scholarly journals The effects of a triclosan/copolymer dentifrice on oral bacteria including those producing hydrogen sulfide

BDJ ◽  
2003 ◽  
Vol 195 (3) ◽  
pp. 143-143
Keyword(s):  
Hydrogen Sulfide ◽  
Oral Bacteria

scholarly journals Effects of pH and Lactate on Hydrogen Sulfide Production by Oral Veillonella spp.

2014 ◽  
Vol 80 (14) ◽  
pp. 4184-4188 ◽  
Author(s):  
Jumpei Washio ◽  
Yuko Shimada ◽  
Masakazu Yamada ◽  
Ryouichi Sakamaki ◽  
Nobuhiro Takahashi
Keyword(s):  
Hydrogen Sulfide ◽  
Environmental Factors ◽  
Enzymatic Activity ◽  
Oral Bacteria ◽  
Resting Cells ◽  
Content Type ◽  
Cell Extracts ◽  
Physiological Properties ◽  
Effects Of Ph ◽  
Type Strains

ABSTRACTIndigenous oral bacteria in the tongue coating such asVeillonellahave been identified as the main producers of hydrogen sulfide (H2S), one of the major components of oral malodor. However, there is little information on the physiological properties of H2S production by oralVeillonellasuch as metabolic activity and oral environmental factors which may affect H2S production. Thus, in the present study, the H2S-producing activity of growing cells, resting cells, and cell extracts of oralVeillonellaspecies and the effects of oral environmental factors, including pH and lactate, were investigated. Type strains ofVeillonella atypica,Veillonella dispar, andVeillonella parvulawere used. TheseVeillonellaspecies produced H2S during growth in the presence ofl-cysteine. Resting cells of these bacteria produced H2S froml-cysteine, and the cell extracts showed enzymatic activity to convertl-cysteine to H2S. H2S production by resting cells was higher at pH 6 to 7 and lower at pH 5. The presence of lactate markedly increased H2S production by resting cells (4.5- to 23.7-fold), while lactate had no effect on enzymatic activity in cell extracts. In addition to H2S, ammonia was produced in cell extracts of all the strains, indicating that H2S was produced by the catalysis of cystathionine γ-lyase (EC 4.4.1.1). Serine was also produced in cell extracts ofV. atypicaandV. parvula, suggesting the involvement of cystathionine β-synthase lyase (EC 4.2.1.22) in these strains. This study indicates thatVeillonellaproduce H2S froml-cysteine and that their H2S production can be regulated by oral environmental factors, namely, pH and lactate.

scholarly journals Structure of hydrogen sulfide-producing enzyme from a periodontal pathogen

2014 ◽  
Vol 70 (a1) ◽  
pp. C454-C454
Author(s):  
Yuichiro Kezuka ◽  
Yasuo Yoshida ◽  
Takamasa Nonaka
Keyword(s):  
Hydrogen Sulfide ◽  
Active Site ◽  
Catalytic Mechanism ◽  
Intermediate Formation ◽  
Fusobacterium Nucleatum ◽  
Oral Bacteria ◽  
Periodontal Pathogen ◽  
Fold Axis ◽  
Key Species ◽  
Active Site Cleft

