A novel adhesion pathway that regulates dendritic cell trafficking and T cell interactions

Research output: Contribution to journalReview articleAcademicpeer-review

Abstract

Dendritic cells (DC) are present in essentially every tissue, where they operate at the interface of innate and acquired immunity by recognizing pathogens and presenting pathogen-derived peptides to T cells. Cell-cell interactions between DC, T cells and endothelial cells are crucial to all immunological processes. Recently, several C-type lectin receptors have been characterized that are abundantly expressed on the surface of DC. It is now becoming clear that these lectin receptors serve not only as antigen-receptors recognizing pathogens, but they may also function as adhesion receptors and/or signaling molecules. In particular the DC specific C-type lectin DC-SIGN (CD209) regulates adhesion processes, such as DC trafficking by interacting with ICAM-2 and T cell synapse formation, upon binding of ICAM-3. C-type lectins such as DC-SIGN contain a lectin domain that recognizes in a Ca2+-dependent manner carbohydrates such as mannose-containing structures presented on the glycoproteins ICAM-2 and ICAM-3. Although the integrin LFA-1 is a counter-receptor for both ICAM-2 and ICAM-3, on DC, DC-SIGN is the high affinity adhesion receptor for ICAM-2/-3. Here we discuss how the heterogeneity of mannose-residues exposed on cellular proteins and pathogens regulates specific binding of a repertoire of DC-expressed C-type lectins that contribute to the diversity of immune responses created by DC.

Original languageEnglish
Pages (from-to)47-56
Number of pages10
JournalImmunological Reviews
Volume186
Publication statusPublished - Aug 2002

Cite this

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title = "A novel adhesion pathway that regulates dendritic cell trafficking and T cell interactions",
abstract = "Dendritic cells (DC) are present in essentially every tissue, where they operate at the interface of innate and acquired immunity by recognizing pathogens and presenting pathogen-derived peptides to T cells. Cell-cell interactions between DC, T cells and endothelial cells are crucial to all immunological processes. Recently, several C-type lectin receptors have been characterized that are abundantly expressed on the surface of DC. It is now becoming clear that these lectin receptors serve not only as antigen-receptors recognizing pathogens, but they may also function as adhesion receptors and/or signaling molecules. In particular the DC specific C-type lectin DC-SIGN (CD209) regulates adhesion processes, such as DC trafficking by interacting with ICAM-2 and T cell synapse formation, upon binding of ICAM-3. C-type lectins such as DC-SIGN contain a lectin domain that recognizes in a Ca2+-dependent manner carbohydrates such as mannose-containing structures presented on the glycoproteins ICAM-2 and ICAM-3. Although the integrin LFA-1 is a counter-receptor for both ICAM-2 and ICAM-3, on DC, DC-SIGN is the high affinity adhesion receptor for ICAM-2/-3. Here we discuss how the heterogeneity of mannose-residues exposed on cellular proteins and pathogens regulates specific binding of a repertoire of DC-expressed C-type lectins that contribute to the diversity of immune responses created by DC.",
keywords = "Animals, Cell Adhesion Molecules/immunology, Dendritic Cells/immunology, Humans, Lectins, C-Type, Receptors, Cell Surface/immunology, T-Lymphocytes/immunology",
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year = "2002",
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language = "English",
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pages = "47--56",
journal = "Immunological Reviews",
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}

A novel adhesion pathway that regulates dendritic cell trafficking and T cell interactions. / van Kooyk, Yvette; Geijtenbeek, Teunis B H.

In: Immunological Reviews, Vol. 186, 08.2002, p. 47-56.

Research output: Contribution to journalReview articleAcademicpeer-review

TY - JOUR

T1 - A novel adhesion pathway that regulates dendritic cell trafficking and T cell interactions

AU - van Kooyk, Yvette

AU - Geijtenbeek, Teunis B H

PY - 2002/8

Y1 - 2002/8

N2 - Dendritic cells (DC) are present in essentially every tissue, where they operate at the interface of innate and acquired immunity by recognizing pathogens and presenting pathogen-derived peptides to T cells. Cell-cell interactions between DC, T cells and endothelial cells are crucial to all immunological processes. Recently, several C-type lectin receptors have been characterized that are abundantly expressed on the surface of DC. It is now becoming clear that these lectin receptors serve not only as antigen-receptors recognizing pathogens, but they may also function as adhesion receptors and/or signaling molecules. In particular the DC specific C-type lectin DC-SIGN (CD209) regulates adhesion processes, such as DC trafficking by interacting with ICAM-2 and T cell synapse formation, upon binding of ICAM-3. C-type lectins such as DC-SIGN contain a lectin domain that recognizes in a Ca2+-dependent manner carbohydrates such as mannose-containing structures presented on the glycoproteins ICAM-2 and ICAM-3. Although the integrin LFA-1 is a counter-receptor for both ICAM-2 and ICAM-3, on DC, DC-SIGN is the high affinity adhesion receptor for ICAM-2/-3. Here we discuss how the heterogeneity of mannose-residues exposed on cellular proteins and pathogens regulates specific binding of a repertoire of DC-expressed C-type lectins that contribute to the diversity of immune responses created by DC.

AB - Dendritic cells (DC) are present in essentially every tissue, where they operate at the interface of innate and acquired immunity by recognizing pathogens and presenting pathogen-derived peptides to T cells. Cell-cell interactions between DC, T cells and endothelial cells are crucial to all immunological processes. Recently, several C-type lectin receptors have been characterized that are abundantly expressed on the surface of DC. It is now becoming clear that these lectin receptors serve not only as antigen-receptors recognizing pathogens, but they may also function as adhesion receptors and/or signaling molecules. In particular the DC specific C-type lectin DC-SIGN (CD209) regulates adhesion processes, such as DC trafficking by interacting with ICAM-2 and T cell synapse formation, upon binding of ICAM-3. C-type lectins such as DC-SIGN contain a lectin domain that recognizes in a Ca2+-dependent manner carbohydrates such as mannose-containing structures presented on the glycoproteins ICAM-2 and ICAM-3. Although the integrin LFA-1 is a counter-receptor for both ICAM-2 and ICAM-3, on DC, DC-SIGN is the high affinity adhesion receptor for ICAM-2/-3. Here we discuss how the heterogeneity of mannose-residues exposed on cellular proteins and pathogens regulates specific binding of a repertoire of DC-expressed C-type lectins that contribute to the diversity of immune responses created by DC.

KW - Animals

KW - Cell Adhesion Molecules/immunology

KW - Dendritic Cells/immunology

KW - Humans

KW - Lectins, C-Type

KW - Receptors, Cell Surface/immunology

KW - T-Lymphocytes/immunology

M3 - Review article

VL - 186

SP - 47

EP - 56

JO - Immunological Reviews

JF - Immunological Reviews

SN - 0105-2896

ER -