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

Lailah Horácio Sales Pereira, Thaís Paiva Porto de Souza, Vidyleison Neves Camargos, Leandro Augusto de Oliveira Barbosa, Alex Guterres Taranto, Moacyr Comar Junior, Hérica de Lima Santos, Débora de Oliveira Lopes, Jaqueline Maria Siqueira Ferreira, Luciana Lara dos Santos

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)2793-2797
Number of pages5
JournalArchives of virology
Volume164
Issue number11
DOIs
StatePublished - Nov 1 2019
Externally publishedYes

ASJC Scopus subject areas

  • Virology

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