scholarly journals IND-6, a Highly Divergent IND-Type Metallo-β-Lactamase from Chryseobacterium indologenes Strain 597 Isolated in Burkina Faso

2009 ◽  
Vol 53 (10) ◽  
pp. 4320-4326 ◽  
Author(s):  
Boukaré Zeba ◽  
Filomena De Luca ◽  
Alain Dubus ◽  
Michael Delmarcelle ◽  
Jacques Simporé ◽  
...  
Keyword(s):  
Burkina Faso ◽  
Posttranslational Modification ◽  
Human Pathogens ◽  
Turnover Rates ◽  
Chryseobacterium Indologenes ◽  
Sequence Identity ◽  
New Variant ◽  
The Family ◽  
Identification And Characterization

ABSTRACT The genus Chryseobacterium and other genera belonging to the family Flavobacteriaceae include organisms that can behave as human pathogens and are known to cause different kinds of infections. Several species of Flavobacteriaceae, including Chryseobacterium indologenes, are naturally resistant to β-lactam antibiotics (including carbapenems), due to the production of a resident metallo-β-lactamase. Although C. indologenes presently constitutes a limited clinical threat, the incidence of infections caused by this organism is increasing in some settings, where isolates that exhibit multidrug resistance phenotypes (including resistance to aminoglycosides and quinolones) have been detected. Here, we report the identification and characterization of a new IND-type variant from a C. indologenes isolate from Burkina Faso that is resistant to β-lactams and aminoglycosides. The levels of sequence identity of the new variant to other IND-type metallo-β-lactamases range between 72 and 90% (for IND-4 and IND-5, respectively). The purified enzyme exhibited N-terminal heterogeneity and a posttranslational modification consisting of the presence of a pyroglutamate residue at the N terminus. IND-6 shows a broad substrate profile, with overall higher turnover rates than IND-5 and higher activities than IND-2 and IND-5 against ceftazidime and cefepime.

scholarly journals Isolation, identification and characterization of a novel elastase from Chryseobacterium indologenes

2018 ◽  
Vol 61 (3) ◽  
pp. 365-372 ◽  
Author(s):  
Yunlong Lei ◽  
Peipei Zhao ◽  
Chenglei Li ◽  
Haixia Zhao ◽  
Zhi Shan ◽  
...  
Keyword(s):  
Chryseobacterium Indologenes ◽  
Identification And Characterization

scholarly journals Tannin Degradation by a Novel Tannase Enzyme Present in Some Lactobacillus plantarum Strains

2014 ◽  
Vol 80 (10) ◽  
pp. 2991-2997 ◽  
Author(s):  
Natalia Jiménez ◽  
María Esteban-Torres ◽  
José Miguel Mancheño ◽  
Blanca de las Rivas ◽  
Rosario Muñoz
Keyword(s):  
Lactobacillus Plantarum ◽  
Tannic Acid ◽  
Plant Material ◽  
Aliphatic Alcohol ◽  
Methyl Gallate ◽  
Content Type ◽  
Sequence Identity ◽  
Tannin Degradation ◽  
Identification And Characterization

ABSTRACTLactobacillus plantarumis frequently isolated from the fermentation of plant material where tannins are abundant.L. plantarumstrains possess tannase activity to degrade plant tannins. AnL. plantarumtannase (TanBLp, formerly called TanLp1) was previously identified and biochemically characterized. In this study, we report the identification and characterization of a novel tannase (TanALp). While all 29L. plantarumstrains analyzed in the study possess thetanBLpgene, the genetanALpwas present in only four strains. Upon methyl gallate exposure, the expression oftanBLpwas induced, whereastanALpexpression was not affected. TanALpshowed only 27% sequence identity to TanBLp, but the residues involved in tannase activity are conserved. Optimum activity for TanALpwas observed at 30°C and pH 6 in the presence of Ca2+ions. TanALpwas able to hydrolyze gallate and protocatechuate esters with a short aliphatic alcohol substituent. Moreover, TanALpwas able to fully hydrolyze complex gallotannins, such as tannic acid. The presence of the extracellular TanALptannase in someL. plantarumstrains provides them an advantage for the initial degradation of complex tannins present in plant environments.

