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Strategies to display heterologous proteins on the cell surface of lactic acid bacteria using as anchor the C-terminal domain of Lactobacillus acidophilus SlpA.
Gordillo, Tania B; Palumbo, Miranda C; Allievi, Mariana Claudia; Fernández Do Porto, Darío A; Ruzal, Sandra M; Palomino, María Mercedes.
Afiliação
  • Gordillo TB; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Cdad. Universitaria, Pabellón II, 4 piso, Lab QB40, CABA, C1428EGA, Buenos Aires, Argentina.
  • Palumbo MC; Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales (IQUIBICEN), CONICET-Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Allievi MC; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Cdad. Universitaria, Pabellón II, 4 piso, Lab QB40, CABA, C1428EGA, Buenos Aires, Argentina.
  • Fernández Do Porto DA; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Cdad. Universitaria, Pabellón II, 4 piso, Lab QB40, CABA, C1428EGA, Buenos Aires, Argentina.
  • Ruzal SM; Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales (IQUIBICEN), CONICET-Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Palomino MM; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Cdad. Universitaria, Pabellón II, 4 piso, Lab QB40, CABA, C1428EGA, Buenos Aires, Argentina.
World J Microbiol Biotechnol ; 36(11): 169, 2020 Oct 12.
Article em En | MEDLINE | ID: mdl-33043388
The surface-layer (S-layer) protein of Lactobacillus acidophilus is a crystalline array of self-assembling subunits, non-covalently bound to the most outer cell wall envelope, which constitutes up to 20% of the total cell protein content. These attributes make S-layer proteins an excellent anchor for the development of microbial cell-surface display systems. In L. acidophilus, the S-layer is formed predominantly by the protein SlpA. We have previously shown that the C-terminal domain of SlpA is responsible for the cell wall anchorage on L. acidophilus ATCC 4356. In the present study, we evaluated the C-terminal domain of SlpA of L. acidophilus ATCC 4356 as a potential anchor domain to display functional proteins on the surface of non-genetically modified lactic acid bacteria (LAB). To this end, green fluorescent protein (GFP)-CTSlpA was firstly produced in Escherichia coli and the recombinant proteins were able to spontaneously bind to the cell wall of LAB in a binding assay. GFP was successfully displayed on the S-layer stripped surface of L. acidophilus. Both the binding stability and cell survival of L. acidophilus decorated with the recombinant protein were then studied in simulated gastrointestinal conditions. Furthermore, NaCl was tested as a safer alternative to LiCl for S-layer removal. This study presents the development of a protein delivery platform involving L. acidophilus, a microorganism generally regarded as safe, which utilizes the contiguous, non-covalently attached S-layer at the cell surface of the bacterium without introducing any genetic modification.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Membrana Celular / Lactobacillales / Lactobacillus acidophilus Idioma: En Revista: World J Microbiol Biotechnol Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Argentina País de publicação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Membrana Celular / Lactobacillales / Lactobacillus acidophilus Idioma: En Revista: World J Microbiol Biotechnol Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Argentina País de publicação: Alemanha