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[PMID]:27771353
[Au] Autor:Peng W
[Ad] Endereço:Institute of Rheumatology and Immunology, Affiliated Hospital of North Sichuan Medical College, Nanchong City, Sichuan 637000, P. R. China; Laboratory of Experimental Surgery, Hadassah-Hebrew University Medical Center, Mount Scopus, Sderot Churchill, Jerusalem, 91240, Israel. Electronic address: pengwei39@hotmail.com.
[Ti] Título:G-CSF treatment promotes apoptosis of autoreactive T cells to restrict the inflammatory cascade and accelerate recovery in experimental allergic encephalomyelitis.
[So] Source:Exp Neurol;289:73-84, 2017 03.
[Is] ISSN:1090-2430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:G-CSF is a hematopoietic growth factor that regulates the proliferation, differentiation and survival of myeloid lineage cells, which has protective effects in autoimmune neuroinflammatory diseases such as EAE. Here we use EAE model treated by G-CSF to address the hypothesis that G-CSF inhibits the proliferative response of splenic T cells via the enhancement of apoptosis, and this priming effect of G-CSF depends on the cell cycle. Our results show that G-CSF administration reduced EAE frequency and severity of attacks. The inflammatory cells and demyelination areas were decreased in the CNS of G-CSF-treated mice. G-CSF treatment altered cytokine profiles in vivo to inhibit the productions of IFN-γ, IL-1ß, IL-2, TNF-α, IL-17 and NO, while the secretions of IL-4 and IL-10 were increased. Splenic T cells from G-CSF-treated mice showed significantly lower proliferative response to specific antigen MOG stimulation. G-CSF enhanced the percentage of a CD4 CD25 T cell subset in spleen T cells. Moreover, G-CSF promoted the G0/G1 to S phase transition of MOG autoreactive T cells inducing apoptosis and elevating Bax gene expression of apoptosis marker. These findings indicate that G-CSF treatment induces the apoptosis of MOG autoreactive T cells, which decreases the production of pro-inflammatory cytokines and NO, suppresses the proliferation of autoreactive T cells and elevates a CD4 CD25 T cell subset to inhibit inflammatory infiltration and demyelination within CNS of EAE. The conclusions of G-CSF treatment in EAE mice suggest that G-CSF is clinically applicable and may be considered for future use in therapeutic measures for multiple sclerosis treatment.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Linfócitos T CD4-Positivos/efeitos dos fármacos
Encefalomielite Autoimune Experimental/tratamento farmacológico
Encefalomielite Autoimune Experimental/fisiopatologia
Fator Estimulador de Colônias de Granulócitos/uso terapêutico
Recuperação de Função Fisiológica/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Anexina A5/metabolismo
Ciclo Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Citocinas/metabolismo
Modelos Animais de Doenças
Encefalomielite Autoimune Experimental/induzido quimicamente
Feminino
Adjuvante de Freund/toxicidade
Expressão Gênica/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Glicoproteína Mielina-Oligodendrócito/toxicidade
Óxido Nítrico/metabolismo
Fragmentos de Peptídeos/toxicidade
Toxina Pertussis/toxicidade
Baço/patologia
Proteína X Associada a bcl-2/genética
Proteína X Associada a bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A5); 0 (Cytokines); 0 (Myelin-Oligodendrocyte Glycoprotein); 0 (Peptide Fragments); 0 (bcl-2-Associated X Protein); 0 (myelin oligodendrocyte glycoprotein (35-55)); 143011-72-7 (Granulocyte Colony-Stimulating Factor); 31C4KY9ESH (Nitric Oxide); 9007-81-2 (Freund's Adjuvant); EC 2.4.2.31 (Pertussis Toxin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:180218
[Lr] Data última revisão:
180218
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:28945785
[Au] Autor:Doijen J; Van Loy T; De Haes W; Landuyt B; Luyten W; Schoofs L; Schols D
[Ad] Endereço:Laboratory of Functional genomics & proteomics, Zoological Institute, KU Leuven, Belgium.
