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Pesquisa : G02.111.570.820.709.275.750.250 [Categoria DeCS]
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  1 / 9 MEDLINE  
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[PMID]:29348579
[Au] Autor:Lin Z; Liu J; Ding H; Xu F; Liu H
[Ad] Endereço:State Key Laboratory of Natural and Biomimetic Drugs & Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing, 100191, China.
[Ti] Título:Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation.
[So] Source:Nat Commun;9(1):268, 2018 01 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:SALM5, a synaptic adhesion molecule implicated in autism, induces presynaptic differentiation through binding to the LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) that have been highlighted as presynaptic hubs for synapse formation. The mechanisms underlying SALM5/LAR-RPTP interaction remain unsolved. Here we report crystal structures of human SALM5 LRR-Ig alone and in complex with human PTPδ Ig1-3 (MeA ). Distinct from other LAR-RPTP ligands, SALM5 mainly exists as a dimer with LRR domains from two protomers packed in an antiparallel fashion. In the 2:2 heterotetrameric SALM5/PTPδ complex, a SALM5 dimer bridges two separate PTPδ molecules. Structure-guided mutations and heterologous synapse formation assays demonstrate that dimerization of SALM5 is prerequisite for its functionality in inducing synaptic differentiation. This study presents a structural template for the SALM family and reveals a mechanism for how a synaptic adhesion molecule directly induces cis-dimerization of LAR-RPTPs into higher-order signaling assembly.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular Neuronais/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
[Mh] Termos MeSH secundário: Baculoviridae
Dimerização
Células HEK293
Seres Humanos
Domínios de Imunoglobulina
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (SALM5 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02414-2


  2 / 9 MEDLINE  
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[PMID]:28977504
[Au] Autor:Falkenburg WJJ; Kempers AC; Dekkers G; Ooijevaar-de Heer P; Bentlage AEH; Vidarsson G; van Schaardenburg D; Toes REM; Scherer HU; Rispens T
[Ad] Endereço:Amsterdam Rheumatology and Immunology Center, Reade.
[Ti] Título:Rheumatoid factors do not preferentially bind to ACPA-IgG or IgG with altered galactosylation.
[So] Source:Rheumatology (Oxford);56(11):2025-2030, 2017 Nov 01.
[Is] ISSN:1462-0332
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Objectives: Recent reports describe interactions between the two most prominent RA-related autoantibodies, RFs and ACPAs. The main aim of the present study was to investigate whether RFs preferentially interact with ACPA-IgG over non-ACPA IgG. Additionally, interactions of RFs with IgG with altered galactose content in the Fc domain were examined, since ACPA-IgGs have been shown to have decreased Fc galactose content in RF+ patients. Methods: (Auto)antibody interactions were studied in a surface plasmon resonance imaging assay and with ELISA. Target antibodies were isolated from RA patient plasma (polyclonal ACPA- and non-ACPA-IgG) or recombinantly produced to obtain monoclonal IgG with well-defined Fc galactose content. Interacting autoantibodies were studied using autoantibody positive patient sera and two recombinantly produced IgM-RFs. Results: The sera from 41 RF+ RA patients showed similar RF binding to ACPA- and non-ACPA-IgG and no differences in binding to IgG with normal, high or low levels of Fc galactosylation. Two monoclonal IgM-RFs, one interacting with the CH2-CH3 interface and one binding close to the C-terminal end of the CH3 domain showed no influence of the Fc glycan on IgG binding by IgM-RF. Conclusion: Although interactions between RF and ACPA may play a role in inflammatory processes in RA, RFs do not preferentially interact with ACPA-IgG over non-ACPA-IgG nor with agalatosylated IgG over IgG with normal or high galactosylation.
