Phenotypical characterization and adhesin identification in Escherichia coli strains isolated from dogs with urinary tract infections

Pathogenic strains of Escherichia coli are the most common bacteria associated with urinary tract infections in both humans and companion animals. Standard biochemical tests may be useful in demonstrating detailed phenotypical characteristics of these strains. Thirteen strains of E. coli isolated from dogs with UTIs were submitted to biochemical tests, serotyping for O and H antigens and antimicrobial resistance testing. Furthermore, the presence of papC, sfa, and afa genes was evaluated by PCR, and genetic relationships were established using enterobacterial repetitive intergenic consensus PCR (ERIC-PCR). The antimicrobial that showed the highest resistance rate among the isolates was nalidixic acid (76.9%), followed by cephalotin (69.2%), sulfamethoxazole + trimethoprim (61.5%), tetracycline (61.5%), streptomycin (53.8%), ciprofloxacin (53.8%), ampicillin (46.2%), gentamicin (30.8%) and chloramphenicol (23.1%). No isolate was resistant either to meropenem or nitrofurantoin. Among the five clusters that were identified using ERIC-PCR, one cluster (A) had only one strain, which belonged to a serotype with zoonotic potential (O6:H31) and showed the genes papC+, sfa+, afa-. Strains with the genes papC-, sfa+, afa- were found in two other clusters (C and D), whereas all strains in clusters B and E possessed papC-, sfa-, afa- genes. Sucrose and raffinose phenotypic tests showed some ability in discriminating clusters A, B and C from clusters D and E

Glucocorticoid-induced leucine zipper modulates macrophage polarization and apoptotic cell clearance.

Macrophages are professional phagocytes that display remarkable plasticity, with a range of phenotypes that can be broadly characterized by the M1/M2 dichotomy. Glucocorticoid (GC)-induced leucine zipper (GILZ) is a protein known to mediate anti-inflammatory and some pro-resolving actions, including as neutrophil apoptosis. However, the role of GILZ in key macrophage function is not well understood. Here, we investigated the role of GILZ on macrophage reprogramming and efferocytosis. Using murine bone-marrow-derived macrophages (BMDMs), we found that GILZ was expressed in naive BMDMs and exhibited increased expression in M2-like macrophages (IL4-differentiated). M1-like macrophages (IFN/LPS-differentiated) from GILZ-/- mice showed higher expression of the M1 markers CD86, MHC class II, iNOS, IL-6 and TNF-α, associated with increased levels of phosphorylated STAT1 and lower IL-10 levels, compared to M1-differentiated cells from WT mice. There were no changes in the M2 markers CD206 and arginase-1 in macrophages from GILZ-/- mice differentiated with IL-4, compared to cells from WT animals. Treatment of M1-like macrophages with TAT-GILZ, a cell-permeable GILZ fusion protein, decreased the levels of CD86 and MHC class II in M1-like macrophages without modifying CD206 levels in M2-like macrophages. In line with the in vitro data, increased numbers of M1-like macrophages were found into the pleural cavity of GILZ-/- mice after LPS-injection, compared to WT mice. Moreover, efferocytosis was defective in the context of GILZ deficiency, both in vitro and in vivo. Conversely, treatment of LPS-injected mice with TAT-GILZ promoted inflammation resolution, associated with lower numbers of M1-like macrophages and increased efferocytosis. Collectively, these data indicate that GILZ is a regulator of important macrophage functions, contributing to macrophage reprogramming and efferocytosis, both key steps for the resolution of inflammation

Dietary factors associated with metabolic syndrome in Brazilian adults

<p>Abstract</p> <p>Background</p> <p>Metabolic Syndrome (MS) is defined as the association of numerous factors that increase cardiovascular risk and diet is one of the main factors related to increase the MS in the population. This study aimed to evaluate the association of diet on the presence of MS in an adult population sample.</p> <p>Methodology</p> <p>305 adults were clinically screened to participate in a lifestyle modification program. Anthropometric assessments included waist circumference (WC), body fat and calculated BMI (kg/m²) and muscle-mass index (MMI kg/m²). Dietary intake was estimated by 24 h dietary recall. Fasting blood was used for biochemical analysis. MS was diagnosed using NCEP-ATPIII (2001) criteria with adaptation for glucose (≥ 100 mg/dL). Logistic regression (Odds ratio) was performed in order to determine the odds ratio for developing MS according to dietary intake.</p> <p>Results</p> <p>An adequate intake of fruits, OR = 0.52 (CI:0.28-0.98), and an intake of more than 8 different items in the diet (variety), OR = 0.31 (CI:0.12-0.79) showed to be a protective factor against a diagnosis of MS. Saturated fat intake greater than 10% of total caloric value represented a risk for MS diagnosis, OR = 2.0 (1.04-3.84).</p> <p>Conclusion</p> <p>Regarding the dietary aspect, a risk factor for MS was higher intake of saturated fat, and protective factors were high diet variety and adequate fruit intake.</p

The role and effects of glucocorticoid-induced leucine zipper in the context of inflammation resolution

