A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection

A A Bashirova, T B Geijtenbeek, G C van Duijnhoven, S J van Vliet, J B Eilering, M P Martin, L Wu, T D Martin, N Viebig, P A Knolle, V N KewalRamani, Y van Kooyk, M Carrington

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The discovery of dendritic cell (DC)-specific intercellular adhesion molecule (ICAM)-3-grabbing nonintegrin (DC-SIGN) as a DC-specific ICAM-3 binding receptor that enhances HIV-1 infection of T cells in trans has indicated a potentially important role for adhesion molecules in AIDS pathogenesis. A related molecule called DC-SIGNR exhibits 77% amino acid sequence identity with DC-SIGN. The DC-SIGN and DC-SIGNR genes map within a 30-kb region on chromosome 19p13.2-3. Their strong homology and close physical location indicate a recent duplication of the original gene. Messenger RNA and protein expression patterns demonstrate that the DC-SIGN-related molecule is highly expressed on liver sinusoidal cells and in the lymph node but not on DCs, in contrast to DC-SIGN. Therefore, we suggest that a more appropriate name for the DC-SIGN-related molecule is L-SIGN, liver/lymph node-specific ICAM-3-grabbing nonintegrin. We show that in the liver, L-SIGN is expressed by sinusoidal endothelial cells. Functional studies indicate that L-SIGN behaves similarly to DC-SIGN in that it has a high affinity for ICAM-3, captures HIV-1 through gp120 binding, and enhances HIV-1 infection of T cells in trans. We propose that L-SIGN may play an important role in the interaction between liver sinusoidal endothelium and trafficking lymphocytes, as well as function in the pathogenesis of HIV-1.

Original languageEnglish
Pages (from-to)671-8
Number of pages8
JournalJournal of Experimental Medicine
Volume193
Issue number6
Publication statusPublished - 19 Mar 2001

Cite this

Bashirova, A A ; Geijtenbeek, T B ; van Duijnhoven, G C ; van Vliet, S J ; Eilering, J B ; Martin, M P ; Wu, L ; Martin, T D ; Viebig, N ; Knolle, P A ; KewalRamani, V N ; van Kooyk, Y ; Carrington, M. / A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection. In: Journal of Experimental Medicine. 2001 ; Vol. 193, No. 6. pp. 671-8.
@article{fe69c487c6704aa59fc6956b9409f8f3,
title = "A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection",
abstract = "The discovery of dendritic cell (DC)-specific intercellular adhesion molecule (ICAM)-3-grabbing nonintegrin (DC-SIGN) as a DC-specific ICAM-3 binding receptor that enhances HIV-1 infection of T cells in trans has indicated a potentially important role for adhesion molecules in AIDS pathogenesis. A related molecule called DC-SIGNR exhibits 77{\%} amino acid sequence identity with DC-SIGN. The DC-SIGN and DC-SIGNR genes map within a 30-kb region on chromosome 19p13.2-3. Their strong homology and close physical location indicate a recent duplication of the original gene. Messenger RNA and protein expression patterns demonstrate that the DC-SIGN-related molecule is highly expressed on liver sinusoidal cells and in the lymph node but not on DCs, in contrast to DC-SIGN. Therefore, we suggest that a more appropriate name for the DC-SIGN-related molecule is L-SIGN, liver/lymph node-specific ICAM-3-grabbing nonintegrin. We show that in the liver, L-SIGN is expressed by sinusoidal endothelial cells. Functional studies indicate that L-SIGN behaves similarly to DC-SIGN in that it has a high affinity for ICAM-3, captures HIV-1 through gp120 binding, and enhances HIV-1 infection of T cells in trans. We propose that L-SIGN may play an important role in the interaction between liver sinusoidal endothelium and trafficking lymphocytes, as well as function in the pathogenesis of HIV-1.",
keywords = "Animals, Antigens, CD, Antigens, Differentiation, Base Sequence, Cell Adhesion Molecules/metabolism, Cell Line, Cells, Cultured, Chromosome Mapping, DNA, Complementary, Dendritic Cells, Endothelium/cytology, Exons, HIV Envelope Protein gp120/metabolism, HIV-1/metabolism, Humans, Lectins/genetics, Lectins, C-Type, Liver/metabolism, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Polymorphism, Genetic, Receptors, Antigen/genetics, Receptors, Cell Surface/genetics, Receptors, HIV/genetics, Receptors, Virus/physiology",
author = "Bashirova, {A A} and Geijtenbeek, {T B} and {van Duijnhoven}, {G C} and {van Vliet}, {S J} and Eilering, {J B} and Martin, {M P} and L Wu and Martin, {T D} and N Viebig and Knolle, {P A} and KewalRamani, {V N} and {van Kooyk}, Y and M Carrington",
year = "2001",
month = "3",
day = "19",
language = "English",
volume = "193",
pages = "671--8",
journal = "Journal of Experimental Medicine",
issn = "0022-1007",
publisher = "Rockefeller University Press",
number = "6",

}

Bashirova, AA, Geijtenbeek, TB, van Duijnhoven, GC, van Vliet, SJ, Eilering, JB, Martin, MP, Wu, L, Martin, TD, Viebig, N, Knolle, PA, KewalRamani, VN, van Kooyk, Y & Carrington, M 2001, 'A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection' Journal of Experimental Medicine, vol. 193, no. 6, pp. 671-8.

