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Pesquisa : D12.776.395.550.200.123 [Categoria DeCS]
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  1 / 478 MEDLINE  
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[PMID]:28800489
[Au] Autor:Lin Y; Racaniello VR
[Ad] Endereço:Department of Microbiology&Immunology, Columbia University College of Physicians&Surgeons, 701W. 168th St., New York, NY 10032, USA.
[Ti] Título:Polioviruses that bind a chimeric Pvr-nectin-2 protein identify capsid residues involved in receptor interaction.
[So] Source:Virology;510:305-315, 2017 Oct.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amino acid changes in the C'C"D region in poliovirus receptor domain 1 disrupt poliovirus binding. To examine further the role of the C'C"D region in poliovirus infection, we substituted this region of Pvr into the corresponding region of a murine homolog, nectin-2. The chimeric receptor, nectin-2 , rendered transformed L cells susceptible to infection with poliovirus P1/Mahoney, but not with polioviruses P2/Lansing and P3/Leon, due to lack of binding. Twenty-four variants of P2/Lansing were selected that replicate in nectin-2 producing cell lines. Sequence analysis revealed 30 amino acid changes at 28 capsid residues. One change, K1103R, is found in nearly all isolates and is located at one end of the VP1 BC loop. Other alterations are located on the canyon surface, at the protomer interface, and along the perimeter of the canyon south wall. Unlike poliovirus-Pvr binding, the VP1 BC loop is required for infection of cells producing nectin-2 .
[Mh] Termos MeSH primário: Capsídeo/metabolismo
Moléculas de Adesão Celular/metabolismo
Poliovirus/fisiologia
Receptores Virais/metabolismo
Proteínas Recombinantes de Fusão/metabolismo
Ligação Viral
[Mh] Termos MeSH secundário: Animais
Moléculas de Adesão Celular/genética
Linhagem Celular
Análise Mutacional de DNA
Seres Humanos
Camundongos
Nectinas
Receptores Virais/genética
Proteínas Recombinantes de Fusão/genética
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Nectins); 0 (Receptors, Virus); 0 (Recombinant Fusion Proteins); 0 (poliovirus receptor)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE


  2 / 478 MEDLINE  
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[PMID]:28671524
[Au] Autor:Fujimoto Y; Tomioka Y; Ozaki K; Takeda K; Suyama H; Yamamoto S; Takakuwa H; Morimatsu M; Uede T; Ono E
[Ad] Endereço:1​Department of Biomedicine, Center of Biomedical Research, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan 2​Center of Biomedical Research, Research Center for Human Disease Modeling, Graduate School of Medical Sciences, Kyushu Univers
[Ti] Título:Comparison of the antiviral potential among soluble forms of herpes simplex virus type-2 glycoprotein D receptors, herpes virus entry mediator A, nectin-1 and nectin-2, in transgenic mice.
