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

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.

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Identification and Characterization of a Halotolerant, Cold-Active Marine Endo-β-1,4-Glucanase by Using Functional Metagenomics of Seaweed-Associated Microbiota

Applied and Environmental Microbiology ◽

10.1128/aem.01194-14 ◽

2014 ◽

Vol 80 (16) ◽

pp. 4958-4967 ◽

Cited By ~ 35

Author(s):

Marjolaine Martin ◽

Sophie Biver ◽

Sébastien Steels ◽

Tristan Barbeyron ◽

Murielle Jam ◽

...

Keyword(s):

Metagenomic Library ◽

Functional Screening ◽

Sample Collection ◽

Prolonged Incubation ◽

Content Type ◽

Cold Active ◽

Esterase Loci ◽

Collection Period ◽

Identification And Characterization

ABSTRACTA metagenomic library was constructed from microorganisms associated with the brown algaAscophyllum nodosum. Functional screening of this library revealed 13 novel putative esterase loci and two glycoside hydrolase loci. Sequence and gene cluster analysis showed the wide diversity of the identified enzymes and gave an idea of the microbial populations present during the sample collection period. Lastly, an endo-β-1,4-glucanase having less than 50% identity to sequences of known cellulases was purified and partially characterized, showing activity at low temperature and after prolonged incubation in concentrated salt solutions.

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Characterization of Two Virulent Phages of Lactobacillus plantarum

Applied and Environmental Microbiology ◽

10.1128/aem.02565-12 ◽

2012 ◽

Vol 78 (24) ◽

pp. 8719-8734 ◽

Cited By ~ 27

Author(s):

Mariángeles Briggiler Marcó ◽

Josiane E. Garneau ◽

Denise Tremblay ◽

Andrea Quiberoni ◽

Sylvain Moineau

Keyword(s):

Lactobacillus Plantarum ◽

Corn Silage ◽

Open Reading Frames ◽

High Identity ◽

Content Type ◽

Defense Systems ◽

Double Stranded Dna ◽

Type Phage ◽

Reading Frames

ABSTRACTWe characterized twoLactobacillus plantarumvirulent siphophages, ATCC 8014-B1 (B1) and ATCC 8014-B2 (B2), previously isolated from corn silage and anaerobic sewage sludge, respectively. Phage B2 infected two of the eightL. plantarumstrains tested, while phage B1 infected three. Phage adsorption was highly variable depending on the strain used. Phage defense systems were found in at least twoL. plantarumstrains, LMG9211 and WCSF1. The linear double-stranded DNA genome of thepac-type phage B1 had 38,002 bp, a G+C content of 47.6%, and 60 open reading frames (ORFs). Surprisingly, the phage B1 genome has 97% identity with that ofPediococcus damnosusphage clP1 and 77% identity with that ofL. plantarumphage JL-1; these phages were isolated from sewage and cucumber fermentation, respectively. The double-stranded DNA (dsDNA) genome of thecos-type phage B2 had 80,618 bp, a G+C content of 36.9%, and 127 ORFs with similarities to those ofBacillusandLactobacillusstrains as well as phages. Some phage B2 genes were similar to ORFs fromL. plantarumphage LP65 of theMyoviridaefamily. Additionally, 6 tRNAs were found in the phage B2 genome. Protein analysis revealed 13 (phage B1) and 9 (phage B2) structural proteins. To our knowledge, this is the first report describing such high identity between phage genomes infecting different genera of lactic acid bacteria.

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Identification and Characterization of Mycobacterium tuberculosis Beijing Genotype Strain SBH163, Isolated in Sabah, Malaysia

Microbiology Resource Announcements ◽

10.1128/mra.01322-19 ◽

2020 ◽

Vol 9 (2) ◽

Author(s):

Jaeyres Jani ◽

Siti Fatimah Abu Bakar ◽

Zainal Arifin Mustapha ◽

Chin Kai Ling ◽

Roddy Teo ◽

...

Keyword(s):

Mycobacterium Tuberculosis ◽

Whole Genome Sequence ◽

Beijing Genotype ◽

Molecular Characteristics ◽

Whole Genome ◽

Content Type ◽

Identification And Characterization ◽

Insight Into ◽

Malaysian Borneo

This is a report on the whole-genome sequence of Mycobacterium tuberculosis strain SBH163, which was isolated from a patient in the Malaysian Borneo state of Sabah. This report provides insight into the molecular characteristics of an M. tuberculosis Beijing genotype strain related to strains from Russia and South Africa.

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Identification and Characterization of a Porcine Torovirus

Journal of Virology ◽

10.1128/jvi.72.5.3507-3511.1998 ◽

1998 ◽

Vol 72 (5) ◽

pp. 3507-3511 ◽

Cited By ~ 59

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.