scholarly journals Identification and Characterization of a Porcine Torovirus

1998 ◽  
Vol 72 (5) ◽  
pp. 3507-3511 ◽  
Author(s):  
A. Kroneman ◽  
L. A. H. M. Cornelissen ◽  
M. C. Horzinek ◽  
R. J. de Groot ◽  
H. F. Egberink
Keyword(s):  
Longitudinal Study ◽  
Neutralizing Antibodies ◽  
Rt Pcr ◽  
Gene Encoding ◽  
Nucleocapsid Gene ◽  
Sequence Identity ◽  
Young Pigs ◽  
Porcine Torovirus ◽  
Identification And Characterization

ABSTRACT A porcine torovirus (PoTV) was identified and characterized; it is a novel member of the genus Torovirus (familyCoronaviridae, order Nidovirales), closely related to but clearly distinct from the already recognized equine torovirus (ETV) and bovine torovirus (BoTV) representatives. Immunoelectron microscopy of feces from piglets revealed elongated, 120- by 55-nm particles which were recognized by a torovirus-specific antiserum. Amplification by reverse transcriptase (RT) PCR with primers designed to detect conserved regions (on the basis of the genomes of BoTV strain Breda and ETV strain Berne) resulted in the identification of the 489-bp nucleocapsid gene, encoding a 18.7-kDa protein. The sequence identity in this region between PoTV and both ETV and BoTV was only about 68%, whereas the latter two show 81% identity. Neutralizing antibodies directed against ETV were found in sera of adult and young pigs. In all 10 herds sampled, seropositive animals were present, and 81% of randomly selected adult sows possessed antibodies. A longitudinal study with RT PCR showed that piglets shed virus in the feces for 1 or more days, starting 4 to 14 days after weaning.

scholarly journals Postgenomic Scan of Metallo-β-Lactamase Homologues in Rhizobacteria: Identification and Characterization of BJP-1, a Subclass B3 Ortholog from Bradyrhizobium japonicum

2006 ◽  
Vol 50 (6) ◽  
pp. 1973-1981 ◽  
Author(s):  
Magdalena Stoczko ◽  
Jean-Marie Frère ◽  
Gian Maria Rossolini ◽  
Jean-Denis Docquier
Keyword(s):  
Bradyrhizobium Japonicum ◽  
Catalytic Efficiency ◽  
Open Reading Frames ◽  
Human Pathogens ◽  
Microbial Genomes ◽  
E Coli ◽  
Genes Encoding ◽  
And Function ◽  
Identification And Characterization

ABSTRACT The diffusion of metallo-β-lactamases (MBLs) among clinically important human pathogens represents a therapeutic issue of increasing importance. However, the origin of these resistance determinants is largely unknown, although an important number of proteins belonging to the MBL superfamily have been identified in microbial genomes. In this work, we analyzed the distribution and function of genes encoding MBL-like proteins in the class Rhizobiales. Among 12 released complete genomes of members of the class Rhizobiales, a total of 57 open reading frames (ORFs) were found to have the MBL conserved motif and identity scores with MBLs ranging from 8 to 40%. On the basis of the best identity scores with known MBLs, four ORFs were cloned into Escherichia coli for heterologous expression. Among their products, one (blr6230) encoded by the Bradyrhizobium japonicum USDA110 genome, named BJP-1, hydrolyzed β-lactams when expressed in E. coli. BJP-1 enzyme is most closely related to the CAU-1 enzyme from Caulobacter vibrioides (40% amino acid sequence identity), a member of subclass B3 MBLs. A kinetic analysis revealed that BJP-1 efficiently hydrolyzed most β-lactam substrates, except aztreonam, ticarcillin, and temocillin, with the highest catalytic efficiency measured with meropenem. Compared to other MBLs, BJP-1 was less sensitive to inactivation by chelating agents.

scholarly journals Characterization of a new picornavirus isolated from the freshwater fish Lepomis macrochirus

2014 ◽  
Vol 95 (3) ◽  
pp. 601-613 ◽  
Author(s):  
Marisa Barbknecht ◽  
Sol Sepsenwol ◽  
Eric Leis ◽  
Maren Tuttle-Lau ◽  
Mark Gaikowski ◽  
...  
Keyword(s):  
Freshwater Fish ◽  
New Genus ◽  
Lepomis Macrochirus ◽  
Leader Peptide ◽  
Fish Kill ◽  
Sequence Identity ◽  
Phylogenetic Cluster ◽  
The Family ◽  
Sport Fish

