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1.
Recurso na Internet em Português | LIS - Localizador de Informação em Saúde | ID: lis-LISBR1.1-46945

RESUMO

Site do Ministério da Saúde. (Brasil). Tirando dúvidas sobre o corona Virús. O que é o Virús, suas causas, sintomas, tratamento, diagnostico é prevenção Saiba mais sobre o Coronavirus...


Assuntos
Coronavírus da Síndrome Respiratória do Oriente Médio/patogenicidade , Coronavirus Humano 229E/patogenicidade , Infecções por Coronavirus/prevenção & controle
2.
Nat Commun ; 8(1): 1735, 2017 11 23.
Artigo em Inglês | MEDLINE | ID: mdl-29170370

RESUMO

RNA viruses are characterized by a high mutation rate, a buffer against environmental change. Nevertheless, the means by which random mutation improves viral fitness is not well characterized. Here we report the X-ray crystal structure of the receptor-binding domain (RBD) of the human coronavirus, HCoV-229E, in complex with the ectodomain of its receptor, aminopeptidase N (APN). Three extended loops are solely responsible for receptor binding and the evolution of HCoV-229E and its close relatives is accompanied by changing loop-receptor interactions. Phylogenetic analysis shows that the natural HCoV-229E receptor-binding loop variation observed defines six RBD classes whose viruses have successively replaced each other in the human population over the past 50 years. These RBD classes differ in their affinity for APN and their ability to bind an HCoV-229E neutralizing antibody. Together, our results provide a model for alphacoronavirus adaptation and evolution based on the use of extended loops for receptor binding.


Assuntos
Coronavirus Humano 229E/genética , Coronavirus Humano 229E/fisiologia , Adaptação Fisiológica/genética , Sequência de Aminoácidos , Antígenos CD13/química , Antígenos CD13/metabolismo , Coronavirus Humano 229E/patogenicidade , Infecções por Coronavirus/virologia , Cristalografia por Raios X , Evolução Molecular , Variação Genética , Células HEK293 , Interações Hospedeiro-Patógeno/genética , Humanos , Modelos Biológicos , Modelos Moleculares , Filogenia , Domínios e Motivos de Interação entre Proteínas , Receptores Virais/química , Receptores Virais/metabolismo , Glicoproteína da Espícula de Coronavírus/química , Glicoproteína da Espícula de Coronavírus/genética , Glicoproteína da Espícula de Coronavírus/metabolismo , Ressonância de Plasmônio de Superfície
3.
J Virol ; 86(14): 7577-87, 2012 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-22553325

RESUMO

Human coronaviruses are associated with upper respiratory tract infections that occasionally spread to the lungs and other organs. Although airway epithelial cells represent an important target for infection, the respiratory epithelium is also composed of an elaborate network of dendritic cells (DCs) that are essential sentinels of the immune system, sensing pathogens and presenting foreign antigens to T lymphocytes. In this report, we show that in vitro infection by human coronavirus 229E (HCoV-229E) induces massive cytopathic effects in DCs, including the formation of large syncytia and cell death within only few hours. In contrast, monocytes are much more resistant to infection and cytopathic effects despite similar expression levels of CD13, the membrane receptor for HCoV-229E. While the differentiation of monocytes into DCs in the presence of granulocyte-macrophage colony-stimulating factor and interleukin-4 requires 5 days, only 24 h are sufficient for these cytokines to sensitize monocytes to cell death and cytopathic effects when infected by HCoV-229E. Cell death induced by HCoV-229E is independent of TRAIL, FasL, tumor necrosis factor alpha, and caspase activity, indicating that viral replication is directly responsible for the observed cytopathic effects. The consequence of DC death at the early stage of HCoV-229E infection may have an impact on the early control of viral dissemination and on the establishment of long-lasting immune memory, since people can be reinfected multiple times by HCoV-229E.