A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection. / Bashirova, A A; Geijtenbeek, T B; van Duijnhoven, G C; van Vliet, S J; Eilering, J B; Martin, M P; Wu, L; Martin, T D; Viebig, N; Knolle, P A; KewalRamani, V N; van Kooyk, Y; Carrington, M.

In: Journal of Experimental Medicine, Vol. 193, No. 6, 19.03.2001, p. 671-8.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection

AU - Bashirova, A A

AU - Geijtenbeek, T B

AU - van Duijnhoven, G C

AU - van Vliet, S J

AU - Eilering, J B

AU - Martin, M P

AU - Wu, L

AU - Martin, T D

AU - Viebig, N

AU - Knolle, P A

AU - KewalRamani, V N

AU - van Kooyk, Y

AU - Carrington, M

PY - 2001/3/19

Y1 - 2001/3/19

N2 - The discovery of dendritic cell (DC)-specific intercellular adhesion molecule (ICAM)-3-grabbing nonintegrin (DC-SIGN) as a DC-specific ICAM-3 binding receptor that enhances HIV-1 infection of T cells in trans has indicated a potentially important role for adhesion molecules in AIDS pathogenesis. A related molecule called DC-SIGNR exhibits 77% amino acid sequence identity with DC-SIGN. The DC-SIGN and DC-SIGNR genes map within a 30-kb region on chromosome 19p13.2-3. Their strong homology and close physical location indicate a recent duplication of the original gene. Messenger RNA and protein expression patterns demonstrate that the DC-SIGN-related molecule is highly expressed on liver sinusoidal cells and in the lymph node but not on DCs, in contrast to DC-SIGN. Therefore, we suggest that a more appropriate name for the DC-SIGN-related molecule is L-SIGN, liver/lymph node-specific ICAM-3-grabbing nonintegrin. We show that in the liver, L-SIGN is expressed by sinusoidal endothelial cells. Functional studies indicate that L-SIGN behaves similarly to DC-SIGN in that it has a high affinity for ICAM-3, captures HIV-1 through gp120 binding, and enhances HIV-1 infection of T cells in trans. We propose that L-SIGN may play an important role in the interaction between liver sinusoidal endothelium and trafficking lymphocytes, as well as function in the pathogenesis of HIV-1.

AB - The discovery of dendritic cell (DC)-specific intercellular adhesion molecule (ICAM)-3-grabbing nonintegrin (DC-SIGN) as a DC-specific ICAM-3 binding receptor that enhances HIV-1 infection of T cells in trans has indicated a potentially important role for adhesion molecules in AIDS pathogenesis. A related molecule called DC-SIGNR exhibits 77% amino acid sequence identity with DC-SIGN. The DC-SIGN and DC-SIGNR genes map within a 30-kb region on chromosome 19p13.2-3. Their strong homology and close physical location indicate a recent duplication of the original gene. Messenger RNA and protein expression patterns demonstrate that the DC-SIGN-related molecule is highly expressed on liver sinusoidal cells and in the lymph node but not on DCs, in contrast to DC-SIGN. Therefore, we suggest that a more appropriate name for the DC-SIGN-related molecule is L-SIGN, liver/lymph node-specific ICAM-3-grabbing nonintegrin. We show that in the liver, L-SIGN is expressed by sinusoidal endothelial cells. Functional studies indicate that L-SIGN behaves similarly to DC-SIGN in that it has a high affinity for ICAM-3, captures HIV-1 through gp120 binding, and enhances HIV-1 infection of T cells in trans. We propose that L-SIGN may play an important role in the interaction between liver sinusoidal endothelium and trafficking lymphocytes, as well as function in the pathogenesis of HIV-1.

KW - Animals

KW - Antigens, CD

KW - Antigens, Differentiation

KW - Base Sequence

KW - Cell Adhesion Molecules/metabolism

KW - Cell Line

KW - Cells, Cultured

KW - Chromosome Mapping

KW - DNA, Complementary

KW - Dendritic Cells

KW - Endothelium/cytology

KW - Exons

KW - HIV Envelope Protein gp120/metabolism

KW - HIV-1/metabolism

KW - Humans

KW - Lectins/genetics

KW - Lectins, C-Type

KW - Liver/metabolism

KW - Mice

KW - Mice, Inbred BALB C

KW - Molecular Sequence Data

KW - Polymorphism, Genetic

KW - Receptors, Antigen/genetics

KW - Receptors, Cell Surface/genetics

KW - Receptors, HIV/genetics

KW - Receptors, Virus/physiology

M3 - Article

VL - 193

SP - 671

EP - 678

JO - Journal of Experimental Medicine

JF - Journal of Experimental Medicine

SN - 0022-1007

IS - 6

ER -