[So] Source:J Gen Virol;98(7):1815-1822, 2017 Jul.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Herpesvirus entry mediator A (HVEM), nectin-1 and nectin-2 are cellular receptors of glycoprotein D (gD) of herpes simplex virus type-2 (HSV-2). It has been shown that soluble forms of HSV gD receptors have the antiviral potential in cultured cells and transgenic mice. Here, to compare antiviral potential of soluble forms of HVEM, nectin-1 and nectin-2 against HSV-2 infections in vivo, transgenic mice expressing fusion proteins consisting of the entire ectodomain of HVEM, nectin-1 or nectin-2 and the Fc portion of human IgG (HVEMIg, nectin-1Ig and nectin-2Ig, respectively) were intraperitoneally infected with HSV-2. In the infection with 3 MLD50 (50 % mouse lethal dose), effective resistance was not observed in transgenic mice expressing nectin-2Ig. In a transgenic mouse line with high expression of nectin-1Ig, significant protection from the infection with 30 and 300 MLD50 was observed (survival rate of 100 and 71 %, respectively). On the other hand, transgenic mice expressing HVEMIg showed a complete resistance to the lethal infection even with 300 MLD50 (survival rate of 100 %). These results demonstrated that HVEMIg could exert effective antiviral activities against HSV-2 infections in vivo as compared with other soluble forms of HSV gD receptors.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/imunologia
Herpes Simples/imunologia
Herpesvirus Humano 2/metabolismo
Membro 14 de Receptores do Fator de Necrose Tumoral/imunologia
Receptores Virais/imunologia
Proteínas do Envelope Viral/metabolismo
[Mh] Termos MeSH secundário: Animais
Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/metabolismo
Herpes Simples/genética
Herpes Simples/metabolismo
Herpes Simples/virologia
Herpesvirus Humano 2/genética
Herpesvirus Humano 2/imunologia
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Nectinas
Membro 14 de Receptores do Fator de Necrose Tumoral/genética
Membro 14 de Receptores do Fator de Necrose Tumoral/metabolismo
Receptores Virais/genética
Receptores Virais/metabolismo
Proteínas do Envelope Viral/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (NECTIN1 protein, human); 0 (Nectin1 protein, mouse); 0 (Nectins); 0 (Receptors, Tumor Necrosis Factor, Member 14); 0 (Receptors, Virus); 0 (Viral Envelope Proteins); 0 (glycoprotein D-herpes simplex virus type 2)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000804


  3 / 478 MEDLINE  
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[PMID]:28515320
[Au] Autor:Deuss FA; Gully BS; Rossjohn J; Berry R
[Ad] Endereço:From the Infection and Immunity Program, Biomedicine Discovery Institute and.
[Ti] Título:Recognition of nectin-2 by the natural killer cell receptor T cell immunoglobulin and ITIM domain (TIGIT).
[So] Source:J Biol Chem;292(27):11413-11422, 2017 Jul 07.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:T cell immunoglobulin and ITIM domain (TIGIT) is an inhibitory receptor expressed on the surface of natural killer (NK) cells. TIGIT recognizes nectin and nectin-like adhesion molecules and thus plays a critical role in the innate immune response to malignant transformation. Although the TIGIT nectin-like protein-5 (necl-5) interaction is well understood, how TIGIT engages nectin-2, a receptor that is broadly over-expressed in breast and ovarian cancer, remains unknown. Here, we show that TIGIT bound to the immunoglobulin domain of nectin-2 that is most distal from the membrane with an affinity of 6 µm, which was moderately lower than the affinity observed for the TIGIT/necl-5 interaction (3.2 µm). The TIGIT/nectin-2 binding disrupted pre-assembled nectin-2 oligomers, suggesting that receptor-ligand and ligand-ligand associations are mutually exclusive events. Indeed, the crystal structure of TIGIT bound to the first immunoglobulin domain of nectin-2 indicated that the receptor and ligand dock using the same molecular surface and a conserved "lock and key" binding motifs previously observed to mediate nectin/nectin homotypic interactions as well as TIGIT/necl-5 recognition. Using a mutagenesis approach, we dissected the energetic basis for the TIGIT/nectin-2 interaction and revealed that an "aromatic key" of nectin-2 is critical for this interaction, whereas variations in the lock were tolerated. Moreover, we found that the C-C' loop of the ligand dictates the TIGIT binding hierarchy. Altogether, these findings broaden our understanding of nectin/nectin receptor interactions and have implications for better understanding the molecular basis for autoimmune disease and cancer.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/química
Receptores Imunológicos/química
[Mh] Termos MeSH secundário: Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/metabolismo
Cristalografia por Raios X
Seres Humanos
Mutagênese
Nectinas
Domínios Proteicos
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Receptores Imunológicos/genética
Receptores Imunológicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Nectins); 0 (Receptors, Immunologic); 0 (TIGIT protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.786483


  4 / 478 MEDLINE  
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[PMID]:28423057
[Au] Autor:Petrovic B; Gianni T; Gatta V; Campadelli-Fiume G
[Ad] Endereço:Department of Experimental, Diagnostic and Specialty Medicine, University of Bologna, via S. Giacomo 12, Bologna, Italy.