[Ti] Título:Signaling properties of the human chemokine receptors CXCR4 and CXCR7 by cellular electric impedance measurements.
[So] Source:PLoS One;12(9):e0185354, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The chemokine receptor 4 (CXCR4) and 7 (CXCR7) are G-protein-coupled receptors involved in various diseases including human cancer. As such, they have become important targets for therapeutic intervention. Cell-based receptor assays, able to detect agents that modulate receptor activity, are of key importance for drug discovery. We evaluated the potential of cellular electric impedance for this purpose. Dose-dependent and specific stimulation of CXCR4 was detected upon addition of its unique chemokine ligand CXCL12. The response magnitude correlated with the CXCR4 expression level. Gαi coupling and signaling contributed extensively to the impedance response, whereas Gαq- and Gßγ-related events had only minor effects on the impedance profile. CXCR7 signaling could not be detected using impedance measurements. However, increasing levels of CXCR7 expression significantly reduced the CXCR4-mediated impedance readout, suggesting a regulatory role for CXCR7 on CXCR4-mediated signaling. Taken together, cellular electric impedance spectroscopy can represent a valuable alternative pharmacological cell-based assay for the identification of molecules targeting CXCR4, but not for CXCR7 in the absence of CXCR4.
[Mh] Termos MeSH primário: Receptores CXCR4/metabolismo
Receptores CXCR/metabolismo
[Mh] Termos MeSH secundário: Sinalização do Cálcio
Linhagem Celular Tumoral
Quimiocina CXCL12/genética
Quimiocina CXCL12/metabolismo
Impedância Elétrica
Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/metabolismo
Células HT29
Seres Humanos
Ligantes
Toxina Pertussis/toxicidade
Receptores CXCR/genética
Receptores CXCR4/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CXCL12 protein, human); 0 (CXCR4 protein, human); 0 (CXCR7 protein, human); 0 (Chemokine CXCL12); 0 (Ligands); 0 (Receptors, CXCR); 0 (Receptors, CXCR4); 0 (Recombinant Proteins); EC 2.4.2.31 (Pertussis Toxin); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gi-Go)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185354


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[PMID]:28887436
[Au] Autor:Chen C; Barbieri JT
[Ad] Endereço:From the Department of Microbiology and Immunology, Medical College of Wisconsin, Milwaukee, Wisconsin 53226.
[Ti] Título:When doesn't fit the mold: A pertussis-like toxin with altered specificity.
[So] Source:J Biol Chem;292(36):15159-15160, 2017 Sep 08.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacterial toxins introduce protein modifications such as ADP-ribosylation to manipulate host cell signaling and physiology. Several general mechanisms for toxin function have been established, but the extent to which previously uncharacterized toxins utilize these mechanisms is unknown. A study of an pertussis-like toxin demonstrates that this protein acts on a known toxin substrate but displays distinct and dual chemoselectivity, suggesting this pertussis-like toxin may serve as a unique tool to study G-protein signaling in eukaryotic cells.
[Mh] Termos MeSH primário: Toxinas Bacterianas/química
Toxinas Bacterianas/farmacologia
Escherichia coli/química
Proteínas Heterotriméricas de Ligação ao GTP/antagonistas & inibidores
Toxina Pertussis/química
[Mh] Termos MeSH secundário: Animais
Células Eucarióticas/efeitos dos fármacos
Células Eucarióticas/metabolismo
Proteínas Heterotriméricas de Ligação ao GTP/metabolismo
Seres Humanos
Modelos Moleculares
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Toxins); EC 2.4.2.31 (Pertussis Toxin); EC 3.6.5.1 (Heterotrimeric GTP-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170910
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.H117.796094


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[PMID]:28855310
[Au] Autor:Zaid A; Hor JL; Christo SN; Groom JR; Heath WR; Mackay LK; Mueller SN
[Ad] Endereço:Department of Microbiology and Immunology, The University of Melbourne, at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria 3000 Australia.
