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1.
Osteoporos Int ; 31(1): 175-180, 2020 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-31641800

RESUMEN

Diabetes mellitus is associated with a higher risk of fracture. In this study, we analysed the bone quality of premenopausal women with type 1 diabetes mellitus by microindentation. No differences in bone quality were identified between patients and healthy controls, suggesting that intensive insulin therapy can preserve bone health. PURPOSE: To compare the bone quality of women with type 1 diabetes mellitus (T1DM) and healthy controls, and to determine the relationship with bone mineral density (BMD). METHODS: This was a cross-sectional study of 45 premenopausal women with T1DM and 21 healthy controls, matched according to age and BMI. Clinical parameters, BMD and bone tissue mechanical properties (assessed using the bone material strength index [BMSi]) were evaluated in each group using microindentation. In T1DM patients, glycosylated haemoglobin (HbA1c), the number of hypoglycaemic events and the status of chronic complications were also analysed. RESULTS: No differences in BMSi or BMD between T1DM patients and healthy controls were identified. In the T1DM patients, the mean HbA1c was 7.52% ± 1.00% and the mean time elapsed since diagnosis was 22.6 ± 12.2 years. Eight patients (17.7%) met the criteria for metabolic syndrome (MetS), and microvascular complications were present in 12 patients (26.7%). Neither the number of features of MetS present nor the presence of microangiopathy was found to be associated with BMSi. CONCLUSIONS: T1DM premenopausal patients showed bone tissue properties comparable to those shown by controls. Further larger-scale studies should be conducted to confirm these results.


Asunto(s)
Densidad Ósea , Diabetes Mellitus Tipo 1 , Fracturas Óseas , Adulto , Huesos , Estudios Transversales , Diabetes Mellitus Tipo 1/complicaciones , Diabetes Mellitus Tipo 1/tratamiento farmacológico , Femenino , Humanos , Persona de Mediana Edad , Premenopausia
2.
Rev Clin Esp (Barc) ; 220(3): 167-173, 2020 Apr.
Artículo en Inglés, Español | MEDLINE | ID: mdl-31739985

RESUMEN

BACKGROUND AND OBJECTIVES: Hospitalized surgical patients are increasing in medical complexity, thereby increasing the need for support by internal medicine departments. This support is provided through interconsultations, which present problems that have resulted in the development of shared care (SC). Our objective was to compare the healthcare results achieved by the SC and interconsultation models in Orthopaedic Surgery and Trauma. MATERIALS AND METHODS: We conducted an observational, prospective, multicentre study of patients hospitalized for emergency Orthopaedic Surgery and Trauma recorded in the REINA-SEMI registry, treated by internal medicine departments through interconsultation or SC. We recorded the demographic characteristics, comorbidity, medical complications, hospital stay and mortality. RESULTS: The study included 697 patients, 415 with SC and 282 with interconsultations. The SC patients were older (78.9 vs. 74.3; P<.001) underwent more operations (89.9 vs. 78.7%; P<.001), had fewer medical complications (50.4 vs. 62.8%; P<.001) and had shorter hospital stays (10 vs. 18 days; P<.001), with no differences in comorbidity or mortality. The following independent factors were associated with stays longer than 15 days: heart failure (OR 3.4; 95% CI 1.8-6.1; P<.001), the male sex (OR 1.9; 95% CI 1.2-3.1; P=.004), electrolyte disorder (OR 2.4; 95% CI 1.3-4.4; P=.003), respiratory infection (OR 1.9; 95% CI 1.04-3.7; P=.035), surgical delay (OR 1.1; 95% CI 1.08-1.2; P<.001) and treatment using the interconsultation on demand model (OR 3.5; 95% CI 2.3-5.4; P<.001). CONCLUSIONS: SC offers better healthcare results than interconsultations for patients hospitalized for emergency Orthopaedic Surgery and Trauma.

