Publications by authors named "Sergio Guerrero"

Article Synopsis
  • - The study aimed to assess the bacterial diversity and potential health risks in stray dogs with tick infestations in northern Mexico by analyzing their blood samples for harmful bacteria.
  • - Researchers collected blood from 12 dogs, extracted DNA, and used next-generation sequencing to identify 620 bacterial species, including 64 with possible pathogenic or zoonotic risks.
  • - Findings highlight the significance of stray dogs as potential carriers of tick-borne and other zoonotic diseases, emphasizing the importance of advanced molecular techniques for understanding these risks.
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Background: Entamoeba histolytica, an intestinal parasitic protozoan that usually lives and multiplies within the human gut, is the causative agent of amoebiasis. To date, de novo glutathione biosynthesis and its associated enzymes have not been identified in the parasite. Cysteine has been proposed to be the main intracellular thiol.

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Trypanosoma cruzi is the causal agent of Chagas Disease and is a unicellular parasite that infects a wide variety of mammalian hosts. The parasite exhibits auxotrophy by L-Met; consequently, it must be acquired from the extracellular environment of the host, either mammalian or invertebrate. Methionine (Met) oxidation produces a racemic mixture (R and S forms) of methionine sulfoxide (MetSO).

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The phosphorolysis of cello-oligosaccharides is a critical process played in the rumen by to degrade cellulose. Cellodextrins, made up of a few glucosyl units, have gained lots of interest by their potential applications. Here, we characterized a cellobiose phosphorylase (CBP) and a cellodextrin phosphorylase (CDP) from 8.

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Visceral leishmaniasis is a zoonotic infectious disease with a severe impact on humans and animals. Infection is transmitted by phlebotomine sand flies. The dogs are main reservoir for human infection.

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Endo-β-1,3-glucanases from several organisms have attracted much attention in recent years because of their capability for in vitro degrading β-1,3-glucan as a critical step for both biofuels production and short-chain oligosaccharides synthesis. In this study, we biochemically characterized a putative endo-β-1,3-glucanase (EgrGH64) belonging to the family GH64 from the single-cell protist Euglena gracilis. The gene coding for the enzyme was heterologously expressed in a prokaryotic expression system supplemented with 3% (v/v) ethanol to optimize the recombinant protein right folding.

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Euglenoids (Euglenida) are unicellular flagellates possessing exceptionally wide geographical and ecological distribution. Euglenoids combine a biotechnological potential with a unique position in the eukaryotic tree of life. In large part these microbes owe this success to diverse genetics including secondary endosymbiosis and likely additional sources of genes.

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Thiol redox proteins and low molecular mass thiols have essential functions in maintaining cellular redox balance in almost all living organisms. In the pathogenic bacterium Leptospira interrogans, several redox components have been described, namely, typical 2-Cys peroxiredoxin, a functional thioredoxin system, glutathione synthesis pathway, and methionine sulfoxide reductases. However, until now, information about proteins linked to GSH metabolism has not been reported in this pathogen.

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Euglena gracilis is a eukaryotic single-celled and photosynthetic organism grouped under the kingdom Protista. This phytoflagellate can accumulate the carbon photoassimilate as a linear β-1,3-glucan chain called paramylon. This storage polysaccharide can undergo degradation to provide glucose units to obtain ATP and reducing power both in aerobic and anaerobic growth conditions.

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Chagas Disease, African sleeping sickness, and leishmaniasis are neglected diseases caused by pathogenic trypanosomatid parasites, which have a considerable impact on morbidity and mortality in poor countries. The available drugs used as treatment have high toxicity, limited access, and can cause parasite drug resistance. Long-term treatments, added to their high toxicity, result in patients that give up therapy.

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Background: Methionine (Met) oxidation leads to a racemic mixture of R and S forms of methionine sulfoxide (MetSO). Methionine sulfoxide reductases (Msr) are enzymes that can reduce specifically each isomer of MetSO, both free and protein-bound. The Met oxidation could change the structure and function of many proteins, not only of those redox-related but also of others involved in different metabolic pathways.

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We analyzed the structure to function relationships in Ruminococcus albus 8 xylanase 10A (RalXyn10A) finding that the N-terminus 34-amino acids sequence (N34) in the protein is particularly functional. We performed the recombinant wild type enzyme's characterization and that of the truncated mutant lacking the N34 extreme (RalΔN34Xyn10A). The truncated enzyme exhibited about half of the activity and reduced affinity for binding to insoluble saccharides.

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Structures are reported for two matched sets of substituted 4-styrylquinolines which were prepared by the formation of the heterocyclic ring in cyclocondensation reactions between 1-(2-aminophenyl)-3-arylprop-2-en-1-ones with 1,3-dicarbonyl compounds. (E)-3-Acetyl-4-[2-(4-methoxyphenyl)ethenyl]-2-methylquinoline, CHNO, (I), (E)-3-acetyl-4-[2-(4-bromophenyl)ethenyl]-2-methylquinoline, CHBrNO, (II), and (E)-3-acetyl-2-methyl-4-{2-[4-(trifluoromethyl)phenyl]ethenyl}quinoline, CHFNO, (III), are isomorphous and in each structure the molecules are linked by a single C-H..