[Mh] Termos MeSH primário: Artrite Reumatoide/metabolismo
Citrulina/metabolismo
Galactose/metabolismo
Imunoglobulina G/metabolismo
Fator Reumatoide/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação de Anticorpos
Ensaio de Imunoadsorção Enzimática
Seres Humanos
Domínios de Imunoglobulina
Imunoglobulina M/metabolismo
Ligação Proteica
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulin G); 0 (Immunoglobulin M); 29VT07BGDA (Citrulline); 9009-79-4 (Rheumatoid Factor); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1093/rheumatology/kex284


  3 / 9 MEDLINE  
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[PMID]:26891472
[Au] Autor:Christaller WA; Vos Y; Gebre-Medhin S; Hofstra RM; Schäfer MK
[Ad] Endereço:Department of Anesthesiology, University Medical Center, Johannes Gutenberg-University Mainz, Mainz, Germany.
[Ti] Título:L1 syndrome diagnosis complemented with functional analysis of L1CAM variants located to the two N-terminal Ig-like domains.
[So] Source:Clin Genet;91(1):115-120, 2017 Jan.
[Is] ISSN:1399-0004
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:L1CAM gene mutations cause neurodevelopmental disorders collectively termed L1 syndrome. Insufficient information about L1CAM variants complicates clinical prognosis, genetic diagnosis and genetic counseling. We combined clinical data, in silico effect predictions and functional analysis of four L1CAM variants, p.I37N, p.T38M, p.M172I and p.D202Y, located to the two N-terminal Ig-like domains present in five families with symptoms of L1 syndrome. Software tools predicted destabilizing effects of p.I37N and p.D202Y but results for p.T38M and p.M172I were inconsistent. Cell surface expression of mutant proteins L1-T38M, L1-M172I and L1-D202Y was normal. Conversely, L1-I37N accumulated in the endoplasmic reticulum (ER) and showed temperature-sensitive protein maturation suggesting that p.I37N induces protein misfolding. L1CAM-mediated cell-cell aggregation was severely impaired by L1CAM variants p.I37N, p.M172I and p.D202Y but was preserved by the variant p.T38M. Our experimental data indicate that protein misfolding and accumulation in the ER affect function of the L1CAM variant p.I37N whereas the variants p.M172I and p.D202Y impair homophilic interaction at the cell surface.
[Mh] Termos MeSH primário: Doenças Genéticas Ligadas ao Cromossomo X/genética
Predisposição Genética para Doença/genética
Deficiência Intelectual/genética
Mutação de Sentido Incorreto
Molécula L1 de Adesão de Célula Nervosa/genética
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação/genética
Comunicação Celular/genética
Membrana Celular/metabolismo
Retículo Endoplasmático/metabolismo
Saúde da Família
Feminino
Doenças Genéticas Ligadas ao Cromossomo X/diagnóstico
Doenças Genéticas Ligadas ao Cromossomo X/metabolismo
Células HEK293
Seres Humanos
Immunoblotting
Domínios de Imunoglobulina/genética
Deficiência Intelectual/diagnóstico
Deficiência Intelectual/metabolismo
Masculino
Microscopia Confocal
Molécula L1 de Adesão de Célula Nervosa/metabolismo
Linhagem
Homologia de Sequência de Aminoácidos
Paraplegia Espástica Hereditária/diagnóstico
Paraplegia Espástica Hereditária/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neural Cell Adhesion Molecule L1)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160219
[St] Status:MEDLINE
[do] DOI:10.1111/cge.12763


  4 / 9 MEDLINE  
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[PMID]:27821665
[Au] Autor:Jansen CA; van Haarlem DA; Sperling B; van Kooten PJ; de Vries E; Viertlboeck BC; Vervelde L; Göbel TW
[Ad] Endereço:Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, the Netherlands; and.
[Ti] Título:Identification of an Activating Chicken Ig-like Receptor Recognizing Avian Influenza Viruses.
