Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran
Dextran, the α-1,6-linked glucose polymer widely used in biology and medicine, promises new applications. Linear dextran applied as a blood plasma substitute demonstrates a high rate of biocompatibility. Dextran is present in foods, drugs, and vaccines and in most cases is applied as a biologically...
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Canadian Society for Pharmaceutical Sciences
2014-08-01
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doaj-baa7946e50c34ff487161917696423af2020-11-25T03:41:23ZengCanadian Society for Pharmaceutical SciencesJournal of Pharmacy & Pharmaceutical Sciences1482-18262014-08-0117310.18433/J3N590Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with DextranSergey Pustylnikov0Divya Sagar1Pooja Jain2Zafar K Khan3Group of Molecular Biology Research, Novosibirsk Tuberculosis Research Institute, Novosibirsk, Russia. Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USA.Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USA.Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USA.Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USA. Dextran, the α-1,6-linked glucose polymer widely used in biology and medicine, promises new applications. Linear dextran applied as a blood plasma substitute demonstrates a high rate of biocompatibility. Dextran is present in foods, drugs, and vaccines and in most cases is applied as a biologically inert substance. In this review we analyze dextran's cellular uptake principles, receptor specificity and, therefore, its ability to interfere with pathogen–lectin interactions: a promising basis for new antimicrobial strategies. Dextran-binding receptors in humans include the DC-SIGN (dendritic cell–specific intercellular adhesion molecule 3-grabbing nonintegrin) family receptors: DC-SIGN (CD209) and L-SIGN (the liver and lymphatic endothelium homologue of DC-SIGN), the mannose receptor (CD206), and langerin. These receptors take part in the uptake of pathogens by dendritic cells and macrophages and may also participate in the modulation of immune responses, mostly shown to be beneficial for pathogens per se rather than host(s). It is logical to predict that owing to receptor-specific interactions, dextran or its derivatives can interfere with these immune responses and improve infection outcome. Recent data support this hypothesis. We consider dextran a promising molecule for the development of lectin–glycan interaction-blocking molecules (such as DC-SIGN inhibitors) that could be applied in the treatment of diseases including tuberculosis, influenza, hepatitis B and C, human immunodeficiency virus infection and AIDS, etc. Dextran derivatives indeed change the pathology of infections dependent on DC-SIGN and mannose receptors. Complete knowledge of specific dextran–lectin interactions may also be important for development of future dextran applications in biological research and medicine. This article is open to POST-PUBLICATION REVIEW. Registered readers (see “For Readers”) may comment by clicking on ABSTRACT on the issue’s contents page. https://journals.library.ualberta.ca/jpps/index.php/JPPS/article/view/22139 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sergey Pustylnikov Divya Sagar Pooja Jain Zafar K Khan |
spellingShingle |
Sergey Pustylnikov Divya Sagar Pooja Jain Zafar K Khan Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran Journal of Pharmacy & Pharmaceutical Sciences |
author_facet |
Sergey Pustylnikov Divya Sagar Pooja Jain Zafar K Khan |
author_sort |
Sergey Pustylnikov |
title |
Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran |
title_short |
Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran |
title_full |
Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran |
title_fullStr |
Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran |
title_full_unstemmed |
Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran |
title_sort |
targeting the c-type lectins-mediated host-pathogen interactions with dextran |
publisher |
Canadian Society for Pharmaceutical Sciences |
series |
Journal of Pharmacy & Pharmaceutical Sciences |
issn |
1482-1826 |
publishDate |
2014-08-01 |
description |
Dextran, the α-1,6-linked glucose polymer widely used in biology and medicine, promises new applications. Linear dextran applied as a blood plasma substitute demonstrates a high rate of biocompatibility. Dextran is present in foods, drugs, and vaccines and in most cases is applied as a biologically inert substance. In this review we analyze dextran's cellular uptake principles, receptor specificity and, therefore, its ability to interfere with pathogen–lectin interactions: a promising basis for new antimicrobial strategies. Dextran-binding receptors in humans include the DC-SIGN (dendritic cell–specific intercellular adhesion molecule 3-grabbing nonintegrin) family receptors: DC-SIGN (CD209) and L-SIGN (the liver and lymphatic endothelium homologue of DC-SIGN), the mannose receptor (CD206), and langerin. These receptors take part in the uptake of pathogens by dendritic cells and macrophages and may also participate in the modulation of immune responses, mostly shown to be beneficial for pathogens per se rather than host(s). It is logical to predict that owing to receptor-specific interactions, dextran or its derivatives can interfere with these immune responses and improve infection outcome. Recent data support this hypothesis. We consider dextran a promising molecule for the development of lectin–glycan interaction-blocking molecules (such as DC-SIGN inhibitors) that could be applied in the treatment of diseases including tuberculosis, influenza, hepatitis B and C, human immunodeficiency virus infection and AIDS, etc. Dextran derivatives indeed change the pathology of infections dependent on DC-SIGN and mannose receptors. Complete knowledge of specific dextran–lectin interactions may also be important for development of future dextran applications in biological research and medicine.
This article is open to POST-PUBLICATION REVIEW. Registered readers (see “For Readers”) may comment by clicking on ABSTRACT on the issue’s contents page.
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url |
https://journals.library.ualberta.ca/jpps/index.php/JPPS/article/view/22139 |
work_keys_str_mv |
AT sergeypustylnikov targetingthectypelectinsmediatedhostpathogeninteractionswithdextran AT divyasagar targetingthectypelectinsmediatedhostpathogeninteractionswithdextran AT poojajain targetingthectypelectinsmediatedhostpathogeninteractionswithdextran AT zafarkkhan targetingthectypelectinsmediatedhostpathogeninteractionswithdextran |
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