Andrei Santos Siqueira

Draft Genome Sequence of the Brazilian Cyanobium sp. Strain CACIAM 14.

ABSTRACT Given the scarcity of data pertaining to whole-genome sequences of cyanobacterial strains isolated in Brazil, we hereby present the draft genome sequence of the Cyanobium sp. strain CACIAM 14, isolated in southeastern Amazonia.

Draft Genome Sequence of Blastomonas sp. Strain CACIA 14H2, a Heterotrophic Bacterium Associated with Cyanobacteria

ABSTRACT With the new methods for assembling sequence data from metagenomic samples, the genomic study of heterotrophic bacterium-cyanobacterium associations can now be improved. In this work, the draft genome sequence of Blastomonas sp. strain CACIA 14H2, obtained from a nonaxenic culture of a Cyanobium sp., is presented.

Draft Genome Sequence of Microcystis aeruginosa CACIAM 03, a Cyanobacterium Isolated from an Amazonian Freshwater Environment

ABSTRACT Given its toxigenic potential, Microcystis aeruginosa is an important bloom-forming cyanobacterium. Here, we present a draft genome and annotation of the strain CACIAM 03, which was isolated from an Amazonian freshwater environment.

Draft Genome Sequence of Rhodobacter sp. Strain CACIA 14H1, a Heterotrophic Bacterium Obtained from a Nonaxenic Culture of a Cyanobium Species

ABSTRACT Despite their prominent importance, few efforts have been paid to the genomic analysis of heterotrophic bacteria associated with cyanobacteria. Thus, this work presents the draft genome sequence (~3.9 Mbp) of a heterotrophic bacterium (Rhodobacter sp. strain CACIA 14H1) recovered from a nonaxenic culture of a Cyanobium species.

Determination of biodiesel properties based on a fatty acid profile of eight Amazon cyanobacterial strains grown in two different culture media

The primary source of biodiesel obtainment in Brazil is concentrated in oleaginous vegetables, especially soy. However, there is a great hold-up caused by competition with the food industry, which makes the search for alternative pathways that do not compete with other industries needed. The goal of this study was to investigate the biotechnological potential of cyanobacteria, which were grown in two different culture media, as an alternative approach for obtaining biodiesel. For this purpose, Microcystis aeruginosa CACIAM03, CACIAM08, Synechocystis sp. CACIAM05, Lyngbya sp. CACIAM07, Cyanobium sp. CACIAM14, Leptolyngbya sp. CACIAM18, Limnothrix redekei CACIAM25 and Planktothrix pseudoagardhii CACIAM27 were evaluated. Fatty acid composition was determined using gas chromatography. Fatty acids found in all strains were identified as palmitic acid (C16:0) (7.43–38.37% content), stearic acid (C18:0) (1.44–13.82%), caproic acid (C6:0) (0.82–78.84%) and oleic acid (C18:1) (1.13–46.76%). The biodiesel quality parameters were calculated based on the fatty acid profile. Strains that showed the best values and provided better biodiesel quality were Synechocystis sp. CACIAM05 and Microcystis aeruginosa CACIAM03 that were grown in BG-11 medium. This study showed us a promising source of biodiesel production from cyanobacterial lipids based on empirical calculations of the parameters of biodiesel quality that met the fuel standards. Furthermore, our results suggest the production of fatty acids through a metabolic route, due to the change in the profile of fatty acids in both culture media, providing valuable information for future engineering to increase the percentage of fatty acids that give better biodiesel quality.

Genomic screening of new putative antiviral lectins from Amazonian cyanobacteria based on a bioinformatics approach