4.
Genome Announc ; 1(5)2013 Oct 24.
Artículo en Inglés | MEDLINE | ID: mdl-24158552

RESUMEN

Bordetella hinzii colonizes the respiratory tracts of poultry but can also infect immunocompromised humans. Bordetella trematum, however, only infects humans, causing ear and wound infections. Here, we present the first draft genome sequences of strains B. hinzii ATCC 51730 and B. trematum CCUG 13902.

14.
Vaccine ; 20(1-2): 235-41, 2001 Oct 12.
Artículo en Inglés | MEDLINE | ID: mdl-11567769

RESUMEN

BrkA is a Bvg-regulated Bordetella pertussis protein that mediates serum resistance and adherence. It shares sequence identity with another B. pertussis virulence factor called pertactin, and it is a member of the diverse group of proteins found in Gram-negative bacteria that are secreted by an autotransporter mechanism. Sera, either from individuals who have been vaccinated with acellular pertussis vaccines, or from individuals who have no re-collection of recent infection with B. pertussis fail to kill wild-type B. pertussis, but kill brkA mutant strains very well. We examined whether BrkA could be neutralised in serum fitting this profile. BrkA is synthesised as a 103kDa precursor that is processed into a surface-associated N-terminal 73kDa passenger domain, and an outer-membrane embedded C-terminal 30kDa transporter moiety. Polyclonal antibodies were raised to a recombinant, re-folded histidine-tagged fusion protein representing the 73kDa passenger region. These anti-BrkA antibodies were shown to boost the existing bactericidal capacity of human serum against B. pertussis by neutralising BrkA.


Asunto(s)
Anticuerpos Antibacterianos/inmunología , Antígenos Bacterianos/inmunología , Proteínas de la Membrana Bacteriana Externa/inmunología , Actividad Bactericida de la Sangre , Bordetella pertussis/inmunología , Adulto , Animales , Especificidad de Anticuerpos , Citotoxicidad Celular Dependiente de Anticuerpos , Antígenos Bacterianos/biosíntesis , Antígenos Bacterianos/química , Proteínas de la Membrana Bacteriana Externa/biosíntesis , Proteínas de la Membrana Bacteriana Externa/química , Proteínas de la Membrana Bacteriana Externa/fisiología , Humanos , Sueros Inmunes , Pruebas de Neutralización , Fragmentos de Péptidos/inmunología , Vacuna contra la Tos Ferina/inmunología , Precursores de Proteínas/inmunología , Precursores de Proteínas/metabolismo , Procesamiento Proteico-Postraduccional , Conejos , Proteínas Recombinantes de Fusión/inmunología , Organismos Libres de Patógenos Específicos
15.
J Mol Biol ; 312(1): 1-5, 2001 Sep 07.
Artículo en Inglés | MEDLINE | ID: mdl-11545580

RESUMEN

Horizontally transferred DNA is largely responsible for the dissemination of virulence traits amongst bacteria. Rapid identification of acquired DNA remains difficult as whole-genome sequencing of outbreak strains is impractical, and microarray-based approaches, while powerful, are limited to genes present only in the reference strains. Here we present a novel bacterial comparative genomic hybridization method that directly compares the genomes of related strains at sub-kilobase resolution in order to identify acquired DNA. Bacterial comparative genomic hybridization utilizes the concept of metaphase chromosome comparative genomic hybridization, and exploits the resolving power of two-dimensional DNA electrophoresis. Comparison of isogenic variants of the pathogen Pseudomonas aeruginosa detected a single-copy gene insertion responsible for gentamicin resistance.


Asunto(s)
Bacterias/genética , Transferencia de Gen Horizontal , Hibridación in Situ/métodos , ADN Bacteriano/química , Desoxirribonucleasas de Localización Especificada Tipo II/genética , Desoxirribonucleasas de Localización Especificada Tipo II/metabolismo , Electroforesis en Gel Bidimensional , Pseudomonas aeruginosa/genética , Mapeo Restrictivo
16.
J Bacteriol ; 181(18): 5838-42, 1999 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-10482528

RESUMEN

BrkA is a 103-kDa outer membrane protein of Bordetella pertussis that mediates resistance to antibody-dependent killing by complement. It is proteolytically processed into a 73-kDa N-terminal domain and a 30-kDa C-terminal domain as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. BrkA is also a member of the autotransporter family of proteins. Translocation of the N-terminal domain of the protein across the outer membrane is hypothesized to occur through a pore formed by the C-terminal domain. To test this hypothesis, we performed black lipid bilayer experiments with purified recombinant protein. The BrkA C-terminal protein showed an average single-channel conductance of 3.0 nS in 1 M KCl. This result strongly suggests that the C-terminal autotransporter domain of BrkA is indeed capable of forming a pore.


