Genome Sequence and Analysis of the Oral Bacterium
            <i>Fusobacterium nucleatum</i>
            Strain ATCC 25586

Kapatral, Vinayak; Anderson, Iain; Ivanova, Natalia; Reznik, Gary; Los, Tamara; Lykidis, Athanasios; Bhattacharyya, Anamitra; Bartman, Allen E.; Gardner, Warren L.; Grechkin, Galina; Zhu, Lihua Julie; Vasieva, Olga; Chu, Lien; Kogan, Yakov; Chaga, Oleg Y.; Goltsman, Eugene; Bernal, Axel; Larsen, Niels; D’Souza, Mark; Walunas, Theresa L.; Pusch, Gordon D.; Haselkorn, Robert; Fonstein, Michael; Kyrpides, Nikos C.; Overbeek, Ross

doi:10.1128/jb.184.7.2005-2018.2002

Cited by 321 publications

(315 citation statements)

References 45 publications

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“…trophozoites cultivated in the presence of 20 M of TFMET were completely lysed within 72 h. The IC 50 of TFMET (for the growth inhibition) was determined to be 18 M, which is slightly higher than that of the most commonly used antiamebic drug metronidazole [1-(2-hydroxyethyl)-2-methyl-5-nitroimidazole], which showed an IC 50 of 7 M under the same conditions (Fig. 5A).…”

Section: Table I Products Of L-methionine Degradation By the Amebic Cmentioning

confidence: 90%

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Identification and Characterization of Two Isoenzymes of Methionine γ-Lyase from Entamoeba histolytica

Tokoro

Asai

Kobayashi

et al. 2003

Journal of Biological Chemistry

107

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To better understand the metabolism of sulfur-containing amino acids, which likely plays a key role in a variety of cell functions, in Entamoeba histolytica, we searched the genome data base for genes encoding putative orthologs of enzymes known to be involved in the metabolism. The search revealed that E. histolytica possesses only incomplete cysteine-methionine conversion pathways in both directions. Instead, this parasite possesses genes encoding two isoenzymes of methionine ␥-lyase (EC 4.4.1.11, EhMGL1/2), which has been implicated in the degradation of sulfur-containing amino acids. The two amebic MGL isoenzymes, showing 69% identity to each other, encode 389-and 392-amino acid polypeptides with predicted molecular masses of 42.3 and 42.7 kDa and pIs of 6.01 and 6.63, respectively. Amino acid comparison and phylogenetic analysis suggested that these amebic MGLs are likely to have been horizontally transferred from the Archaea, whereas an MGL from another anaerobic protist Trichomonas vaginalis has MGL isotypes that share a common ancestor with bacteria. Enzymological and immunoblot analyses of the partially purified native amebic MGL confirmed that both of the MGL isotypes are expressed in a comparable amount predominantly in the cytosol and form a homotetramer. Recombinant EhMGL1 and 2 proteins catalyzed degradation of L-methionine, DL-homocysteine, L-cysteine, and O-acetyl-L-serine to form ␣-keto acid, ammonia, and hydrogen sulfide or methanethiol, whereas activity toward cystathionine was negligible. These two isoenzymes showed notable differences in substrate specificity and pH optimum. In addition, we showed that EhMGL is an ideal target for the development of new chemotherapeutic agents against amebiasis by demonstrating an amebicidal effect of the methionine analog trifluoromethionine on trophozoites in culture (IC 50 18 M) and that this effect of trifluoromethionine was completely abolished by the addition of the MGL-specific inhibitor DL-propargylglycine.Entamoeba histolytica is a causative agent of amebiasis, which annually affects an estimated 48 million people and results in 70,000 deaths (1). The most common clinical presentation of amebiasis is amebic dysentery and colitis; extraintestinal abscesses, i.e. hepatic, pulmonary, and cerebral, however, are also common and often lethal. This microaerophilic anaerobe has been considered to be a unique eukaryotic organism because it apparently lacks organelles typical of eukaryotic organisms such as mitochondria, the rough endoplasmic reticulum, and the Golgi apparatus (2). However, a recent demonstration of genes encoding mitochondrial proteins, i.e. cpn60 and pyridine nucleotide transhydrogenase (3), together with electron micrographic demonstration of the rough endoplasmic reticulum and the Golgi apparatus (4), suggested the presence of a residual organelle of mitochondria (called crypton or mitosome) (5, 54) and also indicated that this group of parasitic protists possess a unique organelle organization. This parasite also reveals numerous unusual...