Lectins are proteins of nonimmune origin, which are capable of recognizing and binding to glycoconjugate moieties. Some of them can block the interaction of viral glycoproteins to the host cell receptors acting as antiviral agents. Although cyanobacterial lectins have presented broad biotechnological potential, little research has been directed to Amazonian Cyanobacterial diversity. In order to identify new antiviral lectins, we performed genomic analysis in seven cyanobacterial strains from Coleção Amazônica de Cianobactérias e Microalgas (CACIAM). We found 75 unique CDS presenting one or more lectin domains. Since almost all were annotated as hypothetical proteins, we used homology modeling and molecular dynamics simulations to evaluate the structural and functional properties of three CDS that were more similar to known antiviral lectins. Nostoc sp. CACIAM 19 as well as Tolypothrix sp. CACIAM 22 strains presented cyanovirin‐N homologues whose function was confirmed by binding free energy calculations. Asn, Glu, Thr, Lys, Leu, and Gly, which were described as binding residues for cyanovirin, were also observed on those structures. As for other known cyanovirins, those residues in both our models also made favorable interactions with dimannose. Finally, Alkalinema sp. CACIAM 70d presented one CDS, which was identified as a seven‐bladed beta‐propeller structure with binding sites predicted for sialic acid and N‐acetylglucosamine. Despite its singular structure, our analysis suggested this molecule as a new putative antiviral lectin. Overall, the identification and the characterization of new lectins and their homologues are a promising area in antiviral research, and Amazonian cyanobacteria present biotechnological potential to be explored in this regard.

In silico characterization of a cyanobacterial plant-type isoaspartyl aminopeptidase/asparaginase

Asparaginases are found in a range of organisms, although those found in cyanobacteria have been little studied, in spite of their great potential for biotechnological application. This study therefore sought to characterize the molecular structure of an L-asparaginase from the cyanobacterium Limnothrix sp. CACIAM 69d, which was isolated from a freshwater Amazonian environment. After homology modeling, model validation was performed using a Ramachandran plot, VERIFY3D, and the RMSD. We also performed molecular docking and dynamics simulations based on binding free-energy analysis. Structural alignment revealed homology with the isoaspartyl peptidase/asparaginase (EcAIII) from Escherichia coli. When compared to the template, our model showed full conservation of the catalytic site. In silico simulations confirmed the interaction of cyanobacterial isoaspartyl peptidase/asparaginase with its substrate, β-Asp-Leu dipeptide. We also observed that the residues Thr154, Thr187, Gly207, Asp218, and Gly237 were fundamental to protein–ligand complexation. Overall, our results suggest that L-asparaginase from Limnothrix sp. CACIAM 669d has similar properties to E. coli EcAIII asparaginase. Our study opens up new perspectives for the biotechnological exploitation of cyanobacterial asparaginases.

In silico analysis of the cyanobacterial lectin scytovirin: new insights into binding properties

Scytovirin is a lectin isolated from the cyanobacterium Scytonema varium that has shown activity against HIV, SARS coronavirus and Zaire Ebola virus. Its 95 amino acids are divided into two structural domains (SD), the first spanning amino acids 1–48 (SD1) and the second 49–95 (SD2). Interestingly, the domains are nearly identical but differ in their affinities for carbohydrates. With the aim of enhancing understanding of the binding properties of scytovirin, we performed molecular dynamics (MD) simulations of scytovirin complexed with Man4. We set up three systems: (i) Man4 bound to both domains (SD1 + SD2) using the full-length protein; (ii) Man4 bound to an incomplete protein, containing only SD1 and (iii) Man4 bound to an incomplete protein containing only SD2. Contrary to other reports, binding free energy results suggest that Man4 can bind simultaneously to SD1 and SD2 binding regions, but SD1 individually has the best values of energy and the best affinity for Man4. Decomposition of the binding free energy showed that the residues that interact with Man4 were different in the three systems, suggesting that the binding mechanism of Man4 varies between full-length protein, SD1 and SD2. The results presented here may help to formulate strategies to use scytovirin and promote mutagenesis studies to improve the antiviral activity of scytovirin.

Draft Genome Sequence of Limnobacter sp. Strain CACIAM 66H1, a Heterotrophic Bacterium Associated with Cyanobacteria.

ABSTRACT Ecological interactions between cyanobacteria and heterotrophic prokaryotes are poorly known. To improve the genomic studies of heterotrophic bacterium-cyanobacterium associations, the draft genome sequence (3.2 Mbp) of Limnobacter sp. strain CACIAM 66H1, found in a nonaxenic culture of Synechococcus sp. (cyanobacteria), is presented here.