The freshwater fish Lepomis macrochirus (bluegill) is common to North American waters, and important both ecologically and as a sport fish. In 2001 an unknown virus was isolated from bluegills following a bluegill fish kill. This virus was identified as a picornavirus [termed bluegill picornavirus (BGPV)] and a diagnostic reverse transcriptase PCR was developed. A survey of bluegills in Wisconsin waters showed the presence of BGPV in 5 of 17 waters sampled, suggesting the virus is widespread in bluegill populations. Experimental infections of bluegills confirmed that BGPV can cause morbidity and mortality in bluegills. Molecular characterization of BGPV revealed several distinct genome characteristics, the most unusual of which is the presence of a short poly(C) tract in the 3′ UTR. Additionally, the genome encodes a polyprotein lacking a leader peptide and a VP0 maturation cleavage site, and is predicted to encode two distinct 2A proteins. Sequence comparison showed that the virus is most closely related to a phylogenetic cluster of picornaviruses that includes the genera Aquamavirus, Avihepatovirus and Parechovirus. However, it is distinct enough, for example sharing only about 38 % sequence identity to the parechoviruses in the 3D region, that it may represent a new genus in the family Picornaviridae.

scholarly journals Identification and Characterization of a New Metallo-β-Lactamase, IND-5, from a Clinical Isolate of Chryseobacterium indologenes

2007 ◽  
Vol 51 (8) ◽  
pp. 2988-2990 ◽  
Author(s):  
Mariagrazia Perilli ◽  
Bibiana Caporale ◽  
Giuseppe Celenza ◽  
Cristina Pellegrini ◽  
Jean Denis Docquier ◽  
...  
Keyword(s):  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Homology ◽  
Chryseobacterium Indologenes ◽  
Identification And Characterization

ABSTRACT A new natural IND-type metallo-β-lactamase variant, IND-5, was identified in a clinical isolate of Chryseobacterium indologenes. IND-5 shared 92.8% and 92.4% amino acid homology with IND-1 and IND-3, respectively. Purified enzyme (pI = 8.8, M r = 25,000) was able to hydrolyze penicillins, some narrow- and expanded-spectrum cephalosporins, and carbapenems but not monobactams.

scholarly journals Malonic Semialdehyde Reductase from the Archaeon Nitrosopumilus maritimus Is Involved in the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle

2014 ◽  
Vol 81 (5) ◽  
pp. 1700-1707 ◽  
Author(s):  
Julia Otte ◽  
Achim Mall ◽  
Daniel M. Schubert ◽  
Martin Könneke ◽  
Ivan A. Berg
Keyword(s):  
Succinic Semialdehyde ◽  
Alcohol Dehydrogenases ◽  
Content Type ◽  
Metallosphaera Sedula ◽  
Ammonia Oxidizing Archaea ◽  
The Family ◽  
Terrestrial Environments ◽  
Identification And Characterization ◽  
Low Activity

ABSTRACTThe recently described ammonia-oxidizing archaea of the phylumThaumarchaeotaare highly abundant in marine, geothermal, and terrestrial environments. All characterized representatives of this phylum are aerobic chemolithoautotrophic ammonia oxidizers assimilating inorganic carbon via a recently described thaumarchaeal version of the 3-hydroxypropionate/4-hydroxybutyrate cycle. Although some genes coding for the enzymes of this cycle have been identified in the genomes ofThaumarchaeota, many other genes of the cycle are not homologous to the characterized enzymes from other species and can therefore not be identified bioinformatically. Here we report the identification and characterization of malonic semialdehyde reductase Nmar_1110 in the cultured marine thaumarchaeonNitrosopumilus maritimus. This enzyme, which catalyzes the reduction of malonic semialdehyde with NAD(P)H to 3-hydroxypropionate, belongs to the family of iron-containing alcohol dehydrogenases and is not homologous to malonic semialdehyde reductases fromChloroflexus aurantiacusandMetallosphaera sedula. It is highly specific to malonic semialdehyde (Km, 0.11 mM;Vmax, 86.9 μmol min−1mg−1of protein) and exhibits only low activity with succinic semialdehyde (Km, 4.26 mM;Vmax, 18.5 μmol min−1mg−1of protein). Homologues ofN. maritimusmalonic semialdehyde reductase can be found in the genomes of allThaumarchaeotasequenced so far and form a well-defined cluster in the phylogenetic tree of iron-containing alcohol dehydrogenases. We conclude that malonic semialdehyde reductase can be regarded as a characteristic enzyme for the thaumarchaeal version of the 3-hydroxypropionate/4-hydroxybutyrate cycle.

