Sulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III.

Dengue virus (DENV) is an emerging mosquito-borne pathogen that causes cytokine-mediated alterations in the barrier function of the microvascular endothelium, leading to dengue hemorrhagic fever (DHF) and dengue shock syndrome (DSS). We observed that DENV (serotype 2) productively infects primary (H...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Peter Vervaeke, Marijke Alen, Sam Noppen, Dominique Schols, Pasqua Oreste, Sandra Liekens
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2013
Materias:
R
Q
Acceso en línea:https://doaj.org/article/be2f1b3ec7084da8aeebde707f98286c
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:be2f1b3ec7084da8aeebde707f98286c
record_format dspace
spelling oai:doaj.org-article:be2f1b3ec7084da8aeebde707f98286c2021-11-18T08:57:48ZSulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III.1932-620310.1371/journal.pone.0074035https://doaj.org/article/be2f1b3ec7084da8aeebde707f98286c2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24015314/?tool=EBIhttps://doaj.org/toc/1932-6203Dengue virus (DENV) is an emerging mosquito-borne pathogen that causes cytokine-mediated alterations in the barrier function of the microvascular endothelium, leading to dengue hemorrhagic fever (DHF) and dengue shock syndrome (DSS). We observed that DENV (serotype 2) productively infects primary (HMVEC-d) and immortalized (HMEC-1) human dermal microvascular endothelial cells, despite the absence of well-described DENV receptors, such as dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) or the mannose receptor on the cell surface. However, heparan sulfate proteoglycans (HSPGs) were highly expressed on these cells and pre-treatment of HMEC-1 cells with heparinase II or with glycosaminoglycans reduced DENV infectivity up to 90%, suggesting that DENV uses HSPGs as attachment receptor on microvascular endothelial cells. Sulfated Escherichia coli K5 derivatives, which are structurally similar to heparin/heparan sulfate but lack anticoagulant activity, were able to block DENV infection of HMEC-1 and HMVEC-d cells in the nanomolar range. The highly sulfated K5-OS(H) and K5-N,OS(H) inhibited virus attachment and subsequent entry into microvascular endothelial cells by interacting with the viral envelope (E) protein, as shown by surface plasmon resonance (SPR) analysis using the receptor-binding domain III of the E protein.Peter VervaekeMarijke AlenSam NoppenDominique ScholsPasqua OresteSandra LiekensPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e74035 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Peter Vervaeke
Marijke Alen
Sam Noppen
Dominique Schols
Pasqua Oreste
Sandra Liekens
Sulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III.
description Dengue virus (DENV) is an emerging mosquito-borne pathogen that causes cytokine-mediated alterations in the barrier function of the microvascular endothelium, leading to dengue hemorrhagic fever (DHF) and dengue shock syndrome (DSS). We observed that DENV (serotype 2) productively infects primary (HMVEC-d) and immortalized (HMEC-1) human dermal microvascular endothelial cells, despite the absence of well-described DENV receptors, such as dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) or the mannose receptor on the cell surface. However, heparan sulfate proteoglycans (HSPGs) were highly expressed on these cells and pre-treatment of HMEC-1 cells with heparinase II or with glycosaminoglycans reduced DENV infectivity up to 90%, suggesting that DENV uses HSPGs as attachment receptor on microvascular endothelial cells. Sulfated Escherichia coli K5 derivatives, which are structurally similar to heparin/heparan sulfate but lack anticoagulant activity, were able to block DENV infection of HMEC-1 and HMVEC-d cells in the nanomolar range. The highly sulfated K5-OS(H) and K5-N,OS(H) inhibited virus attachment and subsequent entry into microvascular endothelial cells by interacting with the viral envelope (E) protein, as shown by surface plasmon resonance (SPR) analysis using the receptor-binding domain III of the E protein.
format article
author Peter Vervaeke
Marijke Alen
Sam Noppen
Dominique Schols
Pasqua Oreste
Sandra Liekens
author_facet Peter Vervaeke
Marijke Alen
Sam Noppen
Dominique Schols
Pasqua Oreste
Sandra Liekens
author_sort Peter Vervaeke
title Sulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III.
title_short Sulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III.
title_full Sulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III.
title_fullStr Sulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III.
title_full_unstemmed Sulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III.
title_sort sulfated escherichia coli k5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein e domain iii.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/be2f1b3ec7084da8aeebde707f98286c
work_keys_str_mv AT petervervaeke sulfatedescherichiacolik5polysaccharidederivativesinhibitdenguevirusinfectionofhumanmicrovascularendothelialcellsbyinteractingwiththeviralenvelopeproteinedomainiii
AT marijkealen sulfatedescherichiacolik5polysaccharidederivativesinhibitdenguevirusinfectionofhumanmicrovascularendothelialcellsbyinteractingwiththeviralenvelopeproteinedomainiii
AT samnoppen sulfatedescherichiacolik5polysaccharidederivativesinhibitdenguevirusinfectionofhumanmicrovascularendothelialcellsbyinteractingwiththeviralenvelopeproteinedomainiii
AT dominiqueschols sulfatedescherichiacolik5polysaccharidederivativesinhibitdenguevirusinfectionofhumanmicrovascularendothelialcellsbyinteractingwiththeviralenvelopeproteinedomainiii
AT pasquaoreste sulfatedescherichiacolik5polysaccharidederivativesinhibitdenguevirusinfectionofhumanmicrovascularendothelialcellsbyinteractingwiththeviralenvelopeproteinedomainiii
AT sandraliekens sulfatedescherichiacolik5polysaccharidederivativesinhibitdenguevirusinfectionofhumanmicrovascularendothelialcellsbyinteractingwiththeviralenvelopeproteinedomainiii
_version_ 1718421107427508224