Assuntos
Resfriado Comum/virologia , Coronavirus Humano 229E/patogenicidade , Efeito Citopatogênico Viral , Células Dendríticas/virologia , Monócitos/virologia , Mucosa Respiratória/virologia , Antígenos CD34/análise , Antígenos CD13/análise , Caspases/metabolismo , Morte Celular , Coronavirus Humano 229E/fisiologia , Células Dendríticas/patologia , Proteína Ligante Fas/metabolismo , Células Gigantes/patologia , Células Gigantes/virologia , Humanos , Monócitos/imunologia , Monócitos/patologia , Mucosa Respiratória/citologia , Ligante Indutor de Apoptose Relacionado a TNF/metabolismo , Fator de Necrose Tumoral alfa/biossíntese , Fator de Necrose Tumoral alfa/metabolismo , Replicação Viral
4.
J Gen Virol ; 93(Pt 3): 494-503, 2012 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-22090214

RESUMO

Human coronavirus strain 229E (HCoV-229E) commonly causes upper respiratory tract infections. However, lower respiratory tract infections can occur in some individuals, indicating that cells in the distal lung are susceptible to HCoV-229E. This study determined the virus susceptibility of primary cultures of human alveolar epithelial cells and alveolar macrophages (AMs). Fluorescent antibody staining indicated that HCoV-229E could readily infect AMs, but no evidence was found for infection in differentiated alveolar epithelial type II cells and only a very low level of infection in type II cells transitioning to the type I-like cell phenotype. However, a human bronchial epithelial cell line (16HBE) was readily infected. The innate immune response of AMs to HCoV-229E infection was evaluated for cytokine production and interferon (IFN) gene expression. AMs secreted significant amounts of tumour necrosis factor alpha (TNF-α), regulated on activation normal T-cell expressed and secreted (RANTES/CCL5) and macrophage inflammatory protein 1ß (MIP-1ß/CCL4) in response to HCoV-229E infection, but these cells exhibited no detectable increase in IFN-ß or interleukin-29 in mRNA levels. AMs from smokers had reduced secretion of TNF-α compared with non-smokers in response to HCoV-229E infection. Surfactant protein A (SP-A) and SP-D are part of the innate immune system in the distal lung. Both surfactant proteins bound to HCoV-229E, and pre-treatment of HCoV-229E with SP-A or SP-D inhibited infection of 16HBE cells. In contrast, there was a modest reduction in infection in AMs by SP-A, but not by SP-D. In summary, AMs are an important target for HCoV-229E, and they can mount a pro-inflammatory innate immune response to infection.


Assuntos
Coronavirus Humano 229E/patogenicidade , Macrófagos Alveolares/virologia , Células Cultivadas , Citocinas/biossíntese , Citocinas/metabolismo , Ensaio de Imunoadsorção Enzimática , Células Epiteliais/virologia , Técnica Direta de Fluorescência para Anticorpo , Expressão Gênica , Perfilação da Expressão Gênica , Humanos , Macrófagos Alveolares/imunologia , Ensaio de Placa Viral
6.
J Virol ; 85(13): 6381-9, 2011 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-21507972

RESUMO

Coronaviruses are a family of enveloped single-stranded positive-sense RNA viruses causing respiratory, enteric, and neurologic diseases in mammals and fowl. Human coronaviruses are recognized to cause up to a third of common colds and are suspected to be involved in enteric and neurologic diseases. Coronavirus replication involves the generation of nested subgenomic mRNAs (sgmRNAs) with a common capped 5' leader sequence. The translation of most of the sgmRNAs is thought to be cap dependent and displays a requirement for eukaryotic initiation factor 4F (eIF4F), a heterotrimeric complex needed for the recruitment of 40S ribosomes. We recently reported on an ultrahigh-throughput screen to discover compounds that inhibit eIF4F activity by blocking the interaction of two of its subunits (R. Cencic et al., Proc. Natl. Acad. Sci. U. S. A. 108:1046-1051, 2011). Herein we describe a molecule from this screen that prevents the interaction between eIF4E (the cap-binding protein) and eIF4G (a large scaffolding protein), inhibiting cap-dependent translation. This inhibitor significantly decreased human coronavirus 229E (HCoV-229E) replication, reducing the percentage of infected cells and intra- and extracellular infectious virus titers. Our results support the strategy of targeting the eIF4F complex to block coronavirus infection.


Assuntos
Antivirais/farmacologia , Coronavirus Humano 229E/fisiologia , Fator de Iniciação 4E em Eucariotos/antagonistas & inibidores , Fator de Iniciação 4G em Eucariotos/antagonistas & inibidores , Replicação Viral/efeitos dos fármacos , Antivirais/química , Linhagem Celular , Coronavirus Humano 229E/efeitos dos fármacos , Coronavirus Humano 229E/metabolismo , Coronavirus Humano 229E/patogenicidade , Descoberta de Drogas , Fator de Iniciação 4E em Eucariotos/metabolismo , Fator de Iniciação 4G em Eucariotos/metabolismo , Ensaios de Triagem em Larga Escala , Humanos , Biossíntese de Proteínas/efeitos dos fármacos , Capuzes de RNA/genética , Capuzes de RNA/metabolismo , Bibliotecas de Moléculas Pequenas , Proteínas Virais/metabolismo
7.
Antivir Ther ; 12(4 Pt B): 651-8, 2007.
Artigo em Inglês | MEDLINE | ID: mdl-17944272

