SrasV1, PubMed, Checkpoint, bibRecord, 000B52

Beyond attachment: Roles of DC-SIGN in dengue virus infection.

Identifieur interne : 000B52 ( PubMed/Checkpoint ); précédent : 000B51; suivant : 000B53

Beyond attachment: Roles of DC-SIGN in dengue virus infection.

Auteurs : Ping Liu [États-Unis] ; Marc Ridilla [États-Unis] ; Pratik Patel [États-Unis] ; Laurie Betts [États-Unis] ; Emily Gallichotte [États-Unis] ; Lidea Shahidi [États-Unis] ; Nancy L. Thompson [États-Unis] ; Ken Jacobson [États-Unis]

Source :

Traffic (Copenhagen, Denmark) [ 1600-0854 ] ; 2017.

RBID : pubmed:28128492

Descripteurs français

KwdFr :
- Animaux, Cellules NIH 3T3, Cellules dendritiques (métabolisme), Dengue (métabolisme), Dengue (virologie), Endocytose (physiologie), Lectines de type C (métabolisme), Lignée cellulaire, Membrane cellulaire (métabolisme), Molécules d'adhérence cellulaire (métabolisme), Récepteurs de surface cellulaire (métabolisme), Souris, Virus de la dengue (pathogénicité).
MESH :
- métabolisme : Cellules dendritiques, Dengue, Lectines de type C, Membrane cellulaire, Molécules d'adhérence cellulaire, Récepteurs de surface cellulaire.
- pathogénicité : Virus de la dengue.
- physiologie : Endocytose.
- virologie : Dengue.
- Animaux, Cellules NIH 3T3, Lignée cellulaire, Souris.

English descriptors

KwdEn :
- Animals, Cell Adhesion Molecules (metabolism), Cell Line, Cell Membrane (metabolism), Dendritic Cells (metabolism), Dengue (metabolism), Dengue (virology), Dengue Virus (pathogenicity), Endocytosis (physiology), Lectins, C-Type (metabolism), Mice, NIH 3T3 Cells, Receptors, Cell Surface (metabolism).
MESH :
- chemical , metabolism : Cell Adhesion Molecules, Lectins, C-Type, Receptors, Cell Surface.
- metabolism : Cell Membrane, Dendritic Cells, Dengue.
- pathogenicity : Dengue Virus.
- physiology : Endocytosis.
- virology : Dengue.
- Animals, Cell Line, Mice, NIH 3T3 Cells.

Abstract

Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), a C-type lectin expressed on the plasma membrane by human immature dendritic cells, is a receptor for numerous viruses including Ebola, SARS and dengue. A controversial question has been whether DC-SIGN functions as a complete receptor for both binding and internalization of dengue virus (DENV) or whether it is solely a cell surface attachment factor, requiring either hand-off to another receptor or a co-receptor for internalization. To examine this question, we used 4 cell types: human immature dendritic cells and NIH3T3 cells expressing either wild-type DC-SIGN or 2 internalization-deficient DC-SIGN mutants, in which either the 3 cytoplasmic internalization motifs are silenced by alanine substitutions or the cytoplasmic region is truncated. Using confocal and super-resolution imaging and high content single particle tracking, we investigated DENV binding, DC-SIGN surface transport, endocytosis, as well as cell infectivity. DC-SIGN was found colocalized with DENV inside cells suggesting hand-off at the plasma membrane to another receptor did not occur. Moreover, all 3 DC-SIGN molecules on NIH3T3 cells supported cell infection. These results imply the involvement of a co-receptor because cells expressing the internalization-deficient mutants could still be infected.

DOI: 10.1111/tra.12469
PubMed: 28128492

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), a C-type lectin expressed on the plasma membrane by human immature dendritic cells, is a receptor for numerous viruses including Ebola, SARS and dengue. A controversial question has been whether DC-SIGN functions as a complete receptor for both binding and internalization of dengue virus (DENV) or whether it is solely a cell surface attachment factor, requiring either hand-off to another receptor or a co-receptor for internalization. To examine this question, we used 4 cell types: human immature dendritic cells and NIH3T3 cells expressing either wild-type DC-SIGN or 2 internalization-deficient DC-SIGN mutants, in which either the 3 cytoplasmic internalization motifs are silenced by alanine substitutions or the cytoplasmic region is truncated. Using confocal and super-resolution imaging and high content single particle tracking, we investigated DENV binding, DC-SIGN surface transport, endocytosis, as well as cell infectivity. DC-SIGN was found colocalized with DENV inside cells suggesting hand-off at the plasma membrane to another receptor did not occur. Moreover, all 3 DC-SIGN molecules on NIH3T3 cells supported cell infection. These results imply the involvement of a co-receptor because cells expressing the internalization-deficient mutants could still be infected.</div>
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<Abstract><AbstractText>Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), a C-type lectin expressed on the plasma membrane by human immature dendritic cells, is a receptor for numerous viruses including Ebola, SARS and dengue. A controversial question has been whether DC-SIGN functions as a complete receptor for both binding and internalization of dengue virus (DENV) or whether it is solely a cell surface attachment factor, requiring either hand-off to another receptor or a co-receptor for internalization. To examine this question, we used 4 cell types: human immature dendritic cells and NIH3T3 cells expressing either wild-type DC-SIGN or 2 internalization-deficient DC-SIGN mutants, in which either the 3 cytoplasmic internalization motifs are silenced by alanine substitutions or the cytoplasmic region is truncated. Using confocal and super-resolution imaging and high content single particle tracking, we investigated DENV binding, DC-SIGN surface transport, endocytosis, as well as cell infectivity. DC-SIGN was found colocalized with DENV inside cells suggesting hand-off at the plasma membrane to another receptor did not occur. Moreover, all 3 DC-SIGN molecules on NIH3T3 cells supported cell infection. These results imply the involvement of a co-receptor because cells expressing the internalization-deficient mutants could still be infected.</AbstractText>
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Beyond attachment: Roles of DC-SIGN in dengue virus infection.

Beyond attachment: Roles of DC-SIGN in dengue virus infection.

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