[Ti] Título:Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.
[So] Source:PLoS Pathog;13(4):e1006352, 2017 Apr.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Herpes simplex virus (HSV) entry into the cells requires glycoproteins gD, gH/gL and gB, activated in a cascade fashion by conformational modifications induced by cognate receptors and intermolecular signaling. The receptors are nectin1 and HVEM (Herpes virus entry mediator) for gD, and αvß6 or αvß8 integrin for gH. In earlier work, insertion of a single chain antibody (scFv) to the cancer receptor HER2 (human epidermal growth factor receptor 2) in gD, or in gH, resulted in HSVs specifically retargeted to the HER2-positive cancer cells, hence in highly specific non-attenuated oncolytic agents. Here, the scFv to HER2 was inserted in gB (gBHER2). The insertion re-targeted the virus tropism to the HER2-positive cancer cells. This was unexpected since gB is known to be a fusogenic glycoprotein, not a tropism determinant. The gB-retargeted recombinant offered the possibility to investigate how HER2 mediated entry. In contrast to wt-gB, the activation of the chimeric gBHER2 did not require the activation of the gD and of gH/gL by their respective receptors. Furthermore, a soluble form of HER2 could replace the membrane-bound HER2 in mediating virus entry, hinting that HER2 acted by inducing conformational changes to the chimeric gB. This study shows that (i) gB can be modified and become the major determinant of HSV tropism; (ii) the chimeric gBHER2 bypasses the requirement for receptor-mediated activation of other essential entry glycoproteins.
[Mh] Termos MeSH primário: Glicoproteínas/metabolismo
Herpes Simples/virologia
Herpesvirus Humano 1/fisiologia
Receptor ErbB-2/metabolismo
Anticorpos de Cadeia Única/genética
[Mh] Termos MeSH secundário: Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/metabolismo
Glicoproteínas/genética
Herpes Simples/patologia
Herpesvirus Humano 1/genética
Herpesvirus Humano 1/patogenicidade
Seres Humanos
Integrinas/genética
Integrinas/metabolismo
Ligantes
Macrolídeos/farmacologia
Nectinas
Receptor ErbB-2/genética
Membro 14 de Receptores do Fator de Necrose Tumoral/genética
Membro 14 de Receptores do Fator de Necrose Tumoral/metabolismo
Receptores Virais/genética
Receptores Virais/metabolismo
Proteínas Recombinantes de Fusão
Anticorpos de Cadeia Única/metabolismo
Tropismo Viral
Internalização do Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Glycoproteins); 0 (Integrins); 0 (Ligands); 0 (Macrolides); 0 (NECTIN1 protein, human); 0 (Nectins); 0 (Receptors, Tumor Necrosis Factor, Member 14); 0 (Receptors, Virus); 0 (Recombinant Fusion Proteins); 0 (Single-Chain Antibodies); 0 (integrin alphavbeta8); 116764-51-3 (bafilomycin A); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006352


  5 / 478 MEDLINE  
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[PMID]:28397972
[Au] Autor:Shiotani H; Maruo T; Sakakibara S; Miyata M; Mandai K; Mochizuki H; Takai Y
[Ad] Endereço:Division of Pathogenetic Signaling, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe, 650-0047, Japan.
[Ti] Título:Aging-dependent expression of synapse-related proteins in the mouse brain.
[So] Source:Genes Cells;22(5):472-484, 2017 May.
