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Master's Dissertation
DOI
10.11606/D.17.2017.tde-21072016-162417
Document
Author
Full name
Ricardo de Souza Cardoso
E-mail
Institute/School/College
Knowledge Area
Date of Defense
Published
Ribeirão Preto, 2016
Supervisor
Committee
Arruda Neto, Eurico de (President)
Osako, Mariana Kiomy
Torrecilhas, Ana Cláudia Trócoli
Title in Portuguese
Participação de proteínas da via secretória no tráfego e montagem do vírus sincicial respiratório
Keywords in Portuguese
Corpos de inclusão
HRSV
Incorporação de proteínas celulares no vírus
Secretória
Sorting nexin 2 (SNX2)
Tráfego intracelular de proteínas virais
Trans-Golgi Network 46 (TGN46)
Abstract in Portuguese
O vírus sincicial respiratório humano (HRSV) é o mais frequente agente patogênico da família Paramyxoviridae. Apesar de sua grande importância e impacto em saúde pública, alguns aspectos demandam elucidação. Entre eles, estão os mecanismos de tráfego intracelular de proteínas virais para o sitio de montagem. Baseado nisso, fizemos um estudo de imunofluorescência tentando contribuir para o entendimento da participação da via secretória no tráfego de proteínas estruturais de HRSV que não são glicosiladas: proteínas de matriz (M) e de nucleocapsídeo (N). Pudemos observar que essas proteínas seguem rota similar àquelas que são glicosiladas no Golgi, como a proteína de fusão (F). Ademais, as proteínas M e N, além de colocalizarem com proteínas celulares da via secretória, tais como trans-Golgi network-46 (TGN46) e sorting nexin-2 (SNX2), também influem no recrutamento de proteínas celulares para os corpos de inclusão virais, como mostrado no caso da proteína Glut1. Os dados indicam que proteínas M e N de HRSV seguem pela via endocítica inicial, acumulam-se em corpos de inclusão que seriam fábricas virais e, no caso de TGN46, podem ser incorporadas aos vírus em brotamento
Title in English
Participation of proteins in secretory route traffic and assembling of respiratory syncytial virus
Keywords in English
Cell proteins associated with vírus particle
Early endosome
Human respiratory syncytial virus
Inclusion body
Intracellular trafficking of the viral proteins
Sorting nexin 2 (SNX2)
Trans-Golgi Network 46 (TGN46)
Abstract in English
Human respiratory syncytial virus (HRSV) is the most relevant cause of respiratory infection in children worldwide. Despite its importance in public health, some aspects of the mechanisms of the trafficking of viral structural proteins remain unclear. In the present study, immunofluorescence was used to understand how the virus matrix (M) and nucleocapsid (N) proteins, which are non-glycosylated , are addressed to inclusion bodies in Hep-2 cells (MOI=3). M and N proteins followed similar intracellular trafficking routes as compared to the glycosylated fusion (F) viral protein. Moreover, M and N proteins colocalized with two key elements of the secretory pathway: trans-Golgi network- 46 (TGN46) and sorting nexin-2 (SNX2). Viral proteins M and N appear to be involved in the recruitment of cell proteins at the formation of virus inclusion bodies, as shown for Glucose Transporter Type 1 (Glut1). The data suggest that HRSV M and N proteins follow the secretory pathway, initiating in early endosomes, as indicated by the co-localization with TGN46 and SNX2. In addition, these host cell proteins accumulate in inclusion bodies that are viral factories, and can be part of budding viral progeny. Therefore, HRSV M and N proteins, even though they are not glycosylated, take advantage of the secretory pathway to reach virus inclusion bodies. Confocal images suggest that SNX2, which is known for its membrane-deforming properties, could play a pivotal role in HRSV budding
 
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Publishing Date
2017-08-15
 
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