Hydrogen sulfide (H2S) is one of the predominant volatile sulfur compounds that are primarily responsible for oral malodor and contribute to the progress of periodontal disease. H2S in the human oral cavity is generally produced by enzymatic actions of oral bacteria.Fusobacterium nucleatum, a Gram negative periodontal pathogen, is known to be one of the heaviest H2S producers [1]. For now, four genes (fn0625,fn1055,fn1220, andfn1419) encoding pyridoxal-5′-phosphate (PLP)-dependent H2S-producing enzymes have been identified and characterized inF. nucleatumATCC 25586. Of the four enzymes, Fn1055 protein is a unique H2S-producing enzyme, which produces H2S and L-serine from L-cysteine [2]. Therefore, Fn1055 might play important roles in L-serine biosynthesis in addition to H2S production in this periodontal pathogen. Crystal structures of recombinant Fn1055 and its site-directed mutant complex with L-cysteine (a substrate) were determined at 2.1 Å resolution. The enzyme forms a homodimer whose subunits are related by a two-fold axis. The subunit is composed of two domains with α/β structure. The PLP cofactor forms a covalent internal aldimine linkage with the ε-amino group of Lys46 at the bottom of active site cleft between the domains, in the absence of substrate. On the other hand, in the cocrystal of mutant with L-cysteine, the introduced L-cysteine was found to be covalently bound to PLP, instead of Lys46. This covalent intermediate was identified as an α-aminoacrylate, which is the key species of PLP-dependent-enzyme catalysis, by spectrophotometric measurement. Along with the intermediate formation, closure of active site cleft was also observed. Furthermore, we found an amino acid residue acting as a base and confirmed its indispensability for catalysis by enzymatic analyses. These results support that H2S production by Fn1055 proceeds through the β-elimination of L-cysteine, and enable us to propose a detailed catalytic mechanism of Fn1055.

scholarly journals The Role of Oral Microbiota in Intra-Oral Halitosis

2020 ◽  
Vol 9 (8) ◽  
pp. 2484 ◽  
Author(s):  
Katarzyna Hampelska ◽  
Marcelina Maria Jaworska ◽  
Zuzanna Łucja Babalska ◽  
Tomasz M. Karpiński
Keyword(s):  
Hydrogen Sulfide ◽  
Dimethyl Sulfide ◽  
Anaerobic Bacteria ◽  
Dimethyl Disulfide ◽  
Oral Bacteria ◽  
Oral Microbiota ◽  
Low Concentrations ◽  
Aldehydes And Ketones ◽  
Common Ailment

Halitosis is a common ailment concerning 15% to 60% of the human population. Halitosis can be divided into extra-oral halitosis (EOH) and intra-oral halitosis (IOH). The IOH is formed by volatile compounds, which are produced mainly by anaerobic bacteria. To these odorous substances belong volatile sulfur compounds (VSCs), aromatic compounds, amines, short-chain fatty or organic acids, alcohols, aliphatic compounds, aldehydes, and ketones. The most important VSCs are hydrogen sulfide, dimethyl sulfide, dimethyl disulfide, and methyl mercaptan. VSCs can be toxic for human cells even at low concentrations. The oral bacteria most related to halitosis are Actinomyces spp., Bacteroides spp., Dialister spp., Eubacterium spp., Fusobacterium spp., Leptotrichia spp., Peptostreptococcus spp., Porphyromonas spp., Prevotella spp., Selenomonas spp., Solobacterium spp., Tannerella forsythia, and Veillonella spp. Most bacteria that cause halitosis are responsible for periodontitis, but they can also affect the development of oral and digestive tract cancers. Malodorous agents responsible for carcinogenesis are hydrogen sulfide and acetaldehyde.

Hydrogen Sulfide Production From Cysteine and Homocysteine by Periodontal and Oral Bacteria

2009 ◽  
Vol 80 (11) ◽  
pp. 1845-1851 ◽  
Author(s):  
Akihiro Yoshida ◽  
Mamiko Yoshimura ◽  
Naoya Ohara ◽  
Shigeru Yoshimura ◽  
Shiori Nagashima ◽  
...  
Keyword(s):  
Hydrogen Sulfide ◽  
Oral Bacteria ◽  
Sulfide Production ◽  
Hydrogen Sulfide Production

The formation of hydrogen sulfide and methyl mercaptan by oral bacteria

1990 ◽  
Vol 5 (4) ◽  
pp. 195-201 ◽  
Author(s):  
Sten Persson ◽  
Maj-Britt Edlund ◽  
Rolf Claesson ◽  
Jan Carlsson
Keyword(s):  
Hydrogen Sulfide ◽  
Oral Bacteria ◽  
Methyl Mercaptan