[Is] ISSN:1365-2443
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A synapse is a cell adhesion structure that permits a neuron to pass a chemical or electrical signal to another neuron. They connect neurons and form neural networks that are essential for brain functions, such as learning and memory. At a chemical synapse, the presynapse and the postsynapse are connected by cell adhesion molecules. The presynapse contains synaptic vesicles and their release machinery, whereas the postsynapse contains postsynaptic densities and receptors for the neurotransmitters. Many proteins constituting a synapse have been identified, but their life-span expression profiles remain elusive. Here, we investigated the expression levels of representative synapse-related proteins by Western blot using the extranuclear supernatant fraction of the brains of mice at various ages. These proteins were classified into seven groups depending on their expression profiles during the embryonic stage, those from postnatal day 6 (P6) to P30, and those after P90. The expression levels of the majority of the proteins were gradually increased from the embryonic stage and then decreased at P14 or P30. After P90, the expression levels were not markedly changed or, in some proteins, increased. These results indicate that the expression levels of the synapse-related proteins are regulated orderly in an aging-dependent manner.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Encéfalo/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Sinapses/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/crescimento & desenvolvimento
Caderinas/genética
Caderinas/metabolismo
Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/metabolismo
Proteína 4 Homóloga a Disks-Large
Guanilato Quinases/genética
Guanilato Quinases/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Nectinas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 0 (Cell Adhesion Molecules); 0 (Disks Large Homolog 4 Protein); 0 (Dlg4 protein, mouse); 0 (Membrane Proteins); 0 (Nectins); EC 2.7.4.8 (Guanylate Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE
[do] DOI:10.1111/gtc.12489


  6 / 478 MEDLINE  
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[PMID]:28392352
[Au] Autor:Togashi H; Katsunuma S
[Ad] Endereço:Division of Molecular and Cellular Biology, Department of Biochemistry and Molecular Biology. Electronic address: htogashi@med.kobe-u.ac.jp.
[Ti] Título:Cellular recognition and patterning in sensory systems.
[So] Source:Exp Cell Res;358(1):52-57, 2017 Sep 01.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cells dissociated from various tissues of vertebrate embryos preferentially reaggregate with cells from the same tissue when they are mixed together. This tissue-specific recognition process in vertebrates is mainly mediated by a family of cell adhesion molecules because of their specific binding properties. Recent studies have revealed that two families of adhesion molecules, nectins and cadherins, are associated with each other, and these associations provide cells with the differential adhesive affinities required for cellular recognition and complex cellular pattern formations during development. This review provides an overview of recent findings regarding the cooperative functions of nectins and cadherins, as well as a discussion of the molecular basis underlying these functions.
[Mh] Termos MeSH primário: Caderinas/metabolismo
Moléculas de Adesão Celular/metabolismo
Adesão Celular/fisiologia
Comunicação Celular/fisiologia
Morfogênese/fisiologia
Vertebrados/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Nectinas
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cadherins); 0 (Cell Adhesion Molecules); 0 (Nectins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE


  7 / 478 MEDLINE  
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[PMID]:28381567
[Au] Autor:Deschamps T; Dogrammatzis C; Mullick R; Kalamvoki M
[Ad] Endereço:University of Kansas Medical Center, Department of Microbiology, Molecular Genetics and Immunology, Kansas City, Kansas, USA.
[Ti] Título:Cbl E3 Ligase Mediates the Removal of Nectin-1 from the Surface of Herpes Simplex Virus 1-Infected Cells.