[So] Source:J Immunol;197(12):4696-4703, 2016 Dec 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chicken Ig-like receptors (CHIRs) represent a multigene family encoded by the leukocyte receptor complex that encodes a variety of receptors that are subdivided into activating CHIR-A, inhibitory CHIR-B, and bifunctional CHIR-AB. Apart from CHIR-AB, which functions as an Fc receptor, CHIR ligands are unknown. In the current study, we used a panel of different BWZ.36 CHIR reporter cells to identify an interaction between specific CHIRs and avian influenza virus (AIV). The specificity of the CHIR-AIV interaction was further demonstrated using CHIR fusion proteins that bound to AIV-coated plates and were able to reduce the interaction of reporter cells with AIV. There was no difference in binding of CHIR to different AIV strains. Furthermore, CHIR fusion proteins reduced AIV-induced in vitro activation of NK cells obtained from lungs of AIV-infected animals, as judged by the lower frequency of CD107 cells. Because the original CHIR reporter lines were generated based on sequence information about extracellular CHIR domains, we next identified a full-length CHIR that displayed similar binding to AIV. The sequence analysis identified this CHIR as a CHIR-A. Neuraminidase treatment of coated CHIR-human Ig proteins reduced binding of trimeric H5 proteins to CHIR. This suggests that the interaction is dependent on sialic acid moieties on the receptor. In conclusion, this article identifies AIV as a ligand of CHIR-A and describes the functional consequences of this interaction.
[Mh] Termos MeSH primário: Proteínas Aviárias/metabolismo
Galinhas/imunologia
Vírus da Influenza A Subtipo H9N2/imunologia
Influenza Aviária/imunologia
Células Matadoras Naturais/imunologia
Pulmão/patologia
Receptores Fc/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas Aviárias/genética
Cães
Domínios de Imunoglobulina/genética
Células Matadoras Naturais/virologia
Ativação Linfocitária
Células Madin Darby de Rim Canino
Camundongos
Família Multigênica/genética
Engenharia de Proteínas
Receptores Fc/genética
Proteínas Recombinantes de Fusão/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Avian Proteins); 0 (Receptors, Fc); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161109
[St] Status:MEDLINE


  5 / 9 MEDLINE  
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[PMID]:27645568
[Au] Autor:Li J; Zhou C; Dong B; Zhong H; Chen S; Li Q; Wang Z
[Ad] Endereço:a School of Pharmaceutical Sciences, Sun Yat-Sen University , Guangzhou , China.
[Ti] Título:Single domain antibody-based bispecific antibody induces potent specific anti-tumor activity.
[So] Source:Cancer Biol Ther;17(12):1231-1239, 2016 Dec.
[Is] ISSN:1555-8576
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bispecific antibodies have emerged as powerful therapeutic agents given their high specificity and ability to induce a potent immune response. Various bispecific antibody formats have been designed and studied regarding their applications in cancer therapy, though associated with issues of short half-life or manufacturing difficulties. Herein, a novel bispecific antibody, SS-Fc, was constructed by pairing 2 single-domain antibodies, anti-CD16 and anti-CEA, which were fused with CH3 "knobs into holes" mutations individually. SS-Fc was expressed and purified from E.coli. In vitro and in vivo experiments confirmed that SS-Fc can form a heterodimeric bispecific antibody when expressed and purified from E. coli. By engaging natural killer (NK) cells through an anti-CD16 single domain antibody, the SS-Fc bispecific antibody exhibited potent in vitro and in vivo cytotoxicity against cancer cells with carcinoembryonic antigen (CEA) expression. Thus, SS-Fc represents a novel bispecific antibody format that can be applied to a wide range of both discovery and clinical applications.
[Mh] Termos MeSH primário: Anticorpos Biespecíficos/uso terapêutico
Antígeno Carcinoembrionário/imunologia
Imunoterapia/métodos
Células Matadoras Naturais/efeitos dos fármacos
Neoplasias/imunologia
Neoplasias/terapia
Receptores de IgG/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Biespecíficos/administração & dosagem
Desenho de Drogas
Células HT29
Seres Humanos
Domínios de Imunoglobulina
Células Matadoras Naturais/imunologia
Camundongos
Camundongos Endogâmicos NOD
Camundongos SCID
Proteínas Recombinantes/imunologia
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Bispecific); 0 (Carcinoembryonic Antigen); 0 (Receptors, IgG); 0 (Recombinant Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160921
[St] Status:MEDLINE
[do] DOI:10.1080/15384047.2016.1235659


  6 / 9 MEDLINE  
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[PMID]:27539083
[Au] Autor:Reichert MC; Brown HE; Evans TA
[Ad] Endereço:Department of Biological Sciences, University of Arkansas, Fayetteville, AR, 72701, USA.