RESUMO

SARS-CoV, human coronavirus NL63 (HCoV-NL63) and HCoV-HKU1 were first described in 2003, 2004 and 2005 respectively. Nevertheless, discovery of three new human coronaviruses does not necessary represent a sudden increase in emerging infections by new coronaviruses. Only SARS-CoV has recently been introduced to the human population; the other two have been circulating in humans for a long time. HCoV-HKU1 and HCoV-NL63 are respiratory coronaviruses, are frequently found during lower and upper respiratory tract infections, have spread worldwide, and prefer the winter season. These characteristics do not differ greatly from the symptoms described for the 'old' viruses HCoV-229E and HCoV-OC43. This report presents an overview of the current knowledge of the four human coronavirus that are now circulating in the human population.


Assuntos
Infecções por Coronavirus/fisiopatologia , Coronavirus/patogenicidade , Adulto , Idoso , Criança , Pré-Escolar , Coronavirus/classificação , Coronavirus Humano 229E/patogenicidade , Infecções por Coronavirus/virologia , Coronavirus Humano OC43/patogenicidade , Humanos , Lactente , Masculino , Infecções Respiratórias/fisiopatologia , Infecções Respiratórias/virologia , Vírus da SARS/patogenicidade , Síndrome Respiratória Aguda Grave/fisiopatologia , Síndrome Respiratória Aguda Grave/virologia
11.
J Virol ; 80(17): 8639-52, 2006 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-16912312

RESUMO

We have recently demonstrated that the severe acute respiratory syndrome coronavirus (SARS-CoV) receptor angiotensin converting enzyme 2 (ACE2) also mediates cellular entry of the newly discovered human coronavirus (hCoV) NL63. Here, we show that expression of DC-SIGN augments NL63 spike (S)-protein-driven infection of susceptible cells, while only expression of ACE2 but not DC-SIGN is sufficient for entry into nonpermissive cells, indicating that ACE2 fulfills the criteria of a bona fide hCoV-NL63 receptor. As for SARS-CoV, murine ACE2 is used less efficiently by NL63-S for entry than human ACE2. In contrast, several amino acid exchanges in human ACE2 which diminish SARS-S-driven entry do not interfere with NL63-S-mediated infection, suggesting that SARS-S and NL63-S might engage human ACE2 differentially. Moreover, we observed that NL63-S-driven entry was less dependent on a low-pH environment and activity of endosomal proteases compared to infection mediated by SARS-S, further suggesting differences in hCoV-NL63 and SARS-CoV cellular entry. NL63-S does not exhibit significant homology to SARS-S but is highly related to the S-protein of hCoV-229E, which enters target cells by engaging CD13. Employing mutagenic analyses, we found that the N-terminal unique domain in NL63-S, which is absent in 229E-S, does not confer binding to ACE2. In contrast, the highly homologous C-terminal parts of the NL63-S1 and 229E-S1 subunits in conjunction with distinct amino acids in the central regions of these proteins confer recognition of ACE2 and CD13, respectively. Therefore, despite the high homology of these sequences, they likely form sufficiently distinct surfaces, thus determining receptor specificity.


Assuntos
Coronavirus Humano 229E/patogenicidade , Coronavirus/patogenicidade , Glicoproteínas de Membrana/química , Peptidil Dipeptidase A/metabolismo , Receptores Virais/metabolismo , Proteínas do Envelope Viral/química , Animais , Moléculas de Adesão Celular/metabolismo , Linhagem Celular , Coronavirus/metabolismo , Coronavirus/fisiologia , Coronavirus Humano 229E/metabolismo , Coronavirus Humano 229E/fisiologia , Cricetinae , Humanos , Lectinas Tipo C/metabolismo , Glicoproteínas de Membrana/genética , Glicoproteínas de Membrana/metabolismo , Camundongos , Receptores de Superfície Celular/metabolismo , Glicoproteína da Espícula de Coronavírus , Proteínas do Envelope Viral/genética , Proteínas do Envelope Viral/metabolismo
12.
Pediatr Infect Dis J ; 24(11 Suppl): S223-7, discussion S226, 2005 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-16378050

