Diego Mariano

Dr. Diego Mariano

Federal University of Minas Gerais
orcid

Research Focus & Metrics

Academic Career Length

13Years (2014-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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30 October 2014 in Microbiology Resource Announcements
Verified
Journal Article
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LOLeticia Oliveira
Leticia Oliveira
TSTessália D. L. Saraiva
Tessália D. L. Saraiva
Siomar SoaresSiomar Soares
Siomar Soares
RRRommel Thiago Juca Ramos
Rommel Thiago Juca Ramos
PSPablo Sá
Pablo Sá
Vasco AzevedoVasco Azevedo
Vasco Azevedo
Lactococcus lactis subsp. lactis NCDO 2118 is a nondairy lactic acid bacterium, a xylose fermenter, and a gamma-aminobutyric acid (GABA) producer isolated from frozen peas. Here, we report the complete genome sequence of L. lactis NCDO 2118, a strain with probiotic potential activity.

4 September 2019 in Molecules
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Journal Article
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LCLeon Costa
Leon Costa
Diego MarianoDiego Mariano
Diego Mariano
RRRafael Eduardo Oliveira Rocha
Rafael Eduardo Oliveira Rocha
JKJohannes Kraml
Johannes Kraml
Carlos Henrique da SilveiraCarlos Henrique da Silveira
Carlos Henrique da Silveira
LLLeonardo Henrique Lima
Leonardo Henrique Lima
β-Glucosidases are enzymes with high importance for many industrial processes, catalyzing the last and limiting step of the conversion of lignocellulosic material into fermentable sugars for biofuel production. However, β-glucosidases are inhibited by high concentrations of the product (glucose), which limits the biofuel production on an industrial scale. For this reason, the structural mechanisms of tolerance to product inhibition have been the target of several studies. In this study, we performed in silico experiments, such as molecular dynamics (MD) simulations, free energy landscape (FEL) estimate, Poisson–Boltzmann surface area (PBSA), and grid inhomogeneous solvation theory (GIST) seeking a better understanding of the glucose tolerance and inhibition mechanisms of a representative GH1 β-glucosidase and a GH3 one. Our results suggest that the hydrophobic residues Y180, W350, and F349, as well the polar one D238 act in a mechanism for glucose releasing, herein called “slingshot mechanism”, dependent also on an allosteric channel (AC). In addition, water activity modulation and the protein loop motions suggest that GH1 β-Glucosidases present an active site more adapted to glucose withdrawal than GH3, in consonance with the GH1s lower product inhibition. The results presented here provide directions on the understanding of the molecular mechanisms governing inhibition and tolerance to the product in β-glucosidases and can be useful for the rational design of optimized enzymes for industrial interests.

12 March 2019 in Biochemistry and Molecular Biology Education
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Journal Article
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Diego MarianoDiego Mariano
Diego Mariano
PMPedro Martins
Pedro Martins
LSLucianna Helene Santos
Lucianna Helene Santos
RMRaquel Cardoso de Melo‐ Minardi
Raquel Cardoso de Melo‐ Minardi

8 April 2016 in Standards in Genomic Sciences
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SASintia Almeida
Sintia Almeida
Sandeep TiwariSandeep Tiwari
Sandeep Tiwari
Diego MarianoDiego Mariano
Diego Mariano
FSFlávia Souza
Flávia Souza
SJSyed Babar Jamal
Syed Babar Jamal
Vasco AzevedoVasco Azevedo
Vasco Azevedo
Corynebacterium pseudotuberculosisstrain VD57 (Cp_VD57), a highly virulent, nonmotile, non-sporulating, and a mesophilic bacterium, was isolated from a goat’s granulomatous lesion in the municipality of Juazeiro, Bahia State, Brazil. Here, we describe a set of features of the strain, together with the details of its complete genome sequence and annotation. The genome comprises of a 2.5 Mbp long, single circular genome with 2,101 protein-coding genes, 12 rRNA, 49 tRNA and 47 pseudogenes and a G + C content of 52.85 %. Genetic variation was detected in Cp_VD57 usingC. pseudotuberculosisstrain 1002 as reference, wherein small genomic insertions and deletions were identified. The comparative analysis of the genome sequence provides means to better understand the host pathogen interactions of this strain and can also help us to understand the molecular and genetic basis of virulence of this bacterium.