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Section: Table I Products Of L-methionine Degradation By the Amebic Cmentioning

confidence: 90%

“…ment of new chemotherapeutic agents against amebiasis by demonstrating an amebicidal effect of the methionine analog trifluoromethionine on trophozoites in culture (IC 50 18 M) and that this effect of trifluoromethionine was completely abolished by the addition of the MGL-specific inhibitor DL-propargylglycine.…”

mentioning

confidence: 99%

Identification and Characterization of Two Isoenzymes of Methionine γ-Lyase from Entamoeba histolytica

Tokoro

Asai

Kobayashi

et al. 2003

Journal of Biological Chemistry

107

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“…Following identification of the fadA gene, the genomic sequence of F. nucleatum ATCC 25586 became available (31). A BLAST search showed that the 2.4-kb fragment containing the fadA gene was highly conserved between F. nucleatum 12230 and ATCC 25586 (data not shown).…”

Section: Resultsmentioning

confidence: 99%

Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria

Han¹,

Ikegami²,

Rajanna³

et al. 2005

J Bacteriol

215

204

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Fusobacterium nucleatum is a gram-negative anaerobe that is prevalent in periodontal disease and infections of different parts of the body. The organism has remarkable adherence properties, binding to partners ranging from eukaryotic and prokaryotic cells to extracellular macromolecules. Understanding its adherence is important for understanding the pathogenesis of F. nucleatum. In this study, a novel adhesin, FadA (Fusobacterium adhesin A), was demonstrated to bind to the surface proteins of the oral mucosal KB cells. FadA is composed of 129 amino acid (aa) residues, including an 18-aa signal peptide, with calculated molecular masses of 13.6 kDa for the intact form and 12.6 kDa for the secreted form. It is highly conserved among F. nucleatum, Fusobacterium periodonticum, and Fusobacterium simiae, the three most closely related oral species, but is absent in the nonoral species, including Fusobacterium gonidiaformans, Fusobacterium mortiferum, Fusobacterium naviforme, Fusobacterium russii, and Fusobacterium ulcerans. In addition to FadA, F. nucleatum ATCC 25586 and ATCC 49256 also encode two paralogues, FN1529 and FNV2159, each sharing 31% identity with FadA. A double-crossover fadA deletion mutant, F. nucleatum 12230-US1, was constructed by utilizing a novel sonoporation procedure. The mutant had a slightly slower growth rate, yet its binding to KB and Chinese hamster ovarian cells was reduced by 70 to 80% compared to that of the wild type, indicating that FadA plays an important role in fusobacterial colonization in the host. Furthermore, due to its uniqueness to oral Fusobacterium species, fadA may be used as a marker to detect orally related fusobacteria. F. nucleatum isolated from other parts of the body may originate from the oral cavity.

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“…ARD or CRD regions with >90 % nucleotide identity were assigned the same type designation. Seven different ARD types and eight different CRD types are present among the 64 hsdS genes ( Kapatral et al, 2002). RloA and RloB are also similar to the AbiLi and AbiLii proteins of Lactococcus lactis biovar diacetylactis plasmid pND861 (Deng et al, 1999), respectively.…”

Section: Hsd Coding Repeatsmentioning

confidence: 99%

Diversity within the Campylobacter jejuni type I restriction–modification loci

et al. 2005

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The type I restriction–modification (hsd) systems of 73 Campylobacter jejuni strains were characterized according to their DNA and amino acid sequences, and/or gene organization. A number of new genes were identified which are not present in the sequenced strain NCTC 11168. The closely related organism Helicobacter pylori has three type I systems; however, no evidence was found that C. jejuni strains contain multiple type I systems, although hsd loci are present in at least two different chromosomal locations. Also, unlike H. pylori, intervening ORFs are present, in some strains, between hsdR and hsdS and between hsdS and hsdM. No definitive function can be ascribed to these ORFs, designated here as rloA–H (R-linked ORF) and mloA–B (M-linked ORF). Based on parsimony analysis of amino acid sequences to assess character relatedness, the C. jejuni type I R–M systems are assigned to one of three families: ‘IAB’, ‘IC’ or ‘IF’. This study confirms that HsdM proteins within a family are highly conserved but share little homology with HsdM proteins from other families. The ‘IC’ hsd loci are >99 % identical at the nucleotide level, as are the ‘IF’ hsd loci. Additionally, whereas the nucleotide sequences of the ‘IAB’ hsdR and hsdM genes show a high degree of similarity, the nucleotide sequences of the ‘IAB’ hsdS and rlo genes vary considerably. This diversity suggests that recombination between ‘IAB’ hsd loci would lead not only to new hsdS alleles but also to the exchange of rlo genes; five C. jejuni hsd loci are presumably the result of such recombination. The importance of these findings with regard to the evolution of C. jejuni type I R–M systems is discussed.

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Genome Sequence and Analysis of the Oral Bacterium Fusobacterium nucleatum Strain ATCC 25586

Cited by 321 publications

References 45 publications

Identification and Characterization of Two Isoenzymes of Methionine γ-Lyase from Entamoeba histolytica

Identification and Characterization of Two Isoenzymes of Methionine γ-Lyase from Entamoeba histolytica

Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria

Diversity within the Campylobacter jejuni type I restriction–modification loci

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