[Ti] Título:Chemokine Receptor-Dependent Control of Skin Tissue-Resident Memory T Cell Formation.
[So] Source:J Immunol;199(7):2451-2459, 2017 Oct 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Infection or inflammation of the skin recruits effector CD8 T cells that enter the epidermis and form populations of long-lived tissue-resident memory T (T ) cells. These skin T cells migrate within the constrained epidermal environment by extending multiple dynamic dendritic projections and squeezing between keratinocytes to survey the tissue for pathogens. In this study, we examined the signals required for this distinctive mode of T cell migration by inhibiting key cytoskeletal components and performing intravital two-photon microscopy to visualize T cell behavior. We found that T cell motility and dendrite formation required an intact actomyosin cytoskeleton and the Rho-associated coiled-coil containing kinases. We also identified an essential role for microtubules for maintaining skin T cell shape and cellular integrity. We reveal a role for pertussis toxin-sensitive signaling for T cell dendritic morphology and migration that is independent of CXCR3 or CXCR6, or the skin-selective chemokine receptors CCR10 and CCR8. However, we found that CXCR6 and CCR10 expression by CD8 T cells was required for the optimal formation of memory T cell populations, in particular T cell populations in the skin.
[Mh] Termos MeSH primário: Linfócitos T CD8-Positivos/fisiologia
Movimento Celular
Epiderme/imunologia
Memória Imunológica
Receptores de Quimiocinas/metabolismo
Pele/imunologia
[Mh] Termos MeSH secundário: Actomiosina/metabolismo
Animais
Linfócitos T CD8-Positivos/imunologia
Células Dendríticas/fisiologia
Epiderme/citologia
Microscopia Intravital/métodos
Camundongos
Microtúbulos/metabolismo
Toxina Pertussis/metabolismo
Receptores CCR10/genética
Receptores CCR10/metabolismo
Receptores CCR8/metabolismo
Receptores CXCR/genética
Receptores CXCR/metabolismo
Receptores CXCR3/metabolismo
Receptores CXCR6
Receptores de Quimiocinas/genética
Transdução de Sinais
Pele/anatomia & histologia
Pele/citologia
Quinases Associadas a rho/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ccr10 protein, mouse); 0 (Cxcr6 protein, mouse); 0 (Receptors, CCR10); 0 (Receptors, CCR8); 0 (Receptors, CXCR); 0 (Receptors, CXCR3); 0 (Receptors, CXCR6); 0 (Receptors, Chemokine); 9013-26-7 (Actomyosin); EC 2.4.2.31 (Pertussis Toxin); EC 2.7.11.1 (rho-Associated Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700571


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[PMID]:28784932
[Au] Autor:Scanlon KM; Snyder YG; Skerry C; Carbonetti NH
[Ad] Endereço:Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
[Ti] Título:Fatal Pertussis in the Neonatal Mouse Model Is Associated with Pertussis Toxin-Mediated Pathology beyond the Airways.
[So] Source:Infect Immun;85(11), 2017 Nov.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In infants, can cause severe disease, manifested as pronounced leukocytosis, pulmonary hypertension, and even death. The exact cause of death remains unknown, and no effective therapies for treating fulminant pertussis exist. In this study, a neonatal mouse model of critical pertussis is characterized, and a central role for pertussis toxin (PT) is described. PT promoted colonization, leukocytosis, T cell phenotypic changes, systemic pathology, and death in neonatal but not adult mice. Surprisingly, PT inhibited lung inflammatory pathology in neonates, a result which contrasts dramatically with observed PT-promoted pathology in adult mice. Infection with a PT-deficient strain induced severe pulmonary inflammation but not mortality in neonatal mice, suggesting that death in these mice was not associated with impaired lung function. Dissemination of infection beyond the lungs was also detected in neonatal mice, which may contribute to the observed systemic effects of PT. We propose that it is the systemic activity of pertussis toxin and not pulmonary pathology that promotes mortality in critical pertussis. In addition, we observed transmission of infection between neonatal mice, the first report of transmission in mice. This model will be a valuable tool to investigate causes of pertussis pathogenesis and identify potential therapies for critical pertussis.