15 December 2016 in BMC Bioinformatics
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Journal Article
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Diego MarianoDiego Mariano
Diego Mariano
FPFelipe Luiz Pereira
Felipe Luiz Pereira
EAEdgar L. Aguiar
Edgar L. Aguiar
LOLeticia Oliveira
Leticia Oliveira
LBLeandro Benevides
Leandro Benevides
Vasco AzevedoVasco Azevedo
Vasco Azevedo
The evolution of Next-Generation Sequencing (NGS) has considerably reduced the cost per sequenced-base, allowing a significant rise of sequencing projects, mainly in prokaryotes. However, the range of available NGS platforms requires different strategies and software to correctly assemble genomes. Different strategies are necessary to properly complete an assembly project, in addition to the installation or modification of various software. This requires users to have significant expertise in these software and command line scripting experience on Unix platforms, besides possessing the basic expertise on methodologies and techniques for genome assembly. These difficulties often delay the complete genome assembly projects. In order to overcome this, we developed SIMBA (SImple Manager for Bacterial Assemblies), a freely available web tool that integrates several component tools for assembling and finishing bacterial genomes. SIMBA provides a friendly and intuitive user interface so bioinformaticians, even with low computational expertise, can work under a centralized administrative control system of assemblies managed by the assembly center head. SIMBA guides the users to execute assembly process through simple and interactive pages. SIMBA workflow was divided in three modules: (i) projects: allows a general vision of genome sequencing projects, in addition to data quality analysis and data format conversions; (ii) assemblies: allows de novo assemblies with the software Mira, Minia, Newbler and SPAdes, also assembly quality validations using QUAST software; and (iii) curation: presents methods to finishing assemblies through tools for scaffolding contigs and close gaps. We also presented a case study that validated the efficacy of SIMBA to manage bacterial assemblies projects sequenced using Ion Torrent PGM. Besides to be a web tool for genome assembly, SIMBA is a complete genome assemblies project management system, which can be useful for managing of several projects in laboratories. SIMBA source code is available to download and install in local webservers at http://ufmg-simba.sourceforge.net .

1 January 2014 in Genetics and Molecular Research
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Journal Article
Closed access
Diego MarianoDiego Mariano
Diego Mariano
CLC. Leite
C. Leite
LSL.H.S. Santos
L.H.S. Santos
LML.F. Marins
L.F. Marins
KMKarina dos Santos Machado
Karina dos Santos Machado
RMR.C. de Melo-Minardi
R.C. de Melo-Minardi
β-glucosidases are enzymes that catalyze the hydrolysis of oligosaccharides and disaccharides, such as cellobiose. These enzymes play a key role in cellulose degrading, such as alleviating product inhibition of cellulases. Consequently, they have been considered essential for the biofuel industry. However, the majority of the characterized β-glucosidases is inhibited by glucose. Hence, glucose-tolerant β-glucosidases have been targeted to improve the production of second-generation biofuels. In this paper, we proceeded a systematic literature review (SLR), collected protein structures and constructed a database of glucose-tolerant β-glucosidases, called betagdb. SLR was performed at PubMed, ScienceDirect and Scopus Library databases and conducted according to PRISMA framework. It was conducted in five steps: i) analysis of duplications, ii) title reading, iii) abstract reading, iv) diagonal reading, and v) full-text reading. The second, third, fourth, and fifth steps were performed independently by two researchers. Besides, we performed bioinformatics analysis on the collected data, such as structural and multiple alignments to detect the most conserved residues in the catalytic pocket, and molecular docking to characterize essential residues for substrate recognizing, glucose tolerance, and the β-glucosidase activity. We selected 27 papers, 23 sequences, and 5 PDB files of glucose-tolerant β-glucosidases. We characterized 11 highly conserved residues: H121, W122, N166, E167, N297, Y299, E355, W402, E409, W410, and F418. The presence of these residues may be essential for β-glucosidases. We also discussed the importance of residues W169, C170, L174, H181, and T226. Furthermore, we proposed that the number of contacts for each residue in the catalytic pocket might be a metric that could be used to suggest mutations. We believe that the herein propositions, together with the sequence and structural data collection, might be helpful for effective engineering of β-glucosidases for biofuel production and may help to shed some light on the degradation of cellulosic biomass.