[So] Source:J Virol;91(12), 2017 Jun 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Cbl E3 ligase has been linked to the down-modulation of surface signaling responses by inducing internalization of surface receptors. The adaptor protein CIN85 is a partner of Cbl that augments many of these interactions. Previously, an interaction was demonstrated between ICP0 and CIN85, which results in the removal of epidermal growth factor receptor (EGFR) from the surface of the infected cells with a concomitant attenuation of EGFR signaling. Here, we examined whether Cbl mediates the removal of the herpes simplex virus 1 (HSV-1) entry receptor Nectin-1 from the surface of infected cells. We found the following: (i) that Cbl, Nectin-1, and the viral glycoprotein D (gD) form a complex in infected cells; (ii) that during infection Nectin-1 is removed from the surface of the infected cells but is retained on the surface of cells that have been depleted of Cbl; and (iii) that in cells infected with a ΔICP0 mutant virus, Nectin-1 remained on the cell surface. Thus, Cbl is necessary but not sufficient for the removal of Nectin-1 from the cell surface. In addition, we observed that in Cbl-depleted cells there was enhanced entry after infection. These cells were susceptible to secondary infections by HSV-1. Viral entry in CIN85-depleted cells was only moderately enhanced compared to that in the Cbl-depleted cells, suggesting that the Cbl-Nectin-1 interaction is likely the key to the downregulation of surface Nectin-1. The removal of the HSV-1 entry receptor Nectin-1 from the surface of the infected cells may be part of the strategy of the virus to efficiently spread to uninfected cells. The Cbl E3 ligase suppresses surface signaling responses by inducing internalization of surface components. The targets of Cbl include such components as immune system receptors, growth factor receptors, adhesion, and cell-to-cell contact molecules. The immediate early protein ICP0 of herpes simplex virus 1 (HSV-1) interacts with CIN85, an adaptor protein that augments Cbl functions. The consequence of this interaction is the removal of the epidermal growth factor receptor (EGFR) from the surface of the infected cells with concomitant suppression of the EGF ligand signaling. The viral entry receptor Nectin-1 is also internalized during HSV-1 infection in a Cbl-dependent mechanism, and that increases the opportunity of the virus to spread to uninfected cells. The diversion of the Cbl/CIN85 endocytic machinery may be a strategy utilized by the virus to alter the cell surface pattern to prevent detrimental host responses.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/metabolismo
Herpesvirus Humano 1/fisiologia
Proteínas Proto-Oncogênicas c-cbl/metabolismo
Internalização do Vírus
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Moléculas de Adesão Celular/deficiência
Moléculas de Adesão Celular/genética
Endocitose
Células HEK293
Células Hep G2
Herpesvirus Humano 1/genética
Seres Humanos
Proteínas Imediatamente Precoces/metabolismo
Nectinas
Proteínas Proto-Oncogênicas c-cbl/genética
Receptor do Fator de Crescimento Epidérmico/deficiência
Receptor do Fator de Crescimento Epidérmico/genética
Receptor do Fator de Crescimento Epidérmico/metabolismo
Transdução de Sinais
Ubiquitina-Proteína Ligases/metabolismo
Proteínas do Envelope Viral/genética
Proteínas do Envelope Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cell Adhesion Molecules); 0 (Immediate-Early Proteins); 0 (NECTIN1 protein, human); 0 (Nectins); 0 (SH3KBP1 protein, human); 0 (Viral Envelope Proteins); 0 (glycoprotein D, Human herpesvirus 1); EC 2.3.2.27 (Proto-Oncogene Proteins c-cbl); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (Vmw110 protein, Human herpesvirus 1); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 6.3.2.- (CBL protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE


  8 / 478 MEDLINE  
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[PMID]:28331086
[Au] Autor:Delpeut S; Sawatsky B; Wong XX; Frenzke M; Cattaneo R; von Messling V
[Ad] Endereço:INRS-Institut Armand-Frappier, University of Quebec, Laval, Quebec, Canada.
[Ti] Título:Nectin-4 Interactions Govern Measles Virus Virulence in a New Model of Pathogenesis, the Squirrel Monkey (Saimiri sciureus).