[Mh] Termos MeSH primário: Bordetella pertussis/patogenicidade
Interações Hospedeiro-Patógeno
Leucocitose/microbiologia
Pulmão/microbiologia
Toxina Pertussis/toxicidade
Coqueluche/microbiologia
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Animais Recém-Nascidos
Bordetella pertussis/crescimento & desenvolvimento
Bordetella pertussis/imunologia
Modelos Animais de Doenças
Seres Humanos
Lactente
Leucocitose/imunologia
Leucocitose/mortalidade
Leucocitose/patologia
Pulmão/imunologia
Pulmão/patologia
Camundongos
Camundongos Endogâmicos BALB C
Neutrófilos/imunologia
Neutrófilos/microbiologia
Neutrófilos/patologia
Toxina Pertussis/biossíntese
Toxina Pertussis/imunologia
Análise de Sobrevida
Linfócitos T/imunologia
Linfócitos T/microbiologia
Linfócitos T/patologia
Coqueluche/imunologia
Coqueluche/mortalidade
Coqueluche/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.4.2.31 (Pertussis Toxin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE


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[PMID]:28700751
[Au] Autor:Moriuchi T; Otsuka N; Hiramatsu Y; Shibayama K; Kamachi K
[Ad] Endereço:Department of Bacteriology II, National Institute of Infectious Diseases, Tokyo, Japan.
[Ti] Título:A high seroprevalence of antibodies to pertussis toxin among Japanese adults: Qualitative and quantitative analyses.
[So] Source:PLoS One;12(7):e0181181, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In 2013, national serosurveillance detected a high seroprevalence of antibodies to pertussis toxin (PT) from Bordetella pertussis among Japanese adults. Thus, we aimed to determine the cause(s) of this high seroprevalence, and analyzed the titers of antibodies to PT and filamentous hemagglutinin (FHA) among adults (35-44 years old), young children (4-7 years old), and older children (10-14 years old). Our quantitative analyses revealed that adults had higher seroprevalences of anti-PT IgG and PT-neutralizing antibodies, and similar titers of anti-FHA IgG, compared to the young and older children. Positive correlations were observed between the titers of PT-neutralizing antibodies and anti-PT IgG in all age groups (rs values of 0.326-0.522), although the correlation tended to decrease with age. The ratio of PT-neutralizing antibodies to anti-PT IgG was significantly different when we compared the serum and purified IgG fractions among adults (p = 0.016), although this result was not observed among young and older children. Thus, it appears that some adults had non-IgG immunoglobulins to PT. Our analyses also revealed that adults had high-avidity anti-PT IgG (avidity index: 63.5%, similar results were observed among the children); however, the adults had lower-avidity anti-FHA IgG (37.9%, p < 0.05). It is possible that low-avidity anti-FHA IgG is related to infection with other respiratory pathogens (e.g., Bordetella parapertussis, Haemophilus influenzae, or Mycoplasma pneumoniae), which produces antibodies to FHA-like proteins. Our observations suggest that these adults had been infected with B. pertussis and other pathogen(s) during their adulthood.
[Mh] Termos MeSH primário: Adesinas Bacterianas/imunologia
Anticorpos Antibacterianos/imunologia
Toxina Pertussis/imunologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Bordetella parapertussis/imunologia
Criança
Pré-Escolar
Feminino
Haemophilus influenzae/imunologia
Seres Humanos
Imunoglobulinas/imunologia
Masculino
Mycoplasma pneumoniae/imunologia
Estudos Soroepidemiológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Antibodies, Bacterial); 0 (Immunoglobulins); EC 2.4.2.31 (Pertussis Toxin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181181


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[PMID]:28663369
[Au] Autor:Littler DR; Ang SY; Moriel DG; Kocan M; Kleifeld O; Johnson MD; Tran MT; Paton AW; Paton JC; Summers RJ; Schembri MA; Rossjohn J; Beddoe T
[Ad] Endereço:From the Infection and Immunity Program and Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria 3800, Australia.