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Characterization of a Feruloyl Esterase from Lactobacillus plantarum

Applied and Environmental Microbiology ◽

10.1128/aem.01523-13 ◽

2013 ◽

Vol 79 (17) ◽

pp. 5130-5136 ◽

Cited By ~ 62

Author(s):

María Esteban-Torres ◽

Inés Reverón ◽

José Miguel Mancheño ◽

Blanca de las Rivas ◽

Rosario Muñoz

Keyword(s):

Lactobacillus Plantarum ◽

Bacterial Species ◽

Hydrolytic Activity ◽

Feruloyl Esterase ◽

Gene Encoding ◽

Content Type ◽

Cell Extracts ◽

Methyl Ferulate ◽

Methyl Caffeate

ABSTRACTLactobacillus plantarumis frequently found in the fermentation of plant-derived food products, where hydroxycinnamoyl esters are abundant.L. plantarumWCFS1 cultures were unable to hydrolyze hydroxycinnamoyl esters; however, cell extracts from the strain partially hydrolyze methyl ferulate and methylp-coumarate. In order to discover whether the protein Lp_0796 is the enzyme responsible for this hydrolytic activity, it was recombinantly overproduced and enzymatically characterized. Lp_0796 is an esterase that, among other substrates, is able to efficiently hydrolyze the four model substrates for feruloyl esterases (methyl ferulate, methyl caffeate, methylp-coumarate, and methyl sinapinate). A screening test for the detection of the gene encoding feruloyl esterase Lp_0796 revealed that it is generally present amongL. plantarumstrains. The present study constitutes the description of feruloyl esterase activity inL. plantarumand provides new insights into the metabolism of hydroxycinnamic compounds in this bacterial species.

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

Applied and Environmental Microbiology ◽

10.1128/aem.03390-14 ◽

2014 ◽

Vol 81 (5) ◽

pp. 1700-1707 ◽

Cited By ~ 16

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.

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Two Zinc Uptake Systems Contribute to the Full Virulence of Listeria monocytogenes during GrowthIn VitroandIn Vivo

Infection and Immunity ◽

10.1128/iai.05904-11 ◽

2011 ◽

Vol 80 (1) ◽

pp. 14-21 ◽

Cited By ~ 39

Author(s):

David Corbett ◽

Jiahui Wang ◽

Stephanie Schuler ◽

Gloria Lopez-Castejon ◽

Sarah Glenn ◽

...

Keyword(s):

Listeria Monocytogenes ◽

Zinc Uptake ◽

Detectable Effect ◽

Intracellular Growth ◽

Content Type ◽

Zinc Sensing ◽

Identification And Characterization ◽

Cell Deletion

ABSTRACTWe report here the identification and characterization of two zinc uptake systems, ZurAM and ZinABC, in the intracellular pathogenListeria monocytogenes. Transcription of both operons was zinc responsive and regulated by the zinc-sensing repressor Zur. Deletion of eitherzurAMorzinAhad no detectable effect on growth in defined media, but a doublezurAM zinAmutant was unable to grow in the absence of zinc supplementation. Deletion ofzinAhad no detectable effect on intracellular growth in HeLa epithelial cells. In contrast, growth of thezurAMmutant was significantly impaired in these cells, indicating the importance of the ZurAM system during intracellular growth. Notably, the deletion of bothzinAandzurAMseverely attenuated intracellular growth, with the double mutant being defective in actin-based motility and unable to spread from cell to cell. Deletion of eitherzurAMorzinAhad a significant effect on virulence in an oral mouse model, indicating that both zinc uptake systems are importantin vivoand establishing the importance of zinc acquisition during infection byL. monocytogenes. The presence of two zinc uptake systems may offer a mechanism by whichL. monocytogenescan respond to zinc deficiency within a variety of environments and during different stages of infection, with each system making distinct contributions under different stress conditions.

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Genetic and Biochemical Characterization of OXA-535, a Distantly Related OXA-48-Like β-Lactamase

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.01198-18 ◽

2018 ◽

Vol 62 (10) ◽

Cited By ~ 2

Author(s):

L. Dabos ◽

A. B. Jousset ◽

R. A. Bonnin ◽

N. Fortineau ◽

A. Zavala ◽

...

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Sequence ◽

Amino Acid Sequence Identity ◽

Biochemical Characterization ◽

Content Type ◽

Sequence Identity

ABSTRACT OXA-535 is a chromosome-encoded carbapenemase of Shewanella bicestrii JAB-1 that shares only 91.3% amino acid sequence identity with OXA-48. Catalytic efficiencies are similar to those of OXA-48 for most β-lactams, except for ertapenem, where a 2,000-fold-higher efficiency was observed with OXA-535. OXA-535 and OXA-436, a plasmid-encoded variant of OXA-535 differing by three amino acids, form a novel cluster of distantly related OXA-48-like carbapenemases. Comparison of blaOXA-535 and blaOXA-436 genetic environments suggests that an ISCR1 may be responsible for blaOXA-436 gene mobilization from the chromosome of Shewanella spp. to plasmids.

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

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.01607-08 ◽

2009 ◽

Vol 53 (10) ◽

pp. 4320-4326 ◽

Cited By ~ 14

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.

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

Journal of Biological Chemistry ◽

10.1074/jbc.m005419200 ◽

2000 ◽

Vol 276 (15) ◽

pp. 11559-11566 ◽

Cited By ~ 28

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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