RESUMO

Human coronaviruses, first characterized in the 1960s, are responsible for a substantial proportion of upper respiratory tract infections in children. Since 2003, at least 5 new human coronaviruses have been identified, including the severe acute respiratory syndrome coronavirus, which caused significant morbidity and mortality. NL63, representing a group of newly identified group I coronaviruses that includes NL and the New Haven coronavirus, has been identified worldwide. These viruses are associated with both upper and lower respiratory tract disease and are likely common human pathogens. The global distribution of a newly identified group II coronavirus, HKU1, has not yet been established. Coronavirology has advanced significantly in the past few years. The SARS epidemic put the animal coronaviruses in the spotlight. The background and history relative to this important and expanding research area are reviewed here.


Assuntos
Infecções por Coronavirus/história , Coronavirus/classificação , Coronavirus/isolamento & purificação , Adulto , Idoso , Animais , Criança , Pré-Escolar , Doenças Transmissíveis Emergentes/história , Coronavirus/patogenicidade , Coronavirus Humano 229E/isolamento & purificação , Coronavirus Humano 229E/patogenicidade , Infecções por Coronavirus/epidemiologia , Infecções por Coronavirus/virologia , Feminino , História do Século XX , Humanos , Lactente , Masculino , Vírus da SARS/isolamento & purificação , Vírus da SARS/patogenicidade , Síndrome Respiratória Aguda Grave
13.
Uirusu ; 55(1): 19-26, 2005 Jun.
Artigo em Japonês | MEDLINE | ID: mdl-16308526

RESUMO

The endocytic function of caveolae has been controversial for a long time. However, a real-time-imaging analysis of Simian virus 40 (SV40) 's entry in cells has indicated the existence of caveolar endocytosis during virus entry. The caveolae engulfed SV40 virions begin budding from plasma membrane depending on dynamin. SV40 enclosed in caveolae vesicles move to the caveosome, then to the endoplasmic reticulum. In addition, it was demonstrated that human coronavirus-229E enters the cell through caveolae. This review examines the involvement of caveolae in endocytosis used by the viral entry system.


Assuntos
Cavéolas/fisiologia , Cavéolas/virologia , Coronavirus Humano 229E/patogenicidade , Endocitose/fisiologia , Vírus 40 dos Símios/patogenicidade , Caveolina 1/fisiologia , Membrana Celular/virologia , Coronavirus Humano 229E/ultraestrutura , Dinaminas/fisiologia , Retículo Endoplasmático/virologia , Endossomos/fisiologia , Endossomos/virologia , Interpretação de Imagem Assistida por Computador/métodos , Microscopia Eletrônica/métodos , Vírus 40 dos Símios/ultraestrutura , Vírion/crescimento & desenvolvimento
14.
Transgenic Res ; 14(6): 803-6, 2005 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-16315087

RESUMO

Humanized mice are crucial tools for studying human pathogens in systemic situations. An animal model of human coronavirus infectious disease has been generated by gene transfer of the human receptor for virus-cell interaction (aminopeptidase N, APN, CD13) into mice. We showed that in vitro and in vivo infections across the species barrier differ in their requirements. Transgenic cells were susceptible to human coronavirus HCoV-229E infection demonstrating the requirement of hAPN for viral cell entry. Transgenic mice, however, could not be infected suggesting additional requirements for in vivo virus susceptibility. Crossing hAPN transgenic mice with interferon unresponsive Stat1(-/- )mice resulted in markedly enhanced virus replication in vitro but did not result in detectable virus replication in vivo. Adaptation of the human virus to murine cells led to successful infection of the humanized transgenic mice. Future genetic engineering approaches are suggested to provide animal models for the better understanding of human infectious diseases.


Assuntos
Antígenos CD13/genética , Coronavirus Humano 229E/patogenicidade , Infecções por Coronavirus/genética , Modelos Animais de Doenças , Animais , Suscetibilidade a Doenças , Humanos , Camundongos , Camundongos Transgênicos , Receptores Virais/genética , Transgenes/genética , Replicação Viral
15.
Proc Natl Acad Sci U S A ; 102(23): 8275-80, 2005 Jun 07.
Artigo em Inglês | MEDLINE | ID: mdl-15919828

RESUMO

Human coronavirus (HCoV) 229E is a group 1 coronavirus and is specific to humans. So far, no animal model is available to study the pathogenesis of infection by HCoV-229E. We show here that the expression of aminopeptidase N (APN, also termed CD13), the receptor for HCoV-229E, is required but not sufficient to confer susceptibility in vivo. HCoV-229E infection was facilitated by crossing APN transgenic mice into signal transducers and activators of transcription (Stat) 1 null mice and by adaptation of HCoV-229E to grow in primary APN transgenic, Stat1 null fibroblasts. Double transgenic mice allow the study of human coronavirus group 1 infections in an animal model, in particular, viral tropism, replication, recombination, and spread in an immunocompromised situation. Furthermore, these mice provide an important tool for the evaluation of biosafety and efficacy of coronavirus-based vectors.


