assessing its role in iron acquisition and overall bacterial fitness.
European Bioinformatics Institute