Evidence that multiple defects in murine DC-SIGN inhibit a functional interaction with pathogens
- Author(s)
- Gramberg, T; Caminschi, I; Wegele, A; Hofmann, H; Pohlmann, S;
- Details
- Publication Year 2006-02-20,Volume 345,Issue #2,Page 482-491
- Journal Title
- VIROLOGY
- Publication Type
- Journal Article
- Abstract
- Certain viruses, bacteria, fungi and parasites target dendritic cells through the interaction with the cellular attachment factor DC-SIGN, making this C-type lectin an attractive target for therapeutic intervention. Studies oil DC-SIGN function Would be greatly aided by the establishment of a mouse model, however, it is unclear if the murine (m) homologue of human (h) DC-SIGN also binds to pathogens. Here, we investigated the interaction of mDC-SIGN, also termed CIRE, with the Ebolavirus glycoprotein (EBOV-GP), a ligand of hDC-SIGN. We found that mDC-SIGN neither binds EBOV-GP nor enhances infection by reporterviruses pseudotyped with EBOV-GP. Analysis of chimeras between mDC-SIGN and hDC-SIGN provided evidence that determinants in the carbohydrate recognition domain and in the neck domain of mDC-SIGN inhibit a functional interaction with EBOV-GP. Moreover, mDC-SIGN was found be monomeric, suggesting that lack of multimerization, which is believed to be required for efficient pathogen recognition by hDC-SIGN, might be one factor that prevents binding of mDC-SIGN to EBOV-GP. Our results Suggest that mDC-SIGN on murine dendritic cells is not an adequate model for pathogen interactions with hDC-SIGN. (c) 2005 Elsevier Inc. All rights reserved.
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- C-TYPE LECTIN; IMMUNODEFICIENCY-VIRUS TYPE-1; MARGINAL ZONE MACROPHAGES; DENDRITIC CELLS; T-CELLS; ENDOTHELIAL-CELLS; STRUCTURAL BASIS; HIV-1 INFECTION; RHESUS MACAQUE; RECEPTOR
- Publisher's Version
- https://doi.org/10.1016/j.virol.2005.10.008
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- Refer to copyright notice on published article.
Creation Date: 2006-02-20 12:00:00