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
Subjects
Biomedical and Life Sciences
Biomedicine
Brief Report
DC-SIGN protein
Dengue fever
Infectious Diseases
Internalization
Isoforms
Mannose
Medical Microbiology
Virology
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Summary: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.
ISSN:0304-8608
1432-8798
DOI:10.1007/s00705-019-04377-9