Attachment of oral bacteria to titanium surfaces: An SEM study

1994 ◽  
Vol 52 ◽  
pp. 468-469
Author(s):  
J. E. Laffoon ◽  
R. L. Anderson ◽  
J. C. Keller ◽  
C. D. Wu-Yuan
Keyword(s):  
Technical Problem ◽  
Titanium Implant ◽  
Oral Bacteria ◽  
Bacterial Cells ◽  
Thin Sections ◽  
Surface Ultrastructure ◽  
Sem Study ◽  
Key Factor ◽  
Titanium Surfaces

Titanium (Ti) dental implants have been used widely for many years. Long term implant failures are related, in part, to the development of peri-implantitis frequently associated with bacteria. Bacterial adherence and colonization have been considered a key factor in the pathogenesis of many biomaterial based infections. Without the initial attachment of oral bacteria to Ti-implant surfaces, subsequent polymicrobial accumulation and colonization leading to peri-implant disease cannot occur. The overall goal of this study is to examine the implant-oral bacterial interfaces and gain a greater understanding of their attachment characteristics and mechanisms. Since the detailed cell surface ultrastructure involved in attachment is only discernible at the electron microscopy level, the study is complicated by the technical problem of obtaining titanium implant and attached bacterial cells in the same ultra-thin sections. In this study, a technique was developed to facilitate the study of Ti implant-bacteria interface.Discs of polymerized Spurr’s resin (12 mm x 5 mm) were formed to a thickness of approximately 3 mm using an EM block holder (Fig. 1). Titanium was then deposited by vacuum deposition to a film thickness of 300Å (Fig. 2).

Endogenous hydrogen sulfide sulfhydrates IKKβ at cysteine 179 to control pulmonary artery endothelial cell inflammation

2019 ◽  
Vol 133 (20) ◽  
pp. 2045-2059 ◽  
Author(s):  
Da Zhang ◽  
Xiuli Wang ◽  
Siyao Chen ◽  
Selena Chen ◽  
Wen Yu ◽  
...  
Keyword(s):  
Hydrogen Sulfide ◽  
Endothelial Cell ◽  
Pulmonary Artery ◽  
Cell Model ◽  
Site Directed Mutagenesis ◽  
Critical Event ◽  
Hypertensive Rats ◽  
Pulmonary Artery Endothelial Cell

Abstract Background: Pulmonary artery endothelial cell (PAEC) inflammation is a critical event in the development of pulmonary arterial hypertension (PAH). However, the pathogenesis of PAEC inflammation remains unclear. Methods: Purified recombinant human inhibitor of κB kinase subunit β (IKKβ) protein, human PAECs and monocrotaline-induced pulmonary hypertensive rats were employed in the study. Site-directed mutagenesis, gene knockdown or overexpression were conducted to manipulate the expression or activity of a target protein. Results: We showed that hydrogen sulfide (H2S) inhibited IKKβ activation in the cell model of human PAEC inflammation induced by monocrotaline pyrrole-stimulation or knockdown of cystathionine γ-lyase (CSE), an H2S generating enzyme. Mechanistically, H2S was proved to inhibit IKKβ activity directly via sulfhydrating IKKβ at cysteinyl residue 179 (C179) in purified recombinant IKKβ protein in vitro, whereas thiol reductant dithiothreitol (DTT) reversed H2S-induced IKKβ inactivation. Furthermore, to demonstrate the significance of IKKβ sulfhydration by H2S in the development of PAEC inflammation, we mutated C179 to serine (C179S) in IKKβ. In purified IKKβ protein, C179S mutation of IKKβ abolished H2S-induced IKKβ sulfhydration and the subsequent IKKβ inactivation. In human PAECs, C179S mutation of IKKβ blocked H2S-inhibited IKKβ activation and PAEC inflammatory response. In pulmonary hypertensive rats, C179S mutation of IKKβ abolished the inhibitory effect of H2S on IKKβ activation and pulmonary vascular inflammation and remodeling. Conclusion: Collectively, our in vivo and in vitro findings demonstrated, for the first time, that endogenous H2S directly inactivated IKKβ via sulfhydrating IKKβ at Cys179 to inhibit nuclear factor-κB (NF-κB) pathway activation and thereby control PAEC inflammation in PAH.

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