[Ti] Título:In vivo functional analysis of Drosophila Robo1 immunoglobulin-like domains.
[So] Source:Neural Dev;11(1):15, 2016 Aug 18.
[Is] ISSN:1749-8104
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In animals with bilateral symmetry, midline crossing of axons in the developing central nervous system is regulated by Slit ligands and their neuronal Roundabout (Robo) receptors. Multiple structural domains are present in an evolutionarily conserved arrangement in Robo family proteins, but our understanding of the functional importance of individual domains for midline repulsive signaling is limited. METHODS: We have examined the functional importance of each of the five conserved immunoglobulin-like (Ig) domains within the Drosophila Robo1 receptor. We generated a series of Robo1 variants, each lacking one of the five Ig domains (Ig1-5), and tested each for their ability to bind Slit when expressed in cultured Drosophila cells. We used a transgenic approach to express each variant in robo1's normal expression pattern in wild-type and robo1 mutant embryos, and examined the effects of deleting each domain on receptor expression, axonal localization, regulation, and midline repulsive signaling in vivo. RESULTS: We show that individual deletion of Ig domains 2-5 does not interfere with Robo1's ability to bind Slit, while deletion of Ig1 strongly disrupts Slit binding. None of the five Ig domains (Ig1-5) are individually required for proper expression of Robo1 in embryonic neurons, for exclusion from commissural axon segments in wild-type embryos, or for downregulation by Commissureless (Comm), a negative regulator of Slit-Robo repulsion in Drosophila. Each of the Robo1 Ig deletion variants (with the exception of Robo1∆Ig1) were able to restore midline crossing in robo1 mutant embryos to nearly the same extent as full-length Robo1, indicating that Ig domains 2-5 are individually dispensable for midline repulsive signaling in vivo. CONCLUSIONS: Our findings indicate that four of the five Ig domains within Drosophila Robo1 are dispensable for its role in midline repulsion, despite their strong evolutionary conservation, and highlight a unique requirement for the Slit-binding Ig1 domain in the regulation of midline crossing.
[Mh] Termos MeSH primário: Orientação de Axônios
Axônios/metabolismo
Proteínas de Drosophila/metabolismo
Domínios de Imunoglobulina
Proteínas do Tecido Nervoso/metabolismo
Receptores Imunológicos/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Axônios/fisiologia
Células Cultivadas
Drosophila
Proteínas de Drosophila/fisiologia
Proteínas de Membrana/metabolismo
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/fisiologia
Receptores Imunológicos/genética
Receptores Imunológicos/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); 0 (Receptors, Immunologic); 0 (commissureless protein, Drosophila); 0 (roundabout protein); 0 (sli protein, Drosophila)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE
[do] DOI:10.1186/s13064-016-0071-0


  7 / 9 MEDLINE  
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[PMID]:27442026
[Au] Autor:Martin JN; Ball LM; Solomon TL; Dewald AH; Criss AK; Columbus L
[Ad] Endereço:Department of Chemistry and ‡Department of Microbiology, Immunology, and Cancer Biology, University of Virginia , Charlottesville, Virginia 22903, United States.
[Ti] Título:Neisserial Opa Protein-CEACAM Interactions: Competition for Receptors as a Means of Bacterial Invasion and Pathogenesis.
