Secreted NS1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate E

Dengue virus (DENV) nonstructural protein-1 (NS1) is a secreted glycoprotein that is absent from viral particles but accumulates in the supernatant and on the plasma membrane of cells during infection. Immune recognition of cell surface NS1 on endothelial cells has been hypothesized as a mechanism f...

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Main Authors: Panisadee Avirutnan, Lijuan Zhang, Nuntaya Punyadee, Ananya Manuyakorn, Chunya Puttikhunt, Watchara Kasinrerk, Prida Malasit, John P. Atkinson, Michael S. Diamond
Format: Journal
Published: 2018
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http://cmuir.cmu.ac.th/jspui/handle/6653943832/60881
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spelling th-cmuir.6653943832-608812018-09-10T04:05:01Z Secreted NS1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate E Panisadee Avirutnan Lijuan Zhang Nuntaya Punyadee Ananya Manuyakorn Chunya Puttikhunt Watchara Kasinrerk Prida Malasit John P. Atkinson Michael S. Diamond Biochemistry, Genetics and Molecular Biology Immunology and Microbiology Dengue virus (DENV) nonstructural protein-1 (NS1) is a secreted glycoprotein that is absent from viral particles but accumulates in the supernatant and on the plasma membrane of cells during infection. Immune recognition of cell surface NS1 on endothelial cells has been hypothesized as a mechanism for the vascular leakage that occurs during severe DENV infection. However, it has remained unclear how NS1 becomes associated with the plasma membrane, as it contains no membrane-spanning sequence motif. Using flow cytometric and ELISA-based binding assays and mutant cell lines lacking selective glycosaminoglycans, we show that soluble NS1 binds back to the surface of uninfected cells primarily via interactions with heparan sulfate and chondroitin sulfate E. DENV NS1 binds directly to the surface of many types of epithelial and mesenchymal cells yet attaches poorly to most peripheral blood cells. Moreover, DENV NS1 preferentially binds to cultured human microvascular compared to aortic or umbilical cord vein endothelial cells. This binding specificity was confirmed in situ as DENV NS1 bound to lung and liver but not intestine or brain endothelium of mouse tissues. Differential binding of soluble NS1 by tissue endothelium and subsequent recognition by anti-NS1 antibodies could contribute to the selective vascular leakage syndrome that occurs during severe secondary DENV infection. © 2007 Avirutnan et al. 2018-09-10T04:00:44Z 2018-09-10T04:00:44Z 2007-11-01 Journal 15537374 15537366 2-s2.0-37349077213 10.1371/journal.ppat.0030183 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=37349077213&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/60881
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
topic Biochemistry, Genetics and Molecular Biology
Immunology and Microbiology
spellingShingle Biochemistry, Genetics and Molecular Biology
Immunology and Microbiology
Panisadee Avirutnan
Lijuan Zhang
Nuntaya Punyadee
Ananya Manuyakorn
Chunya Puttikhunt
Watchara Kasinrerk
Prida Malasit
John P. Atkinson
Michael S. Diamond
Secreted NS1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate E
description Dengue virus (DENV) nonstructural protein-1 (NS1) is a secreted glycoprotein that is absent from viral particles but accumulates in the supernatant and on the plasma membrane of cells during infection. Immune recognition of cell surface NS1 on endothelial cells has been hypothesized as a mechanism for the vascular leakage that occurs during severe DENV infection. However, it has remained unclear how NS1 becomes associated with the plasma membrane, as it contains no membrane-spanning sequence motif. Using flow cytometric and ELISA-based binding assays and mutant cell lines lacking selective glycosaminoglycans, we show that soluble NS1 binds back to the surface of uninfected cells primarily via interactions with heparan sulfate and chondroitin sulfate E. DENV NS1 binds directly to the surface of many types of epithelial and mesenchymal cells yet attaches poorly to most peripheral blood cells. Moreover, DENV NS1 preferentially binds to cultured human microvascular compared to aortic or umbilical cord vein endothelial cells. This binding specificity was confirmed in situ as DENV NS1 bound to lung and liver but not intestine or brain endothelium of mouse tissues. Differential binding of soluble NS1 by tissue endothelium and subsequent recognition by anti-NS1 antibodies could contribute to the selective vascular leakage syndrome that occurs during severe secondary DENV infection. © 2007 Avirutnan et al.
format Journal
author Panisadee Avirutnan
Lijuan Zhang
Nuntaya Punyadee
Ananya Manuyakorn
Chunya Puttikhunt
Watchara Kasinrerk
Prida Malasit
John P. Atkinson
Michael S. Diamond
author_facet Panisadee Avirutnan
Lijuan Zhang
Nuntaya Punyadee
Ananya Manuyakorn
Chunya Puttikhunt
Watchara Kasinrerk
Prida Malasit
John P. Atkinson
Michael S. Diamond
author_sort Panisadee Avirutnan
title Secreted NS1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate E
title_short Secreted NS1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate E
title_full Secreted NS1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate E
title_fullStr Secreted NS1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate E
title_full_unstemmed Secreted NS1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate E
title_sort secreted ns1 of dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate e
publishDate 2018
url https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=37349077213&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/60881
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