Renata Pinheiro Chaves , Ana Kátia Barbosa dos Santos , Alexandre Lopes Andrade , Aryane de Azevedo Pinheiro , Juliana Meneses de Sena Silva , Francisca Manuela Santos da Silva , Jucilene Pereira de Sousa , Ito Liberato Barroso Neto , Eduardo Henrique Salviano Bezerra , Jade Oliveira Abreu , Fátima Cristiane Teles de Carvalho , Oscarina Viana de Sousa , Bruno Lopes de Sousa , Bruno Anderson Matias da Rocha , André Luis Coelho Silva , Luiz Gonzaga do Nascimento Neto , Mayron Alves de Vasconcelos , Edson Holanda Teixeira , Rômulo Farias Carneiro , Alexandre Holanda Sampaio , Celso Shiniti Nagano
{"title":"丝状梭菌凝集素的结构研究及其抗菌和伤口愈合作用。","authors":"Renata Pinheiro Chaves , Ana Kátia Barbosa dos Santos , Alexandre Lopes Andrade , Aryane de Azevedo Pinheiro , Juliana Meneses de Sena Silva , Francisca Manuela Santos da Silva , Jucilene Pereira de Sousa , Ito Liberato Barroso Neto , Eduardo Henrique Salviano Bezerra , Jade Oliveira Abreu , Fátima Cristiane Teles de Carvalho , Oscarina Viana de Sousa , Bruno Lopes de Sousa , Bruno Anderson Matias da Rocha , André Luis Coelho Silva , Luiz Gonzaga do Nascimento Neto , Mayron Alves de Vasconcelos , Edson Holanda Teixeira , Rômulo Farias Carneiro , Alexandre Holanda Sampaio , Celso Shiniti Nagano","doi":"10.1016/j.biochi.2023.05.016","DOIUrl":null,"url":null,"abstract":"<div><p><span>The SfL-1 isoform<span> from the marine red algae </span></span><em>Solieria filiformis</em><span> was produced in recombinant form (rSfL-1) and showed hemagglutinating activity and inhibition similar to native SfL. The analysis of circular dichroism<span><span> revealed the predominance of β-strands structures with spectra of βI-proteins for both lectins, which had Melting Temperature (Tm) between 41 °C and 53 °C. The three-dimensional structure of the rSfL-1 was determined by X-ray crystallography, revealing that it is composed of two β-barrel domains formed by five antiparallel </span>β chains linked by a short peptide between the β-barrels. SfL and rSfL-1 were able to agglutinate strains of </span></span><em>Escherichia coli</em> and <span><em>Staphylococcus aureus</em></span><span> and did not show antibacterial activity. However, SfL induced a reduction in </span><em>E. coli</em> biomass at concentrations from 250 to 125 μg mL<sup>−1</sup>, whereas rSfL-1 induced reduction in all concentrations tested. Additionally, rSfL-1 at concentrations from 250 to 62.5 μg mL<sup>−1</sup><span>, showed a statistically significant reduction in the number of colony-forming units, which was not noticed for SfL. Wound healing assay showed that the treatments with SfL and rSfL-1 act in reducing the inflammatory response and in the activation and proliferation of fibroblasts by a larger and fast deposition of collagen.</span></p></div>","PeriodicalId":251,"journal":{"name":"Biochimie","volume":"214 ","pages":"Pages 61-76"},"PeriodicalIF":3.3000,"publicationDate":"2023-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Structural study and antimicrobial and wound healing effects of lectin from Solieria filiformis (Kützing) P.W.Gabrielson\",\"authors\":\"Renata Pinheiro Chaves , Ana Kátia Barbosa dos Santos , Alexandre Lopes Andrade , Aryane de Azevedo Pinheiro , Juliana Meneses de Sena Silva , Francisca Manuela Santos da Silva , Jucilene Pereira de Sousa , Ito Liberato Barroso Neto , Eduardo Henrique Salviano Bezerra , Jade Oliveira Abreu , Fátima Cristiane Teles de Carvalho , Oscarina Viana de Sousa , Bruno Lopes de Sousa , Bruno Anderson Matias da Rocha , André Luis Coelho Silva , Luiz Gonzaga do Nascimento Neto , Mayron Alves de Vasconcelos , Edson Holanda Teixeira , Rômulo Farias Carneiro , Alexandre Holanda Sampaio , Celso Shiniti Nagano\",\"doi\":\"10.1016/j.biochi.2023.05.016\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><span>The SfL-1 isoform<span> from the marine red algae </span></span><em>Solieria filiformis</em><span> was produced in recombinant form (rSfL-1) and showed hemagglutinating activity and inhibition similar to native SfL. The analysis of circular dichroism<span><span> revealed the predominance of β-strands structures with spectra of βI-proteins for both lectins, which had Melting Temperature (Tm) between 41 °C and 53 °C. The three-dimensional structure of the rSfL-1 was determined by X-ray crystallography, revealing that it is composed of two β-barrel domains formed by five antiparallel </span>β chains linked by a short peptide between the β-barrels. SfL and rSfL-1 were able to agglutinate strains of </span></span><em>Escherichia coli</em> and <span><em>Staphylococcus aureus</em></span><span> and did not show antibacterial activity. However, SfL induced a reduction in </span><em>E. coli</em> biomass at concentrations from 250 to 125 μg mL<sup>−1</sup>, whereas rSfL-1 induced reduction in all concentrations tested. Additionally, rSfL-1 at concentrations from 250 to 62.5 μg mL<sup>−1</sup><span>, showed a statistically significant reduction in the number of colony-forming units, which was not noticed for SfL. 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Structural study and antimicrobial and wound healing effects of lectin from Solieria filiformis (Kützing) P.W.Gabrielson
The SfL-1 isoform from the marine red algae Solieria filiformis was produced in recombinant form (rSfL-1) and showed hemagglutinating activity and inhibition similar to native SfL. The analysis of circular dichroism revealed the predominance of β-strands structures with spectra of βI-proteins for both lectins, which had Melting Temperature (Tm) between 41 °C and 53 °C. The three-dimensional structure of the rSfL-1 was determined by X-ray crystallography, revealing that it is composed of two β-barrel domains formed by five antiparallel β chains linked by a short peptide between the β-barrels. SfL and rSfL-1 were able to agglutinate strains of Escherichia coli and Staphylococcus aureus and did not show antibacterial activity. However, SfL induced a reduction in E. coli biomass at concentrations from 250 to 125 μg mL−1, whereas rSfL-1 induced reduction in all concentrations tested. Additionally, rSfL-1 at concentrations from 250 to 62.5 μg mL−1, showed a statistically significant reduction in the number of colony-forming units, which was not noticed for SfL. Wound healing assay showed that the treatments with SfL and rSfL-1 act in reducing the inflammatory response and in the activation and proliferation of fibroblasts by a larger and fast deposition of collagen.
期刊介绍：
Biochimie publishes original research articles, short communications, review articles, graphical reviews, mini-reviews, and hypotheses in the broad areas of biology, including biochemistry, enzymology, molecular and cell biology, metabolic regulation, genetics, immunology, microbiology, structural biology, genomics, proteomics, and molecular mechanisms of disease. Biochimie publishes exclusively in English.
Articles are subject to peer review, and must satisfy the requirements of originality, high scientific integrity and general interest to a broad range of readers. Submissions that are judged to be of sound scientific and technical quality but do not fully satisfy the requirements for publication in Biochimie may benefit from a transfer service to a more suitable journal within the same subject area.
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