Carbohydrate binding protein Ec60/66 from Escherichia coli: identification, determination of biological role and association with E. coli from hospital infection samples

• Grant number: 06/04482-6
• Support Opportunities: Regular Research Grants
• Start date: March 01, 2007
• End date: February 28, 2009
• Field of knowledge: Biological Sciences - Immunology - Immunochemistry
• Principal Investigator: Ademilson Panunto-Castelo
• Grantee: Ademilson Panunto-Castelo
• Host Institution: Escola de Enfermagem de Ribeirão Preto (EERP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
• City of the host institution: Ribeirão Preto

Abstract

Escherichia coli is an Enterobacteriaceae specie that comprises a large number of groups and serological types. Although E. coli is a common member of normal intestinal microbiota in humans, it becomes infectious in immunocompromised or when gastrointestinal barrier is broken. Most importantly, some E. coli groups are responsible for intestinal infections leading to diarrheal diseases, which are one of the major health problems in developing countries, particularly among infants, and extraintestinal infections that greatly contribute to hospital infections. In general, distinct virulence characteristics of disease-causing serotypes or clones suggest that E. coli specie is composed of a relative large variety of pathogenic bacterias. Fimbriae are among the major bacterial virulence factor required to that bacterias colonise the tissues and establish infection. Some fimbriae have a carbohydrate recognition domain (lectin domain) in their terminal end that is essential for the colonisation and tissue invasion, mainly in bladder epithelium. Our preliminary data showed that E. coli present a mannose binding lectin, termed Ec60/66, which has not yet been described in the literature. The identification of this lectin is crucial to determine its biological role, as well as its possible involvement in the tissue colonisation by E. coli. Therefore, the aim of the project is to characterise, determine the amino acid sequence and identify Ec60/66 for its following evaluation as a virulence factor through immunomodulatory and inflammatory cytokines detection. Additionally, it will be determined the presence of Ec60/66 in clinical isolates of E. coli, in which the positive correlation will suggest that Ec60/66 is a predisposing factor in hospital infection by E. coli. The participation of Ec60/66 in the processes of colonisation and infection might open perspectives for the use of this protein as a target in therapeutic interventions. (AU)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

LANDGRAF, TAISE NATALI; BERLESE, ALAN; FERNANDES, FABRICIO FREITAS; MILANEZI, MARIANI LIMA; MARTINEZ, ROBERTO; PANUNTO-CASTELO, ADEMILSON. O receptor de aerobactina IutA, uma proteína isolada em coluna de agarose, não é essencial para a infecção por Escherichia coli uropatogênica. Revista Latino-Americana de Enfermagem, v. 20, n. 2, p. 340-345, MAR-APR 2012. (06/04482-6)

TAISE NATALI LANDGRAF; ALAN BERLESE; FABRICIO FREITAS FERNANDES; MARIANI LIMA MILANEZI; ROBERTO MARTINEZ; ADEMILSON PANUNTO-CASTELO. O receptor de aerobactina IutA, uma proteína isolada em coluna de agarose, não é essencial para a infecção por Escherichia coli uropatogênica. Revista Latino-Americana de Enfermagem, v. 20, n. 2, p. 340-345, 2012-04-00. (06/04482-6)

LANDGRAF, TAISE NATALI; BERLESE, ALAN; FERNANDES, FABRICIO FREITAS; MILANEZI, MARIANI LIMA; MARTINEZ, ROBERTO; PANUNTO-CASTELO, ADEMILSON. The ferric aerobactin receptor IutA, a protein isolated on agarose column, is not essential for uropathogenic Escherichia coli infection. REVISTA LATINO-AMERICANA DE ENFERMAGEM, v. 20, n. 2, p. 6-pg., 2012-03-01. (06/04482-6)