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1.
J Microbiol Biotechnol ; 30(11): 1760-1768, 2020 Nov 28.
Artículo en Inglés | MEDLINE | ID: mdl-32876069

RESUMEN

Vibrio cholerae, cause of the life-threatening diarrheal disease cholera, can be divided into different serogroups based on the structure of its lipopolysaccharide (LPS), which consists of lipid-A, corepolysaccharide and O-antigen polysaccharide (O-PS). The O1 serogroup, the predominant cause of cholera, includes two major serotypes, Inaba and Ogawa. These serotypes are differentiated by the presence of a single 2-O-methyl group in the upstream terminal perosamine of the Ogawa O-PS, which is absent in the Inaba O-PS. To ensure the consistent quality and efficacy of the current cholera vaccines, accurate measurement and characterization of each of these two serotypes is highly important. In this study, we efficiently screened a phage-displayed human synthetic Fab library by bio-panning against Ogawa LPS and finally selected three unique mAbs (D9, E11, and F7) that specifically react with Ogawa LPS. The mAbs bound to Vibrio cholerae vaccine in a dose-dependent fashion. Sequence and structure analyses of antibody paratopes suggest that IgG D9 might have the same fine specificity as that of the murine mAbs, which were shown to bind to the upstream terminal perosamine of Ogawa O-PS, whereas IgGs F7 and E11 showed some different characteristics in the paratopes. To our knowledge, this study is the first to demonstrate the generation of Ogawa-specific mAbs using phage display technology. The mAbs will be useful for identification and quantification of Ogawa LPS in multivalent V. cholerae vaccines.


Asunto(s)
Anticuerpos Antibacterianos/química , Anticuerpos Antibacterianos/inmunología , Anticuerpos Monoclonales/química , Anticuerpos Monoclonales/inmunología , Lipopolisacáridos/inmunología , Vibrio cholerae O1/inmunología , Animales , Vacunas Bacterianas/inmunología , Bacteriófagos/genética , Epítopos , Humanos , Lipopolisacáridos/química , Lipopolisacáridos/aislamiento & purificación , Ratones , Antígenos O/inmunología , Análisis de Secuencia , Serogrupo , Vibrio cholerae O1/genética
2.
Genome Announc ; 5(38)2017 Sep 21.
Artículo en Inglés | MEDLINE | ID: mdl-28935747

RESUMEN

Mycoplasma hyopneumoniae is the etiological agent of swine enzootic pneumonia, resulting in considerable economic losses in the swine industry. A few genome sequences of M. hyopneumoniae have been reported to date, implying that additional genome data are needed for further genetic studies. Here, we present the annotated genome sequence of M. hyopneumoniae strain KM014.

3.
Genome Announc ; 5(38)2017 Sep 21.
Artículo en Inglés | MEDLINE | ID: mdl-28935749

RESUMEN

Actinobacillus pleuropneumoniae is a bacterial pathogen causing highly contagious porcine pleuropneumonia. Due to limited information on this species, it is difficult to study the biology of A. pleuropneumoniae at the genome level. Here, we report the fully annotated genome sequence of A. pleuropneumoniae strain KL 16.

4.
Clin Sci (Lond) ; 130(2): 105-16, 2016 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-26519425

RESUMEN

Although apolipoprotein B100 (ApoB100) plays a key role in peripheral fat deposition, it is not considered a suitable therapeutic target in obesity. In the present study we describe a novel ApoB100 mimotope, peptide pB1, and the use of pB1-based vaccine-like formulations (BVFs) against high-fat diet (HFD)-induced obesity. In HFD- compared with chow-fed adolescent mice, BVFs reduced the 3-month body-weight gains attributable to increased dietary fat by 44-65%, and prevented mesenteric fat accumulation and liver steatosis. The body-weight reductions paralleled the titres of pB1-reactive immunoglobulin G (IgG) antibodies, and pB1-reactive antibodies specifically recognized native ApoB100 and a synthetic peptide from the C-terminal half of ApoB100. In cultured 3T3L1 adipocytes, anti-pB1 antibodies increased lipolysis and inhibited low-density lipoprotein (LDL) uptake. In cultured RAW 264.7 macrophages, the same antibodies enhanced LDL uptake (without causing foam cell formation). These findings make ApoB100 a promising target for an immunization strategy against HFD-induced obesity.


Asunto(s)
Fármacos Antiobesidad/uso terapéutico , Apolipoproteína B-100/efectos de los fármacos , Hipolipemiantes/farmacología , Obesidad/prevención & control , Péptidos/uso terapéutico , Animales , Fármacos Antiobesidad/inmunología , Formación de Anticuerpos/efectos de los fármacos , Apolipoproteína B-100/inmunología , Apolipoproteína B-100/fisiología , Dieta Alta en Grasa/efectos adversos , Epítopos/inmunología , Hígado Graso/prevención & control , Hipolipemiantes/inmunología , Lipólisis/efectos de los fármacos , Lipólisis/inmunología , Lipólisis/fisiología , Lipoproteínas LDL/metabolismo , Masculino , Ratones , Ratones Endogámicos BALB C , Ratones Endogámicos C57BL , Ratones Endogámicos ICR , Péptidos/inmunología , Ratas , Ratas Sprague-Dawley
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