Asunto(s)
Proteínas de la Membrana Bacteriana Externa/química , Proteínas de la Membrana Bacteriana Externa/metabolismo , Bordetella pertussis/metabolismo , Membrana Dobles de Lípidos , Proteínas de la Membrana Bacteriana Externa/genética , Bordetella pertussis/genética , Clonación Molecular , Electroforesis en Gel de Poliacrilamida , Escherichia coli , Liposomas , Fragmentos de Péptidos/química , Fragmentos de Péptidos/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Mapeo Restrictivo , Especificidad de la Especie
17.
Infect Immun ; 67(3): 1424-31, 1999 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-10024590

RESUMEN

The Bordetella pertussis BrkA protein protects against the bactericidal activity of complement and antibody; however, some individuals mount an immune response that overcomes this bacterial defense. To further characterize this process, the bactericidal activities of sera from 13 adults with different modes of exposure to B. pertussis (infected as adults, occupational exposure, immunized with an acellular vaccine, or no identified exposure) against a wild-type strain and a BrkA complement-sensitive mutant were evaluated. All of the sera killed the BrkA mutant, suggesting past exposure to B. pertussis or cross-reactive organisms. Several samples had no or minimal activity against the wild type. All of the sera collected from the infected and occupationally exposed individuals but not all of the sera from vaccinated individuals had bactericidal activity against the wild-type strain, suggesting that some types of exposure can induce an immune response that can overcome the BrkA resistance mechanism. Adsorbing serum with the wild-type strain removed the bactericidal antibodies; however, adsorbing the serum with a lipopolysaccharide (LPS) mutant or an avirulent (bvg mutant) strain did not always result in loss of bactericidal activity, suggesting that antibodies to either LPS or bvg-regulated proteins could be bactericidal. All the samples, including those that lacked bactericidal activity, contained antibodies that recognized the LPS of B. pertussis. Bactericidal activity correlated best with the presence of the immunoglobulin G3 (IgG3) antibodies to LPS, the IgG subtype that is most effective at fixing complement.


Asunto(s)
Anticuerpos Antibacterianos/inmunología , Actividad Bactericida de la Sangre , Bordetella pertussis/inmunología , Adsorción , Adulto , Western Blotting , Ensayo de Inmunoadsorción Enzimática , Humanos , Inmunoglobulina G/sangre , Inmunoglobulina G/clasificación , Lipopolisacáridos/inmunología
18.
Infect Immun ; 66(8): 3978-80, 1998 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-9673291

RESUMEN

BrkA confers resistance to killing by complement in Bordetella pertussis. Complement resistance in Bordetella bronchiseptica was examined. Four B. bronchiseptica strains possessed the brkA gene; however, only three expressed the protein. Only the strain lacking BrkA was susceptible to complement. Introduction of the B. pertussis brkA gene restored BrkA expression to this strain but did not confer resistance. brkA was mutated in the strains that naturally expressed BrkA, and loss of BrkA did not confer sensitivity to complement. As a species, B. bronchiseptica is more resistant to complement than B. pertussis, and BrkA does not mediate resistance.