[Ti] Título:Structure-function analyses of a pertussis-like toxin from pathogenic reveal a distinct mechanism of inhibition of trimeric G-proteins.
[So] Source:J Biol Chem;292(36):15143-15158, 2017 Sep 08.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pertussis-like toxins are secreted by several bacterial pathogens during infection. They belong to the AB virulence factors, which bind to glycans on host cell membranes for internalization. Host cell recognition and internalization are mediated by toxin B subunits sharing a unique pentameric ring-like assembly. Although the role of pertussis toxin in whooping cough is well-established, pertussis-like toxins produced by other bacteria are less studied, and their mechanisms of action are unclear. Here, we report that some extra-intestinal pathogens ( those that reside in the gut but can spread to other bodily locations) encode a pertussis-like toxin that inhibits mammalian cell growth We found that this protein, Plt, is related to toxins produced by both nontyphoidal and typhoidal serovars. Pertussis-like toxins are secreted as disulfide-bonded heterohexamers in which the catalytic ADP-ribosyltransferase subunit is activated when exposed to the reducing environment in mammalian cells. We found here that the reduced Plt exhibits large structural rearrangements associated with its activation. We noted that inhibitory residues tethered within the NAD -binding site by an intramolecular disulfide in the oxidized state dissociate upon the reduction and enable loop restructuring to form the nucleotide-binding site. Surprisingly, although pertussis toxin targets a cysteine residue within the α subunit of inhibitory trimeric G-proteins, we observed that activated Plt toxin modifies a proximal lysine/asparagine residue instead. In conclusion, our results reveal the molecular mechanism underpinning activation of pertussis-like toxins, and we also identified differences in host target specificity.
[Mh] Termos MeSH primário: Toxinas Bacterianas/química
Toxinas Bacterianas/farmacologia
Escherichia coli/química
Proteínas Heterotriméricas de Ligação ao GTP/antagonistas & inibidores
Toxina Pertussis/química
[Mh] Termos MeSH secundário: Animais
Proliferação Celular/efeitos dos fármacos
Cercopithecus aethiops
Relação Dose-Resposta a Droga
Células Epiteliais/efeitos dos fármacos
Células HEK293
Proteínas Heterotriméricas de Ligação ao GTP/metabolismo
Seres Humanos
Modelos Moleculares
Relação Estrutura-Atividade
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Toxins); EC 2.4.2.31 (Pertussis Toxin); EC 3.6.5.1 (Heterotrimeric GTP-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.796094


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[PMID]:28407060
[Au] Autor:Millard SM; Wang L; Wattanachanya L; O'Carroll D; Fields AJ; Pang J; Kazakia G; Lotz JC; Nissenson RA
[Ad] Endereço:Endocrine Research Unit, VA Medical Center, San Francisco, California 94158.
[Ti] Título:Role of Osteoblast Gi Signaling in Age-Related Bone Loss in Female Mice.
[So] Source:Endocrinology;158(6):1715-1726, 2017 Jun 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Age-related bone loss is an important risk factor for fractures in the elderly; it results from an imbalance in bone remodeling mainly due to decreased bone formation. We have previously demonstrated that endogenous G protein-coupled receptor (GPCR)-driven Gi signaling in osteoblasts (Obs) restrains bone formation in mice during growth. Here, we launched a longitudinal study to test the hypothesis that Gi signaling in Obs restrains bone formation in aging mice, thereby promoting bone loss. Our approach was to block Gi signaling in maturing Obs by the induced expression of the catalytic subunit of pertussis toxin (PTX) after the achievement of peak bone mass. In contrast to the progressive cancellous bone loss seen in aging sex-matched littermate control mice, aging female Col1(2.3)+/PTX+ mice showed an age-related increase in bone volume. Increased bone volume was associated with increased bone formation at both trabecular and endocortical surfaces as well as increased bending strength of the femoral middiaphyses. In contrast, male Col1(2.3)+/PTX+ mice were not protected from age-related bone loss. Our results indicate that Gi signaling markedly restrains bone formation at cancellous and endosteal bone surfaces in female mice during aging. Blockade of the relevant Gi-coupled GPCRs represents an approach for the development of osteoporosis therapies-at least in the long bones of aging women.
