| Full text | |
| Author(s): Show less - |
Mobilon, Cristiane
[1]
;
Szymanski de Toledo, Marcelo Augusto
[2]
;
Paganelli, Fernanda Laroza
[3]
;
dos Santos, Clelton Aparecido
[2]
;
de Pace, Fernanda
[4]
;
de Paiva, Jacqueline Boldrin
[1]
;
Stehling, Eliana Guedes
[5]
;
Nakazato, Gerson
[6]
;
Balieiro, Aline Gambaro
[7]
;
da Silva Airoldi, Flavia Pereira
[7]
;
Machado Reis, Francisco de Assis
[7]
;
da Silveira, Wanderley Dias
[1]
Total Authors: 12
|
| Affiliation: | [1] Univ Estadual Campinas, Dept Genet Evolut & Bioagents, Campinas, SP - Brazil
[2] Univ Estadual Campinas, Ctr Mol Biol & Genet Engn, Campinas, SP - Brazil
[3] Univ Med Ctr Utrecht, Dept Med Microbiol, Utrecht - Netherlands
[4] Univ Estadual Campinas, Dept Internal Med, Campinas, SP - Brazil
[5] Univ Sao Paulo, Dept Toxicol & Bromatol Clin Anal, Ribeirao Preto, SP - Brazil
[6] Univ Estadual Londrina, Dept Microbiol, Londrina, PR - Brazil
[7] Univ Estadual Campinas, Inst Chem, Dept Organ Chem, Campinas, SP - Brazil
Total Affiliations: 7
|
| Document type: | Journal article |
| Source: | PROTEIN AND PEPTIDE LETTERS; v. 20, n. 2, p. 133-139, FEB 2013. |
| Web of Science Citations: | 0 |
| Abstract | |
Shigella flexneri is a Gram-negative bacillus that is responsible for a severe form of dysentery called Shigellosis, which mainly affects children and the elderly in both underdeveloped and developed countries. Pathogenic S. flexneri strains possess a large virulence plasmid that codes for effector proteins that are required for the entry and spread of the bacteria into colonocytes. Among these proteins is the translocator IpaC, which plays an important role in the invasion process; IpaC is implicated in pore formation in the host cell membrane and induces cytoskeletal rearrangements in macrophages and epithelial cells, thereby promoting bacterial entry. The ability of IpaC to insert into the plasma membrane is due to a large nonpolar region of the protein structure. This characteristic also renders difficulties in recovery and purification when the protein is expressed in E. coli. Several works have considered different methodologies for the improved production and purification of IpaC. Herein, we propose an alternative method that is based on changes in the induction temperature and extraction buffer to facilitate the accumulation of high yields of soluble proteins for their further processing and ultimate use in biotechnological approaches. (AU) | |