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SARS Accessory Proteins ORF3a and 9b and Their Functional Analysis

The SARS coronavirus (CoV) positive-stranded RNA viral genome encodes 14 open reading frames (ORFs), eight of which encode proteins termed as “accessory proteins.” These proteins help the virus infect the host and promote virulence. In this chapter we describe some of our latest investigations into...

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Autores principales: Lu, Wei, Xu, Ke, Sun, Bing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7123986/
http://dx.doi.org/10.1007/978-3-642-03683-5_11
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author Lu, Wei
Xu, Ke
Sun, Bing
author_facet Lu, Wei
Xu, Ke
Sun, Bing
author_sort Lu, Wei
collection PubMed
description The SARS coronavirus (CoV) positive-stranded RNA viral genome encodes 14 open reading frames (ORFs), eight of which encode proteins termed as “accessory proteins.” These proteins help the virus infect the host and promote virulence. In this chapter we describe some of our latest investigations into the structure and function of two such accessory proteins: ORF3a and 9b. The ORF3a accessory protein is the largest accessory protein in SARS-CoV and is a unique membrane protein consisting of three transmembrane domains. It colocalizes on the cell membrane and host Golgi networks and may be involved in ion channel formation during infection. Similarly the ORF9b accessory protein is 98 amino acids, associates with the spike and nucleocapsid proteins and has unusual membrane binding properties. In this chapter we have suggested possible new roles for these two accessory proteins which may in the long run contain answers to many unanswered questions and also give us new ideas for drugs and vaccine design.
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spelling pubmed-71239862020-04-06 SARS Accessory Proteins ORF3a and 9b and Their Functional Analysis Lu, Wei Xu, Ke Sun, Bing Molecular Biology of the SARS-Coronavirus Article The SARS coronavirus (CoV) positive-stranded RNA viral genome encodes 14 open reading frames (ORFs), eight of which encode proteins termed as “accessory proteins.” These proteins help the virus infect the host and promote virulence. In this chapter we describe some of our latest investigations into the structure and function of two such accessory proteins: ORF3a and 9b. The ORF3a accessory protein is the largest accessory protein in SARS-CoV and is a unique membrane protein consisting of three transmembrane domains. It colocalizes on the cell membrane and host Golgi networks and may be involved in ion channel formation during infection. Similarly the ORF9b accessory protein is 98 amino acids, associates with the spike and nucleocapsid proteins and has unusual membrane binding properties. In this chapter we have suggested possible new roles for these two accessory proteins which may in the long run contain answers to many unanswered questions and also give us new ideas for drugs and vaccine design. 2009-07-22 /pmc/articles/PMC7123986/ http://dx.doi.org/10.1007/978-3-642-03683-5_11 Text en © Springer-Verlag Berlin Heidelberg 2010 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Lu, Wei
Xu, Ke
Sun, Bing
SARS Accessory Proteins ORF3a and 9b and Their Functional Analysis
title SARS Accessory Proteins ORF3a and 9b and Their Functional Analysis
title_full SARS Accessory Proteins ORF3a and 9b and Their Functional Analysis
title_fullStr SARS Accessory Proteins ORF3a and 9b and Their Functional Analysis
title_full_unstemmed SARS Accessory Proteins ORF3a and 9b and Their Functional Analysis
title_short SARS Accessory Proteins ORF3a and 9b and Their Functional Analysis
title_sort sars accessory proteins orf3a and 9b and their functional analysis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7123986/
http://dx.doi.org/10.1007/978-3-642-03683-5_11
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