Assays with recombinant soluble isoforms of DC-SIGN, a dengue virus ligand, show variation in their ability to bind to mannose residues

The DC-SIGN glycoprotein is responsible for the initial adhesion of dengue virus (DENV) to immune cells by the carbohydrate recognition domain (CRD). There are thirteen soluble and membrane-bound DC-SIGN isoforms, but the role of soluble isoforms in the DENV internalization process is not known. Fiv...

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Published inArchives of virology Vol. 164; no. 11; pp. 2793 - 2797
Main Authors Pereira, Lailah Horácio Sales, de Souza, Thaís Paiva Porto, Camargos, Vidyleison Neves, de Oliveira Barbosa, Leandro Augusto, Taranto, Alex Guterres, Junior, Moacyr Comar, de Lima Santos, Hérica, de Oliveira Lopes, Débora, Ferreira, Jaqueline Maria Siqueira, dos Santos, Luciana Lara
Format Journal Article
LanguageEnglish
Published Vienna Springer Vienna 01.11.2019
Springer Nature B.V
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Abstract The DC-SIGN glycoprotein is responsible for the initial adhesion of dengue virus (DENV) to immune cells by the carbohydrate recognition domain (CRD). There are thirteen soluble and membrane-bound DC-SIGN isoforms, but the role of soluble isoforms in the DENV internalization process is not known. Five isoforms with an altered or absent CRD were identified, and three different soluble isoforms were used to confirm the interactions with mannose residues. The results show the loss of binding ability of one soluble isoform and binding ability of two of them. All of them will be used to verify their role in the DENV internalization process.
AbstractList The DC-SIGN glycoprotein is responsible for the initial adhesion of dengue virus (DENV) to immune cells by the carbohydrate recognition domain (CRD). There are thirteen soluble and membrane-bound DC-SIGN isoforms, but the role of soluble isoforms in the DENV internalization process is not known. Five isoforms with an altered or absent CRD were identified, and three different soluble isoforms were used to confirm the interactions with mannose residues. The results show the loss of binding ability of one soluble isoform and binding ability of two of them. All of them will be used to verify their role in the DENV internalization process.
Author Junior, Moacyr Comar
Taranto, Alex Guterres
de Oliveira Barbosa, Leandro Augusto
de Oliveira Lopes, Débora
dos Santos, Luciana Lara
Camargos, Vidyleison Neves
de Lima Santos, Hérica
Ferreira, Jaqueline Maria Siqueira
Pereira, Lailah Horácio Sales
de Souza, Thaís Paiva Porto
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  givenname: Lailah Horácio Sales
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  givenname: Thaís Paiva Porto
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  fullname: de Oliveira Barbosa, Leandro Augusto
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  givenname: Hérica
  surname: de Lima Santos
  fullname: de Lima Santos, Hérica
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  givenname: Débora
  surname: de Oliveira Lopes
  fullname: de Oliveira Lopes, Débora
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  givenname: Jaqueline Maria Siqueira
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  givenname: Luciana Lara
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  surname: dos Santos
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  email: llaramg@hotmail.com
  organization: Laboratory of Molecular Biology, Universidade Federal de São João Del Rei (UFSJ)
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Snippet The DC-SIGN glycoprotein is responsible for the initial adhesion of dengue virus (DENV) to immune cells by the carbohydrate recognition domain (CRD). There are...
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SubjectTerms Biomedical and Life Sciences
Biomedicine
Brief Report
DC-SIGN protein
Dengue fever
Infectious Diseases
Internalization
Isoforms
Mannose
Medical Microbiology
Virology
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Title Assays with recombinant soluble isoforms of DC-SIGN, a dengue virus ligand, show variation in their ability to bind to mannose residues
URI https://link.springer.com/article/10.1007/s00705-019-04377-9
https://www.ncbi.nlm.nih.gov/pubmed/31440811
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Volume 164
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