Asunto(s)
Proteínas de la Membrana Bacteriana Externa/inmunología , Bordetella bronchiseptica/inmunología , Animales , Anticuerpos Antibacterianos/inmunología , Proteínas de la Membrana Bacteriana Externa/biosíntesis , Proteínas del Sistema Complemento/inmunología , Cobayas , Humanos , Ratones , Conejos , Ratas
19.
FEMS Microbiol Lett ; 163(1): 57-63, 1998 Jun 01.
Artículo en Inglés | MEDLINE | ID: mdl-9631546

RESUMEN

Serum resistance, or resistance to killing by antibody dependent pathway of complement, in Bordetella pertussis is bvg-regulated and the Bordetella resistance to killing (brk) locus mediates much of the resistance. Here we examined whether other bvg-regulated proteins contribute to serum resistance. We found that neither pertussis toxin, adenylate cyclase toxin, filamentous hemagglutinin, dermonecrotic toxin, tracheal colonization factor, nor Vag8 mutants were sensitive to serum killing compared to the wild-type. Filamentous hemagglutinin has been reported to bind C4 binding protein, an inhibitor of complement, but this activity does not appear to contribute to serum resistance, as evidenced by the resistant phenotype of FHA mutants. Clinical isolates were serum resistant and wild-type strains possessing an additional copy of the brk locus were 2-5-fold more resistant to serum killing.


Asunto(s)
Proteínas de la Membrana Bacteriana Externa/fisiología , Proteínas Bacterianas/fisiología , Sangre , Bordetella pertussis/patogenicidad , Mutación/fisiología , Factores de Transcripción/fisiología , Toxina de Adenilato Ciclasa , Adhesinas Bacterianas/genética , Adhesinas Bacterianas/fisiología , Adulto , Proteínas de la Membrana Bacteriana Externa/genética , Proteínas Bacterianas/genética , Actividad Bactericida de la Sangre , Bordetella pertussis/genética , Vía Clásica del Complemento/fisiología , Hemaglutininas/genética , Hemaglutininas/fisiología , Humanos , Proteínas de la Membrana/genética , Proteínas de la Membrana/fisiología , Toxina del Pertussis , Factores de Transcripción/genética , Virulencia , Factores de Virulencia de Bordetella/genética , Tos Ferina/microbiología
20.
Infect Immun ; 64(6): 1968-76, 1996 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-8675295

RESUMEN

Legionella pneumophila 2064 was selectively radiolabelled in mouse L929 cells and human monocytes to identify proteins expressed early in the course of infection. Polypeptide profiles (sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography) of adherent or intracellular bacteria indicated that a 60-kDa stress protein (Hsp60) was preferentially synthesized. Hsp60 synthesis was not induced by medium alone. The synthesis of many polypeptides, including OmpS (major outer membrane protein), diminished over the 1-h period postinfection. However, by 17 h postinfection OmpS and Hsp60 were the dominant proteins synthesized by 2064. To establish whether induction of Hsp60 was a correlate of virulence, an isogenic avirulent strain (2064M) of 2064 was isolated following selection on a nonpermissive medium. 2064M did not exhibit a stress response when adherent or intracellular in L929 cells or in human monocytes and failed to abrogate phagosome-lysosome fusion. When grown in vitro, 2064M exhibited no deficiencies in the heat shock response and its polypeptide profile resembled that of 2064. Immunogold electron microscopy was used to localize Hsp60 in L. pneumophila-infected L929 cells. There was an increase in the number of gold particles associated with phagosomes for phagosomes harboring single 2064 bacteria compared with those harboring 2064M. Moreover, by 1 h postinfection, a sixfold increase in the number of gold spheres associated with the membranes of phagosomes was observed for phagosomes harboring 2064 compared with those harboring 2064M. These studies indicate that virulent, but not NaCl-tolerant avirulent, strains of L. pneumophila respond to host-cell-associated environmental signals early in the course of infection. This response includes increased synthesis and possibly extracellular secretion of Hsp60 concomitant with repression of the expression of other genes, including ompS.


Asunto(s)
Proteínas Bacterianas/biosíntesis , Chaperonina 60/biosíntesis , Legionella pneumophila/patogenicidad , Monocitos/metabolismo , Animales , Chaperonina 60/análisis , Calor , Humanos , Inmunohistoquímica , Ratones , Monocitos/microbiología , Virulencia
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