Assuntos
Antígenos CD13/metabolismo , Coronavirus Humano 229E/fisiologia , Modelos Animais de Doenças , Suscetibilidade a Doenças , Receptores Virais/metabolismo , Animais , Antígenos CD13/genética , Células Cultivadas , Coronavirus Humano 229E/genética , Coronavirus Humano 229E/patogenicidade , Fibroblastos , Genótipo , Humanos , Camundongos , Camundongos Transgênicos , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Receptores Virais/genética , Recombinação Genética/genética , Especificidade da Espécie , Transgenes/genética , Replicação Viral
16.
Med Microbiol Immunol ; 194(1-2): 1-6, 2005 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-15118911

RESUMO

The SARS-coronavirus (SARS-CoV) is a newly emerged, highly pathogenic agent that caused over 8,000 human infections with nearly 800 deaths between November 2002 and September 2003. While direct person-to-person transmission via respiratory droplets accounted for most cases, other modes have not been ruled out. Faecal shedding is common and prolonged and has caused an outbreak in Hong Kong. We studied the stability of SARS-CoV under different conditions, both in suspension and dried on surfaces, in comparison with other human-pathogenic viruses, including human coronavirus HCoV-229E. In suspension, HCoV-229E gradually lost its infectivity completely while SARS-CoV retained its infectivity for up to 9 days; in the dried state, survival times were 24 h versus 6 days. Thermal inactivation at 56 degrees C was highly effective in the absence of protein, reducing the virus titre to below detectability; however, the addition of 20% protein exerted a protective effect resulting in residual infectivity. If protein-containing solutions are to be inactivated, heat treatment at 60 degrees C for at least 30 min must be used. Different fixation procedures, e.g. for the preparation of immunofluorescence slides, as well as chemical means of virus inactivation commonly used in hospital and laboratory settings were generally found to be effective. Our investigations confirm that it is possible to care for SARS patients and to conduct laboratory scientific studies on SARS-CoV safely. Nevertheless, the agents tenacity is considerably higher than that of HCoV-229E, and should SARS re-emerge, increased efforts need to be devoted to questions of environmental hygiene.


Assuntos
Desinfecção/métodos , Vírus da SARS , Animais , Coronavirus Humano 229E/efeitos dos fármacos , Coronavirus Humano 229E/crescimento & desenvolvimento , Coronavirus Humano 229E/patogenicidade , Desinfetantes/química , Desinfetantes/farmacologia , Temperatura Alta , Humanos , Vírus da SARS/efeitos dos fármacos , Vírus da SARS/crescimento & desenvolvimento , Vírus da SARS/patogenicidade , Células Vero/virologia
17.
J Virol ; 78(16): 8701-8, 2004 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-15280478

RESUMO

CD13, a receptor for human coronavirus 229E (HCoV-229E), was identified as a major component of the Triton X-100-resistant membrane microdomain in human fibroblasts. The incubation of living fibroblasts with an anti-CD13 antibody on ice gave punctate labeling that was evenly distributed on the cell surface, but raising the temperature to 37 degrees C before fixation caused aggregation of the labeling. The aggregated labeling of CD13 colocalized with caveolin-1 in most cells. The HCoV-229E virus particle showed a binding and redistribution pattern that was similar to that caused by the anti-CD13 antibody: the virus bound to the cell evenly when incubated on ice but became colocalized with caveolin-1 at 37 degrees C; importantly, the virus also caused sequestration of CD13 to the caveolin-1-positive area. Electron microscopy confirmed that HCoV-229E was localized near or at the orifice of caveolae after incubation at 37 degrees C. The depletion of plasmalemmal cholesterol with methyl beta-cyclodextrin significantly reduced the HCoV-229E redistribution and subsequent infection. A caveolin-1 knockdown by RNA interference also reduced the HCoV-229E infection considerably. The results indicate that HCoV-229E first binds to CD13 in the Triton X-100-resistant microdomain, then clusters CD13 by cross-linking, and thereby reaches the caveolar region before entering cells.