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Canine visceral leishmaniasis (CVL) is the major source of human visceral leishmaniasis. To control the spread of this disease, early and accurate detection of infected dogs is critical but challenging. The serological diagnosis of CVL remains problematic because there are no reliable commercially available tests.

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Background: Methionine is an amino acid susceptible to be oxidized to give a racemic mixture of R and S forms of methionine sulfoxide (MetSO). This posttranslational modification has been reported to occur in vivo under either normal or stress conditions. The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductases (MSRs), thiol-dependent enzymes present in almost all organisms.

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Background: Glutathione (GSH) plays a role as a main antioxidant metabolite in all eukaryotes and many prokaryotes. Most of the organisms synthesize GSH by a pathway involving two enzymatic reactions, each one consuming one molecule of ATP. In a first step mediated by glutamate-cysteine ligase (GCL), the carboxylate of l-glutamic acid reacts with l-cysteine to form the dipeptide γ-glutamylcysteine (γ-GC).

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A concise, efficient and versatile route from simple starting materials to tricyclic tetrahydro-1-benzazepines carrying [a]-fused heterocyclic units is reported. Thus, the easily accessible methyl 2-[(2-allyl-4-chlorophenyl)amino]acetate, (I), was converted, via (2RS,4SR)-7-chloro-2,3,4,5-tetrahydro-1,4-epoxy-1-benzo[b]azepine-2-carboxylate, (II), to the key intermediate methyl (2RS,4SR)-7-chloro-4-hydroxy-2,3,4,5-tetrahydro-1H-benzo[b]azepine-2-carboxylate, (III). Chloroacetylation of (III) provided the two regioisomers methyl (2RS,4SR)-7-chloro-1-(2-chloroacetyl)-4-hydroxy-2,3,4,5-tetrahydro-1H-benzo[b]azepine-2-carboxylate, (IVa), and methyl (2RS,4SR)-7-chloro-4-(2-chloroacetoxy)-2,3,4,5-tetrahydro-1H-benzo[b]azepine-2-carboxylate, CHClNO, (IVb), as the major and minor products, respectively, and further reaction of (IVa) with aminoethanol gave the tricyclic target compound (4aRS,6SR)-9-chloro-6-hydroxy-3-(2-hydroxyethyl)-2,3,4a,5,6,7-hexahydrobenzo[f]pyrazino[1,2-a]azepine-1,4-dione, CHClNO, (V).

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Many oligo and polysaccharides (including paramylon) are critical in the Euglena gracilis life-cycle and they are synthesized by glycosyl transferases using UDP-glucose as a substrate. Herein, we report the molecular cloning of a gene putatively coding for a UDP-glucose pyrophosphorylase (EgrUDP-GlcPPase) in E. gracilis.

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Visceral leishmaniasis is a public health problem worldwide. The early diagnosis in dogs is crucial, since they are an epidemiologically relevant reservoir of the disease. The aim of a field study is to early identify the disease allowing rapid intervention to reduce its effects.

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To combat the deleterious effects that oxidation of the sulfur atom in methionine to sulfoxide may bring, aerobic cells express repair pathways involving methionine sulfoxide reductases (MSRs) to reverse the above reaction. Here, we show that Trypanosoma brucei, the causative agent of African trypanosomiasis, expresses two distinct trypanothione-dependent MSRs that can be distinguished from each other based on sequence, sub-cellular localisation and substrate preference. One enzyme found in the parasite's cytosol, shows homology to the MSRA family of repair proteins and preferentially metabolises the S epimer of methionine sulfoxide.

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Aim: The development of vaccines against Trypanosoma cruzi remains in an exploratory stage. Despite several antigen candidates have been evaluated, a comparison among the performance of the immunogens cannot be carried out because the available reports differ in formulations and infection model. In this work, we compared the protective capacity of seven T.

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Low molecular mass thiols and antioxidant enzymes have essential functions to detoxify reactive oxygen and nitrogen species maintaining cellular redox balance. The metabolic pathways for redox homeostasis in pathogenic (Leptospira interrogans) and free-living (Leptospira biflexa) leptospires species were not functionally characterized. We performed biochemical studies on recombinantly produced proteins to in depth analyze kinetic and structural properties of thioredoxin reductase (LinTrxR) and thioredoxin (LinTrx) from L.

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Facial expressions are an important way through which humans interact socially. Building a system capable of automatically recognizing facial expressions from images and video has been an intense field of study in recent years. Interpreting such expressions remains challenging and much research is needed about the way they relate to human affect.

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Unlabelled: Trypanosoma cruzi, the causative agent of Chagas disease, possesses two tryparedoxins (TcTXNI and TcTXNII), belonging to the thioredoxin superfamily. TXNs are oxidoreductases which mediate electron transfer between trypanothione and peroxiredoxins. This constitutes a difference with the host cells, in which these activities are mediated by thioredoxins.

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Background: Entamoeba histolytica, an intestinal parasite that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen and nitrogen species during tissue invasion. A flavodiiron protein and a rubrerythrin have been characterized in this human pathogen, although their physiological reductants have not been identified.

Methods: The present work deals with biochemical studies performed to reach a better understanding of the kinetic and structural properties of rubredoxin reductase and two ferredoxins from E.

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