PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 11376092

Bacteremia by Dermabacter hominis, a rare pathogen.

J L Gómez-Garcés·J Oteo·G García·B Aracil·J I Alós·G Funke
View original source ↗Export metadata ↓

Abstract

Dermabacter hominis is a gram-positive, catalase-positive, glucose-fermenting rod, which, as it grows forms small greyish-white colonies with a characteristic pungent odor. Previously known as coryneform Centers for Disease Control and Prevention groups 3 and 5, it was catalogued as D. hominis in 1994. Various strains isolated in blood cultures, abscesses, or wounds in the 1970s were retrospectively characterized in referral centers as D. hominis. In this report we describe two patients with severe underlying pathology who developed bacteremias by D. hominis within the context of their clinical pictures.

Explore related subjects

ActinomycetalesActinomycetales InfectionsAdultAgedBacteremiaBloodCulture MediaFemaleHumansMaleCase ReportsJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J L Gómez-Garcés, J Oteo, G García, B Aracil, J I Alós, G Funke. 2001. Bacteremia by Dermabacter hominis, a rare pathogen.. https://doi.org/10.1128/jcm.39.6.2356-2357.2001

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Codon optimized Thermobifida fusca hydrolase secreted by Bacillus megaterium.

Production and secretion of a 28,172 Da hydrolase from Thermobifida fusca (TFH) in Bacillus megaterium MS941 and WH323 was investigated in shake flask and pH controlled bioreactors. Successful production of heterologous TFH was achieved by adapting the original tfh gene to the optimal codon usage of B. megaterium. A codon adaption index close to one was reached. The codon optimized tfh was cloned into an open reading frame with DNA sequence for the N-terminal signal peptide of B. megaterium lipase A and a C-terminal His(6)-tag, all under the control of a xylose inducible promoter. Successful TFH production and secretion were observed using batch reactor cultivations with complex medium. Expression of the tfh gene from the P(xylA) promoter and secretion of produced TFH were compared in detail to batch reactor cultivations with semi-defined growth medium. For the first time, significant TFH secretion was achieved using a semi-defined medium in glucose limited fed batch cultivations yielding 10-fold higher cell densities compared to LB medium cultivation. Comparable volumetric TFH activities were obtained for both cultivation strategies. Surprisingly, measured specific TFH activities exhibited drastic discrepancies between preparations from LB and semi-defined medium grown B. megaterium. TFH recovery by Ni-chelate affinity chromatography resulted in higher purification factors when LB medium was used. These results indicated that secreted TFH is favorably produced by batch cultures of B. megaterium WH323 in LB medium.

Actinomycetales↗
PubMed2007

Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX.

Thermobifida fusca is a moderately thermophilic soil bacterium that belongs to Actinobacteria. It is a major degrader of plant cell walls and has been used as a model organism for the study of secreted, thermostable cellulases. The complete genome sequence showed that T. fusca has a single circular chromosome of 3,642,249 bp predicted to encode 3,117 proteins and 65 RNA species with a coding density of 85%. Genome analysis revealed the existence of 29 putative glycoside hydrolases in addition to the previously identified cellulases and xylanases. The glycosyl hydrolases include enzymes predicted to exhibit mainly dextran/starch- and xylan-degrading functions. T. fusca possesses two protein secretion systems: the sec general secretion system and the twin-arginine translocation system. Several of the secreted cellulases have sequence signatures indicating their secretion may be mediated by the twin-arginine translocation system. T. fusca has extensive transport systems for import of carbohydrates coupled to transcriptional regulators controlling the expression of the transporters and glycosylhydrolases. In addition to providing an overview of the physiology of a soil actinomycete, this study presents insights on the transcriptional regulation and secretion of cellulases which may facilitate the industrial exploitation of these systems.

Actinomycetales↗