[So] Source:Biochemistry;55(31):4286-94, 2016 Aug 09.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carcino-embryonic antigen-like cellular adhesion molecules (CEACAMs), members of the immunoglobulin superfamily, are responsible for cell-cell interactions and cellular signaling events. Extracellular interactions with CEACAMs have the potential to induce phagocytosis, as is the case with pathogenic Neisseria bacteria. Pathogenic Neisseria species express opacity-associated (Opa) proteins, which interact with a subset of CEACAMs on human cells, and initiate the engulfment of the bacterium. We demonstrate that recombinant Opa proteins reconstituted into liposomes retain the ability to recognize and interact with CEACAMs in vitro but do not maintain receptor specificity compared to that of Opa proteins natively expressed by Neisseria gonorrhoeae. We report that two Opa proteins interact with CEACAMs with nanomolar affinity, and we hypothesize that this high affinity is necessary to compete with the native CEACAM homo- and heterotypic interactions in the host. Understanding the mechanisms of Opa protein-receptor recognition and engulfment enhances our understanding of Neisserial pathogenesis. Additionally, these mechanisms provide insight into how human cells that are typically nonphagocytic can utilize CEACAM receptors to internalize exogenous matter, with implications for the targeted delivery of therapeutics and development of imaging agents.
[Mh] Termos MeSH primário: Antígenos CD/metabolismo
Proteínas da Membrana Bacteriana Externa/metabolismo
Antígeno Carcinoembrionário/metabolismo
Moléculas de Adesão Celular/metabolismo
Neisseria/metabolismo
[Mh] Termos MeSH secundário: Antígenos CD/química
Proteínas da Membrana Bacteriana Externa/química
Proteínas da Membrana Bacteriana Externa/genética
Antígeno Carcinoembrionário/química
Moléculas de Adesão Celular/química
Interações Hospedeiro-Patógeno
Seres Humanos
Domínios de Imunoglobulina
Lipossomos
Modelos Moleculares
Neisseria/genética
Neisseria/patogenicidade
Neisseria gonorrhoeae/genética
Neisseria gonorrhoeae/metabolismo
Neisseria gonorrhoeae/patogenicidade
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Bacterial Outer Membrane Proteins); 0 (CD66 antigens); 0 (CEACAM3 protein, human); 0 (Carcinoembryonic Antigen); 0 (Cell Adhesion Molecules); 0 (Liposomes); 0 (Recombinant Proteins); 156319-92-5 (Opa protein, Neisseria)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160722
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00124


  8 / 9 MEDLINE  
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[PMID]:27267927
[Au] Autor:Samatov TR; Wicklein D; Tonevitsky AG
[Ad] Endereço:SRC Bioclinicum, Ugreshskaya str 2/85, 115088 Moscow, Russia; Moscow State University of Mechanical Engineering, Bolshaya Semenovskaya str 38, 107023 Moscow, Russia. Electronic address: t.samatov@bioclinicum.com.
[Ti] Título:L1CAM: Cell adhesion and more.
[So] Source:Prog Histochem Cytochem;51(2):25-32, 2016 08.
[Is] ISSN:1873-2186
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:L1CAM is a cell adhesion molecule of the immunoglobulin superfamily which was originally discovered as a major player in the development of the nervous system. L1CAM was demonstrated to have prognostic value in different cancers and to be a promising target for anti-cancer therapy. Here we overview the present data on L1CAM structure and function, regulation of its expression, role in cancer and therapeutic potential.