[So] Source:J Virol;91(11), 2017 Jun 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In addition to humans, only certain nonhuman primates are naturally susceptible to measles virus (MeV) infection. Disease severity is species dependent, ranging from mild to moderate for macaques to severe and even lethal for certain New World monkey species. To investigate if squirrel monkeys ( ), which are reported to develop a course of disease similar to humans, may be better suited than macaques for the identification of virulence determinants or the evaluation of therapeutics, we infected them with a green fluorescent protein-expressing MeV. Compared to cynomolgus macaques ( ) infected with the same virus, the squirrel monkeys developed more-severe immunosuppression, higher viral load, and a broader range of clinical signs typical for measles. In contrast, infection with an MeV unable to interact with the epithelial receptor nectin-4, while causing immunosuppression, resulted in only a mild and transient rash and a short-lived elevation of the body temperature. Similar titers of the wild-type and nectin-4-blind MeV were detected in peripheral blood mononuclear cells and lymph node homogenates, but only the wild-type virus was found in tracheal lavage fluids and urine. Thus, our study demonstrates the importance of MeV interactions with nectin-4 for clinical disease in the new and better-performing model of measles pathogenesis. The characterization of mechanisms underlying measles virus clinical disease has been hampered by the lack of an animal model that reproduces the course of disease seen in human patients. Here, we report that infection of squirrel monkeys ( ) fulfills these requirements. Comparative infection with wild-type and epithelial cell receptor-blind viruses demonstrated the importance of epithelial cell infection for clinical disease, highlighting the spread to epithelia as an attractive target for therapeutic strategies.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/metabolismo
Vírus do Sarampo/patogenicidade
Sarampo/virologia
Modelos Animais
Saimiri
[Mh] Termos MeSH secundário: Animais
Células Epiteliais/virologia
Proteínas de Fluorescência Verde
Seres Humanos
Leucócitos Mononucleares/química
Leucócitos Mononucleares/virologia
Macaca fascicularis
Vírus do Sarampo/fisiologia
Nectinas
Carga Viral
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Nectins); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE


  9 / 478 MEDLINE  
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[PMID]:28218910
[Au] Autor:Labernadie A; Kato T; Brugués A; Serra-Picamal X; Derzsi S; Arwert E; Weston A; González-Tarragó V; Elosegui-Artola A; Albertazzi L; Alcaraz J; Roca-Cusachs P; Sahai E; Trepat X
[Ad] Endereço:Institute for Bioengineering of Catalonia, Barcelona 08028, Spain.
[Ti] Título:A mechanically active heterotypic E-cadherin/N-cadherin adhesion enables fibroblasts to drive cancer cell invasion.
[So] Source:Nat Cell Biol;19(3):224-237, 2017 Mar.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cancer-associated fibroblasts (CAFs) promote tumour invasion and metastasis. We show that CAFs exert a physical force on cancer cells that enables their collective invasion. Force transmission is mediated by a heterophilic adhesion involving N-cadherin at the CAF membrane and E-cadherin at the cancer cell membrane. This adhesion is mechanically active; when subjected to force it triggers ß-catenin recruitment and adhesion reinforcement dependent on α-catenin/vinculin interaction. Impairment of E-cadherin/N-cadherin adhesion abrogates the ability of CAFs to guide collective cell migration and blocks cancer cell invasion. N-cadherin also mediates repolarization of the CAFs away from the cancer cells. In parallel, nectins and afadin are recruited to the cancer cell/CAF interface and CAF repolarization is afadin dependent. Heterotypic junctions between CAFs and cancer cells are observed in patient-derived material. Together, our findings show that a mechanically active heterophilic adhesion between CAFs and cancer cells enables cooperative tumour invasion.