Assuntos
Antígenos CD13/metabolismo , Cavéolas/virologia , Coronavirus Humano 229E/patogenicidade , Microdomínios da Membrana/metabolismo , Sequência de Aminoácidos , Animais , Caveolina 1 , Caveolinas/genética , Caveolinas/metabolismo , Células Cultivadas , Coronavirus Humano 229E/metabolismo , Fibroblastos/virologia , Humanos , Microscopia Eletrônica , Microscopia de Fluorescência , Dados de Sequência Molecular , Interferência de RNA , RNA Interferente Pequeno , Receptores Virais/metabolismo , Pele/citologia
18.
BMC Bioinformatics ; 5: 72, 2004 Jun 06.
Artigo em Inglês | MEDLINE | ID: mdl-15180906

RESUMO

BACKGROUND: Despite the passing of more than a year since the first outbreak of Severe Acute Respiratory Syndrome (SARS), efficient counter-measures are still few and many believe that reappearance of SARS, or a similar disease caused by a coronavirus, is not unlikely. For other virus families like the picornaviruses it is known that pathology is related to proteolytic cleavage of host proteins by viral proteinases. Furthermore, several studies indicate that virus proliferation can be arrested using specific proteinase inhibitors supporting the belief that proteinases are indeed important during infection. Prompted by this, we set out to analyse and predict cleavage by the coronavirus main proteinase using computational methods. RESULTS: We retrieved sequence data on seven fully sequenced coronaviruses and identified the main 3CL proteinase cleavage sites in polyproteins using alignments. A neural network was trained to recognise the cleavage sites in the genomes obtaining a sensitivity of 87.0% and a specificity of 99.0%. Several proteins known to be cleaved by other viruses were submitted to prediction as well as proteins suspected relevant in coronavirus pathology. Cleavage sites were predicted in proteins such as the cystic fibrosis transmembrane conductance regulator (CFTR), transcription factors CREB-RP and OCT-1, and components of the ubiquitin pathway. CONCLUSIONS: Our prediction method NetCorona predicts coronavirus cleavage sites with high specificity and several potential cleavage candidates were identified which might be important to elucidate coronavirus pathology. Furthermore, the method might assist in design of proteinase inhibitors for treatment of SARS and possible future diseases caused by coronaviruses. It is made available for public use at our website: http://www.cbs.dtu.dk/services/NetCorona/.


Assuntos
Cisteína Endopeptidases/metabolismo , Proteínas/metabolismo , Vírus da SARS/enzimologia , Síndrome Respiratória Aguda Grave/patologia , Inteligência Artificial , Sítios de Ligação/genética , Coronavirus Humano 229E/enzimologia , Coronavirus Humano 229E/patogenicidade , Humanos , Vírus da SARS/patogenicidade , Análise de Sequência de DNA/métodos , Síndrome Respiratória Aguda Grave/virologia
19.
J Virol ; 77(7): 4435-8, 2003 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-12634402

RESUMO

Truncated human coronavirus HCoV-229E spike glycoproteins containing amino acids 407 to 547 bound to purified, soluble virus receptor, human aminopeptidase N (hAPN). Soluble hAPN neutralized the infectivity of HCoV-229E virions at 37 degrees C, but not 4 degrees C. Binding of hAPN may therefore trigger conformational changes in the viral spike protein at 37 degrees C that facilitate virus entry.


Assuntos
Antígenos CD13/fisiologia , Coronavirus Humano 229E/fisiologia , Coronavirus Humano 229E/patogenicidade , Receptores Virais/fisiologia , Sequência de Aminoácidos , Animais , Sítios de Ligação , Antígenos CD13/química , Antígenos CD13/genética , Linhagem Celular , Coronavirus Humano 229E/genética , Humanos , Glicoproteínas de Membrana/química , Glicoproteínas de Membrana/genética , Glicoproteínas de Membrana/fisiologia , Ligação Proteica , Conformação Proteica , Estrutura Terciária de Proteína , Receptores Virais/química , Receptores Virais/genética , Deleção de Sequência , Solubilidade , Glicoproteína da Espícula de Coronavírus , Proteínas do Envelope Viral/química , Proteínas do Envelope Viral/genética , Proteínas do Envelope Viral/fisiologia
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