[Mh] Termos MeSH primário: Transformação Celular Neoplásica/genética
Regulação Neoplásica da Expressão Gênica
Neoplasias/genética
Molécula L1 de Adesão de Célula Nervosa/genética
Neurônios/metabolismo
[Mh] Termos MeSH secundário: Anticorpos Monoclonais/uso terapêutico
Antineoplásicos/uso terapêutico
Adesão Celular/efeitos dos fármacos
Transformação Celular Neoplásica/metabolismo
Transformação Celular Neoplásica/patologia
Células Epiteliais/metabolismo
Células Epiteliais/patologia
Transição Epitelial-Mesenquimal/genética
Fibronectinas/química
Fibronectinas/genética
Fibronectinas/metabolismo
Seres Humanos
Domínios de Imunoglobulina/genética
Neoplasias/metabolismo
Neoplasias/patologia
Neoplasias/terapia
Molécula L1 de Adesão de Célula Nervosa/antagonistas & inibidores
Molécula L1 de Adesão de Célula Nervosa/química
Molécula L1 de Adesão de Célula Nervosa/metabolismo
Neurônios/patologia
Prognóstico
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antineoplastic Agents); 0 (Fibronectins); 0 (Neural Cell Adhesion Molecule L1); 0 (RNA, Small Interfering)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170421
[Lr] Data última revisão:
170421
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE


  9 / 9 MEDLINE  
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[PMID]:27030267
[Au] Autor:Pinkert S; Röger C; Kurreck J; Bergelson JM; Fechner H
[Ad] Endereço:Department of Applied Biochemistry, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany sandra.pinkert@tu-berlin.de.
[Ti] Título:The Coxsackievirus and Adenovirus Receptor: Glycosylation and the Extracellular D2 Domain Are Not Required for Coxsackievirus B3 Infection.
[So] Source:J Virol;90(12):5601-10, 2016 Jun 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: The coxsackievirus and adenovirus receptor (CAR) is a member of the immunoglobulin superfamily (IgSF) and functions as a receptor for coxsackie B viruses (CVBs). The extracellular portion of CAR comprises two glycosylated immunoglobulin-like domains, D1 and D2. CAR-D1 binds to the virus and is essential for virus infection; however, it is not known whether D2 is also important for infection, and the role of glycosylation has not been explored. To understand the function of these structural components in CAR-mediated CVB3 infection, we generated a panel of human (h) CAR deletion and substitution mutants and analyzed their functionality as CVB receptors, examining both virus binding and replication. Lack of glycosylation of the CAR-D1 or -D2 domains did not adversely affect CVB3 binding or infection, indicating that the glycosylation of CAR is not required for its receptor functions. Deletion of the D2 domain reduced CVB3 binding, with a proportionate reduction in the efficiency of virus infection. Replacement of D2 with the homologous D2 domain from chicken CAR, or with the heterologous type C2 immunoglobulin-like domain from IgSF11, another IgSF member, fully restored receptor function; however, replacement of CAR-D2 with domains from CD155 or CD80 restored function only in part. These data indicate that glycosylation of the extracellular domain of hCAR plays no role in CVB3 receptor function and that CAR-D2 is not specifically required. The D2 domain may function largely as a spacer permitting virus access to D1; however, the data may also suggest that D2 affects virus binding by influencing the conformation of D1. IMPORTANCE: An important step in virus infection is the initial interaction of the virus with its cellular receptor. Although the role in infection of the extracellular CAR-D1, cytoplasmic, and transmembrane domains have been analyzed extensively, nothing is known about the function of CAR-D2 and the extracellular glycosylation of CAR. Our data indicate that glycosylation of the extracellular CAR domain has only minor importance for the function of CAR as CVB3 receptor and that the D2 domain is not essential per se but contributes to receptor function by promoting the exposure of the D1 domain on the cell surface. These results contribute to our understanding of the coxsackievirus-receptor interactions.
[Mh] Termos MeSH primário: Proteína de Membrana Semelhante a Receptor de Coxsackie e Adenovirus/química
Proteína de Membrana Semelhante a Receptor de Coxsackie e Adenovirus/metabolismo
Enterovirus Humano B/fisiologia
Ligação Viral
[Mh] Termos MeSH secundário: Animais
Células CHO
Galinhas
Proteína de Membrana Semelhante a Receptor de Coxsackie e Adenovirus/genética
Cricetulus
Enterovirus Humano B/química
Glicosilação
Células HeLa
Seres Humanos
Domínios de Imunoglobulina/genética
Mutação
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coxsackie and Adenovirus Receptor-Like Membrane Protein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170503
[Lr] Data última revisão:
170503
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.00315-16



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