Purification of multifunctional substances active against Shigella sonnei

• Autor(a) principal: Jaqueline Silvana Moreira
• Data de Publicação: 2022
• Outros Autores: Jamil Silvano de Oliveira, Marcelo Porto Bemquerer, Ricardo Andrez Machado de Ávila, Daniel Moreira Dos Santos, Desielle de Matos Clementino, Bruna de Toledo Maria, Paula Prazeres Magalhães, Luiz de Macêdo Farias
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UFMG
• Texto Completo: http://hdl.handle.net/1843/61235; https://orcid.org/0000-0002-0851-5610; https://orcid.org/0000-0002-9740-5818; https://orcid.org/0000-0002-1303-0490
• topic: Shigella sonnei; Shigellosis; Multifuncional substances; Antimicrobial peptides and proteins; Shigella sonnei; Disenteria bacilar; Peptídeos catiônicos antimicrobianos

Shigella is the etiological agent of shigellosis. Antimicrobial peptides and proteins are biologically active substances produced by prokaryotes and eukaryotes that may present antagonistic activity against a wide range of microorganism. In this study, the intracellular extract of a Shigella sonnei isolate was precipitated with 75% ammonium sulfate and purified by sequential chromatography steps using ion exchange, molecular exclusion, and reversed-phase columns. Analysis by mass spectrometry identified three substances with molecular masses of 7.2, 9.2 and 10.7 kDa, active against another Shigella sonnei isolate. The amino acid sequences of the active substances were evaluated with the aid of BLAST - P software. The antagonistic substances were identified, respectively, as 50S ribosomal protein L29 of Escherichia coli, DNA-binding protein HU-beta and ribosome hibernation promoting factor both of Shigella sonnei. Data demonstrated that Shigella sonnei synthesizes three antimicrobial substances that present other classical functions, active against another isolate of the same species.