[Mh] Termos MeSH primário: Caderinas/metabolismo
Fibroblastos Associados a Câncer/metabolismo
Fibroblastos Associados a Câncer/patologia
Neoplasias/patologia
[Mh] Termos MeSH secundário: Adenocarcinoma/patologia
Fenômenos Biomecânicos
Fibroblastos Associados a Câncer/ultraestrutura
Adesão Celular
Moléculas de Adesão Celular/metabolismo
Linhagem Celular Tumoral
Ensaios de Migração Celular
Movimento Celular
Polaridade Celular
Técnicas de Cocultura
Feminino
Seres Humanos
Imagem Tridimensional
Neoplasias Pulmonares/patologia
Mecanotransdução Celular
Proteínas dos Microfilamentos
Nectinas
Invasividade Neoplásica
Neoplasias/metabolismo
Neoplasias de Células Escamosas/patologia
Pinças Ópticas
Esferoides Celulares/patologia
Neoplasias Vulvares/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 0 (Cell Adhesion Molecules); 0 (Microfilament Proteins); 0 (Nectins); 0 (afadin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3478


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[PMID]:28062492
[Au] Autor:Rossignoli A; Shang MM; Gladh H; Moessinger C; Foroughi Asl H; Talukdar HA; Franzén O; Mueller S; Björkegren JL; Folestad E; Skogsberg J
[Ad] Endereço:From the Division of Vascular Biology, Department of Medical Biochemistry and Biophysics (A.R., H.G., C.M., H.F.A., H.A.T., J.L.M.B., E.F., J.S.) and Unit of Computational Medicine, Department of Medicine (M.-M.S.), Karolinska Institutet, Stockholm, Sweden; Department of Genetics and Genomic Science
[Ti] Título:Poliovirus Receptor-Related 2: A Cholesterol-Responsive Gene Affecting Atherosclerosis Development by Modulating Leukocyte Migration.
[So] Source:Arterioscler Thromb Vasc Biol;37(3):534-542, 2017 Mar.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Recently, poliovirus receptor-related 2 ( ) emerged as a top gene in a global gene expression study aiming to detect plasma cholesterol-responsive genes causally related to atherosclerosis regression in hypercholesterolemic mice. PVRL2 is an adherens junction protein implied to play a role in transendothelial migration of leukocytes, a key feature in atherosclerosis development. In this study, we investigated the effect of deficiency on atherosclerosis development and transendothelial migration of leukocytes activity. APPROACH AND RESULTS: -deficient mice bred onto an atherosclerosis-prone background ( ) had less atherosclerotic lesions and more stable plaques compared with littermate controls ( ). mice also showed a 49% decrease in transendothelial migration of leukocytes activity observed using the in vivo air pouch model. In accordance, augmented arterial wall expression of during atherosclerosis progression coincided with an increased gene expression of migrating leukocytes into the vessel wall. Both in human and mice, gene and protein expression of PVRL2 was predominantly observed in the vascular endothelium according to the immunohistochemical and gene expression data. In addition, the cholesterol responsiveness of was also observed in humans. CONCLUSIONS: PVRL2 is a plasma cholesterol-responsive gene acting at endothelial sites of vascular inflammation that could potentially be a new therapeutic target for atherosclerosis prevention through its suggested transendothelial migration of leukocytes modulating activity.
[Mh] Termos MeSH primário: Aorta Torácica/metabolismo
Doenças da Aorta/metabolismo
Aterosclerose/metabolismo
Moléculas de Adesão Celular/metabolismo
Colesterol/sangue
Endotélio Vascular/metabolismo
Leucócitos/metabolismo
Migração Transendotelial e Transepitelial
[Mh] Termos MeSH secundário: Animais
Aorta Torácica/patologia
Doenças da Aorta/genética
Doenças da Aorta/patologia
Apolipoproteínas B/deficiência
Apolipoproteínas B/genética
Aterosclerose/genética
Aterosclerose/patologia
Adesão Celular
Moléculas de Adesão Celular/deficiência
Moléculas de Adesão Celular/genética
Linhagem Celular Tumoral
Técnicas de Cocultura
Modelos Animais de Doenças
Progressão da Doença
Endotélio Vascular/patologia
Predisposição Genética para Doença
Células Endoteliais da Veia Umbilical Humana/metabolismo
Seres Humanos
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Nectinas
Fenótipo
Interferência de RNA
Receptores de LDL/deficiência
Receptores de LDL/genética
Transdução de Sinais
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apob protein, mouse); 0 (Apolipoproteins B); 0 (Cell Adhesion Molecules); 0 (Nectin2 protein, mouse); 0 (Nectins); 0 (Receptors, LDL); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.116.308715



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