[Mh] Termos MeSH primário: Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/fisiologia
Osteoblastos/metabolismo
Osteoporose/genética
[Mh] Termos MeSH secundário: Animais
Densidade Óssea/efeitos dos fármacos
Densidade Óssea/genética
Remodelação Óssea/efeitos dos fármacos
Remodelação Óssea/genética
Colágeno Tipo I/genética
Feminino
Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/metabolismo
Masculino
Camundongos
Camundongos Transgênicos
Osteogênese/efeitos dos fármacos
Osteogênese/genética
Osteoporose/metabolismo
Osteoporose/patologia
Toxina Pertussis/genética
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type I); 0 (collagen type I, alpha 1 chain); EC 2.4.2.31 (Pertussis Toxin); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gi-Go)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1210/en.2016-1365


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[PMID]:28394915
[Au] Autor:Gates I; DuVall M; Ju H; Tondella ML; Pawloski L; Pertussis Working Group
[Ad] Endereço:Division of Bacterial Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia, United States of America.
[Ti] Título:Development of a qualitative assay for screening of Bordetella pertussis isolates for pertussis toxin production.
[So] Source:PLoS One;12(4):e0175326, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bordetella pertussis infection has been increasing in the US, with reported cases reaching over 50,000 in 2012, a number last observed in the 1950s. Concurrently, B. pertussis lacking the pertactin protein, one of the immunogens included in the acellular vaccine formulations, has rapidly emerged since 2010, and has become the predominant circulating phenotype. Monitoring the production of the remaining acellular vaccine immunogens, such as pertussis toxin (Pt), is a critical next step. To date, methods for screening Pt have been either through genomic sequencing means or by conventional ELISAs. However, sequencing limits detection to the DNA level, missing potential disruptions in transcription or translation. Conventional ELISAs are beneficial for detecting the protein; however, they can often suffer from poor sensitivity and specificity. Here we describe a rapid, highly sensitive and specific electrochemiluminescent capture ELISA that can detect Pt production in prepared inactivated bacterial suspensions. Over 340 isolates were analyzed and analytical validation parameters, such as precision, reproducibility, and stability, were rigorously tested. Intra-plate and inter-plate variability measured at 9.8% and 11.5%, respectively. Refrigerated samples remained stable for two months and variability was unaffected (coefficient of variation was 12%). Interestingly, despite the intention of being a qualitative method, the assay was sensitive enough to detect a small, but statistically significant, difference in protein production between different pertussis promoter allelic groups of strains, ptxP1 and ptxP3. This technology has the ability to perform screening of multiple antigens at one time, thus, improving testing characteristics while minimizing costs, specimen volume, and testing time.
[Mh] Termos MeSH primário: Bordetella pertussis/isolamento & purificação
Bordetella pertussis/metabolismo
Técnicas Eletroquímicas
Ensaio de Imunoadsorção Enzimática/métodos
Toxina Pertussis/metabolismo
Coqueluche/diagnóstico
[Mh] Termos MeSH secundário: Análise de Variância
Congelamento
Seres Humanos
Medições Luminescentes
Refrigeração
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
Manejo de Espécimes
Coqueluche/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
EC 2.4.2.31 (Pertussis Toxin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175326


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[PMID]:28376777
[Au] Autor:Kwon HJ; Han SB; Kim BR; Kang KR; Huh DH; Choi GS; Ahn DH; Kang JH
[Ad] Endereço:Department of Pediatrics, Seoul St. Mary's Hospital, College of Medicine, The Catholic University of Korea, 222 Banpo-daero, Seocho-gu, Seoul, 06591, Republic of Korea.