Submitted by sandra infurna ([email protected]) on 2016-05-19T12:38:39Z No. of bitstreams: 1 patricia_silva_etal_IOC-2015.pdf: 1795107 bytes, checksum: aae9a4c71e74f045ce360987eb292feb (MD5)Approved for entry into archive by sandra infurna ([email protected]) on 2016-05-19T13:16:43Z (GMT) No. of bitstreams: 1 patricia_silva_etal_IOC-2015.pdf: 1795107 bytes, checksum: aae9a4c71e74f045ce360987eb292feb (MD5)Made available in DSpace on 2016-05-19T13:16:43Z (GMT). No. of bitstreams: 1 patricia_silva_etal_IOC-2015.pdf: 1795107 bytes, checksum: aae9a4c71e74f045ce360987eb292feb (MD5) Previous issue date: 2015Universidade Federal de Minas Gerais. Faculdade de Farmácia. Departamento de Análises Clínicas e Toxicológicas. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Bioquímica e Imunologia. Imunofarmacologia. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Morfologia. Belo Horizonte, MG, Brasil.Universidade Federal de Minas Gerais. Faculdade de Farmácia. Departamento de Análises Clínicas e Toxicológicas. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Bioquímica e Imunologia. Imunofarmacologia. Belo Horizonte, MG, Brasil.Universidade Federal de Minas Gerais. Departamento de Bioquímica e Imunologia. Imunofarmacologia. Belo Horizonte, MG, Brasil / Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Vírus Respiratórios e do Sarampo. Rio de Janeiro, RJ, Brasil.Universidade Federal de Minas Gerais. Faculdade de Farmácia. Departamento de Análises Clínicas e Toxicológicas. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Bioquímica e Imunologia. Imunofarmacologia. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Morfologia. Belo Horizonte, MG, Brasil.Universidade Federal de Minas Gerais. Faculdade de Farmácia. Departamento de Análises Clínicas e Toxicológicas. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Bioquímica e Imunologia. Imunofarmacologia. Belo Horizonte, MG, Brasil.Universidade Federal de Minas Gerais. Imunofarmacologia, Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, BrasilUniversidade Federal de Minas Gerais. Faculdade de Farmácia. Departamento de Análises Clínicas e Toxicológicas. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Bioquímica e Imunologia. Imunofarmacologia. Belo Horizonte, MG, Brasil.Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Biologia Geral. Belo Horizonte, MG, Brasil.Universidade de São Paulo. Faculdade de Ciências Farmacêuticas. São Paulo, SP, BrasilFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Inflamação. Rio de Janeiro, RJ, Brasil.Universidade Federal de Minas Gerais. Faculdade de Farmácia. Departamento de Análises Clínicas e Toxicológicas. Belo Horizonte, MG, Brasil.Universidade Federal de Minas Gerais. Imunofarmacologia, Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Morfologia. Belo Horizonte, MG, Brasil.University of Perugia. Department of Medicine. Section of Pharmacology. Perugia, Italy.University of Perugia. Department of Medicine. Section of Pharmacology. Perugia, Italy.Monash University Centre for Inflammatory Diseases. Monash Medical Centre. Clayton, Victoria 3168, Australia.Monash University Centre for Inflammatory Diseases. Monash Medical Centre. Clayton, Victoria 3168, Australia.Universidade Federal de Minas Gerais. Imunofarmacologia, Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brasil.Universidade Federal de Minas Gerais. Faculdade de Farmácia. Departamento de Análises Clínicas e Toxicológicas. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Bioquímica e Imunologia. Imunofarmacologia. Belo Horizonte, MG, Brasil / Universidade Federal de Minas Gerais. Departamento de Morfologia. Belo Horizonte, MG, Brasil.Glucocorticoid (GC)-induced leucine zipper (GILZ) has been shown to mediate or mimic several actions of GC. This study assessed the role of GILZ in self-resolving and GC-induced resolution of neutrophilic inflammation induced by LPS in mice. GILZ expression was increased during the resolution phase of LPS-induced pleurisy, especially in macrophages with resolving phenotypes. Pretreating LPS-injected mice with trans-activator of transcription peptide (TAT)-GILZ, a cell-permeable GILZ fusion protein, shortened resolution intervals and improved resolution indices. Therapeutic administration of TAT-GILZ induced inflammation resolution, decreased cytokine levels, and promoted caspase-dependent neutrophil apoptosis. TAT-GILZ also modulated the activation of the survival-controlling proteins ERK1/2, NF-κB and Mcl-1. GILZ deficiency was associated with an early increase of annexin A1 (AnxA1) and did not modify the course of neutrophil influx induced by LPS. Dexamethasone treatment resolved inflammation and induced GILZ expression that was dependent on AnxA1. Dexamethasone-induced resolution was not altered in GILZ(-/-) mice due to compensatory expression and action of AnxA1. Our results show that therapeutic administration of GILZ efficiently induces a proapoptotic program that promotes resolution of neutrophilic inflammation induced by LPS. Alternatively, a lack of endogenous GILZ during the resolution of inflammation is compensated by AnxA1 overexpression