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

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About: Genomic screening of new putative antiviral lectins from Amazonian cyanobacteria based on a bioinformatics approach Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Genomic screening of new putative antiviral lectins from Amazonian cyanobacteria based on a bioinformatics approach
Creator	Santos, Silva Gonçalves, Costa Gonçalves, Silva Júnior, Vianez Lima, Jerônimo Lídio Da, João Ranieri, Alex Santos Siqueira, Andrei Alberdan, \| Delia, \| Evonnildo, \| Figueira Aguiar, Cristina
Source	Medline; PMC
abstract	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.
has issue date	2018-09-25(xsd:dateTime)
bibo:doi	10.1002/prot.25577
bibo:pmid	30035823
has license	no-cc
sha1sum (hex)	b62cb8b15ead1c29a8a4a3b39605dd0a5bbe2f33
schema:url	https://doi.org/10.1002/prot.25577
resource representing a document's title	Genomic screening of new putative antiviral lectins from Amazonian cyanobacteria based on a bioinformatics approach
has PubMed Central identifier	PMC7167734
has PubMed identifier	30035823
schema:publication	Proteins
resource representing a document's body	covid:b62cb8b15ead1c29a8a4a3b39605dd0a5bbe2f33#body_text
is schema:about of	named entity 'lectins' named entity 'domains' named entity 'hypothetical' named entity 'homologues' named entity 'TO IDENTIFY' named entity 'LECTIN' named entity 'ORIGIN' named entity 'TOLYPOTHRIX SP. CACIAM 22' named entity 'HOST CELL' named entity 'ANTIVIRAL' named entity 'CYANOVIRIN-N' named entity 'COLE' named entity 'FOUND' named entity 'INTERACTION' named entity 'BINDING' named entity 'BROAD' named entity 'MOLECULAR DYNAMICS SIMULATIONS' named entity 'HAVE' named entity 'lectins' named entity 'directed' named entity 'binding' named entity 'performed' named entity 'interaction' named entity 'cell receptors' named entity 'antiviral agents' named entity 'cyanobacterial' named entity 'antiviral' named entity 'homologues' named entity 'Cyanobacterial' named entity 'lectin' named entity 'Lectins' named entity 'biotechnological' named entity 'Amazonian' named entity 'Since' named entity 'protein' named entity 'Arginine' named entity 'Glu' named entity 'protonation' named entity 'lectin' named entity 'antiviral activity' named entity 'Cyanothece' named entity 'protein' named entity 'cytotoxic' named entity 'coronavirus' named entity 'homology modeling' named entity 'CDD' named entity 'microbicide' named entity 'Asn' named entity 'lectin' named entity 'beta-propeller' named entity 'RMSD' named entity 'Kcal' named entity 'organism' named entity 'amino acid sequences' named entity 'conformations' named entity 'cyanobacteria' named entity 'ligands' named entity 'crystallographic' named entity 'nanomolar' named entity 'antiviral' named entity 'ligand' named entity 'cyanobacteria' named entity 'complexation' named entity 'homology modeling' named entity 'adverse reactions' named entity 'lectins' named entity 'genomes' named entity 'Perl script' named entity 'sequence alignment' named entity 'steepest descent'

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