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Mannosyl glycodendritic structure inhibits DC-SIGN-mediated Ebola virus infection in cis and in trans.

Abstract
We have designed a glycodendritic structure, BH30sucMan, that blocks the interaction between dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) and Ebola virus (EBOV) envelope. BH30sucMan inhibits DC-SIGN-mediated EBOV infection at nanomolar concentrations. BH30sucMan may counteract important steps of the infective process of EBOV and, potentially, of microorganisms shown to exploit DC-SIGN for cell entry and infection.
AuthorsFátima Lasala, Eva Arce, Joaquín R Otero, Javier Rojo, Rafael Delgado
JournalAntimicrobial agents and chemotherapy (Antimicrob Agents Chemother) Vol. 47 Issue 12 Pg. 3970-2 (Dec 2003) ISSN: 0066-4804 [Print] United States
PMID14638512 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Antiviral Agents
  • BH30sucMan
  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • Lectins, C-Type
  • Mannans
  • Receptors, Cell Surface
  • Viral Envelope Proteins
Topics
  • Antiviral Agents (chemical synthesis, pharmacology)
  • Cell Adhesion Molecules (drug effects)
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Drug Design
  • Ebolavirus (drug effects, growth & development)
  • Hemorrhagic Fever, Ebola (drug therapy, virology)
  • Humans
  • Lectins, C-Type (drug effects)
  • Lentivirus (genetics)
  • Mannans (chemical synthesis, pharmacology)
  • Receptors, Cell Surface (drug effects)
  • Stereoisomerism
  • Vesicular stomatitis Indiana virus (drug effects, growth & development)
  • Viral Envelope Proteins (chemistry, drug effects)

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