[Ti] Título:Assessment of safety and efficacy against Bordetella pertussis of a new tetanus-reduced dose diphtheria-acellular pertussis vaccine in a murine model.
[So] Source:BMC Infect Dis;17(1):247, 2017 Apr 04.
[Is] ISSN:1471-2334
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Tetanus-reduced dose diphtheria-acellular pertussis (Tdap) vaccination during adolescence was introduced in response to the resurgence of pertussis in various countries. A new Tdap vaccine was manufactured in Korea as a countermeasure against a predicted Tdap vaccine shortage. This study was performed to evaluate the immunogenicity, safety, and protection efficacy against Bordetella pertussis of the new Tdap vaccine in a murine model. METHODS: Four-week-old BABL/c mice were used for assessment of immunogenicity and protection efficacy. A single dose of primary diphtheria-tetanus-acellular pertussis (DTaP) vaccine was administered, followed by a single dose of Tdap booster vaccine after a 12-week interval. Anti-pertussis toxin (PT), anti-filamentous hemagglutinin (FHA), and anti-pertactin (PRN) IgG titers were measured before primary vaccination, and before and after booster vaccination. An intranasal challenge test was performed after booster vaccination to determine protection efficacy. To assess safety, mouse weight gain test and leukocytosis promotion test were performed using 4-week-old ddY female mice. RESULTS: Anti-PT and anti-FHA IgG titers after booster vaccination were significantly higher than those before booster vaccination with either the new vaccine or a commercially available Tdap vaccine (P = 0.01 for all occasions). After booster vaccination, no significant difference was observed between the two vaccines in antibody titers against pertussis antigens (P = 0.53 for anti-PT IgG, P = 0.91 for anti-FHA IgG, P = 0.39 for anti-PRN IgG). In the intranasal challenge test, inoculated B. pertussis was eradicated 7 days after infection. On days 4 and 7 after infection, colony counts of B. pertussis were not significantly different between the new and positive control vaccine groups (P = 1.00). Mean body weight changes and leukocyte counts of the new vaccine, positive control, and negative control groups were not significantly different 7 days after vaccination (P = 0.87 and P = 0.37, respectively). All leukocyte counts in the new vaccine group were within a mean ± 3 standard deviations range. CONCLUSIONS: A murine model involving a single dose primary DTaP vaccination followed by a single dose Tdap booster vaccination can be used for non-clinical studies of Tdap vaccines. The new Tdap vaccine manufactured in Korea exhibited comparable immunogenicity, protection efficacy, and safety with a commercially available Tdap vaccine.
[Mh] Termos MeSH primário: Bordetella pertussis/imunologia
Vacinas contra Difteria, Tétano e Coqueluche Acelular/imunologia
Coqueluche/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Anticorpos Anti-Idiotípicos
Anticorpos Antibacterianos
Antígenos de Bactérias/imunologia
Proteínas da Membrana Bacteriana Externa/imunologia
Vacinas contra Difteria, Tétano e Coqueluche Acelular/administração & dosagem
Vacinas contra Difteria, Tétano e Coqueluche Acelular/efeitos adversos
Relação Dose-Resposta Imunológica
Feminino
Hemaglutininas
Seres Humanos
Imunização Secundária
Imunogenicidade da Vacina
Camundongos
Camundongos Endogâmicos C57BL
Toxina Pertussis
República da Coreia
Fatores de Virulência de Bordetella/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Anti-Idiotypic); 0 (Antibodies, Bacterial); 0 (Antigens, Bacterial); 0 (Bacterial Outer Membrane Proteins); 0 (Diphtheria-Tetanus-acellular Pertussis Vaccines); 0 (Hemagglutinins); 0 (Virulence Factors, Bordetella); 0 (anti-IgG); 0 (pertactin); EC 2.4.2.31 (Pertussis Toxin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170628
[Lr] Data última revisão:
170628
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1186/s12879-017-2369-x



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