scholarly journals Identification and Characterization of a New Variant of Shiga Toxin 1 in Escherichia coli ONT:H19 of Bovine Origin

2003 ◽  
Vol 41 (5) ◽  
pp. 2106-2112 ◽  
Author(s):  
C. Burk ◽  
R. Dietrich ◽  
G. Acar ◽  
M. Moravek ◽  
M. Bulte ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Shiga Toxin ◽  
New Variant ◽  
Identification And Characterization

scholarly journals Introduction to cancer genetic susceptibility syndromes

Hematology ◽  
2016 ◽  
Vol 2016 (1) ◽  
pp. 293-301 ◽  
Author(s):  
Rose B. McGee ◽  
Kim E. Nichols
Keyword(s):  
Genetic Susceptibility ◽  
Germ Line ◽  
Cancer Susceptibility ◽  
Underlying Disease ◽  
Cancer Genetic ◽  
Genetic Syndrome ◽  
Hematopoietic Malignancies ◽  
The Family ◽  
Identification And Characterization

AbstractThe last 30 years have witnessed tremendous advances in our understanding of the cancer genetic susceptibility syndromes, including those that predispose to hematopoietic malignancies. The identification and characterization of families affected by these syndromes is enhancing our knowledge of the oncologic and nononcologic manifestations associated with predisposing germ line mutations and providing insights into the underlying disease mechanisms. Here, we provide an overview of the cancer genetic susceptibility syndromes, focusing on aspects relevant to the evaluation of patients with leukemia and lymphoma. Guidance is provided to facilitate recognition of these syndromes by hematologists/oncologists, including descriptions of the family history features, tumor genotype, and physical or developmental findings that should raise concern for an underlying cancer genetic syndrome. The clinical implications and management challenges associated with cancer susceptibility syndromes are also discussed.

scholarly journals Characterization of TbPDE2A, a Novel Cyclic Nucleotide-specific Phosphodiesterase from the Protozoan ParasiteTrypanosoma brucei

2000 ◽  
Vol 276 (15) ◽  
pp. 11559-11566 ◽  
Author(s):  
Roya Zoraghi ◽  
Stefan Kunz ◽  
Kewei Gong ◽  
Thomas Seebeck
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Trypanosoma Brucei ◽  
Dictyostelium Discoideum ◽  
Cyclic Nucleotide ◽  
Catalytic Domain ◽  
Sequence Identity ◽  
Essential Enzyme ◽  
Identification And Characterization

This study reports the identification and characterization of a cAMP-specific phosphodiesterase from the parasitic hemoflagellateTrypanosoma brucei. TbPDE2A is a class I phosphodiesterase. Its catalytic domain exhibits 30–40% sequence identity with those of all 11 mammalian phosphodiesterase (PDE) families, as well as withPDE2fromSaccharomyces cerevisiae,duncefromDrosophila melanogaster, andregAfromDictyostelium discoideum. The overall structure of TbPDE2A resembles that of human PDE11A in that its N-terminal region contains a single GAF domain. This domain is very similar to those of the mammalian PDE2, -5, -6, -10, and -11, where it constitutes a potential cGMP binding site. TbPDE2A can be expressed inS. cerevisiae, and it complements anS. cerevisiaePDE deletion strain. Recombinant TbPDE2A is specific for cAMP, with aKmof ∼2 μm. It is entirely resistant to the nonselective PDE inhibitor 3-isobutyl-1-methylxanthine, but it is sensitive to trequinsin, dipyridamole, sildenafil, and ethaverine with IC50values of 5.4, 5.9, 9.4, and 14.2 μm, respectively. All four compounds inhibit proliferation of bloodstream form trypanosomes in culture, indicating that TbPDE2A is an essential enzyme.

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