The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand

Jordi Bella, Prasanna Kolatkar, Christopher W. Marlor, Jeffrey M. Greve, Michael G. Rossmann

Research output: Contribution to journalArticle

173 Citations (Scopus)

Abstract

The normal function of human intercellular adhesion molecule-1 (ICAM-1) is to provide adhesion between endothelial cells and leukocytes after injury or stress. ICAM-1 binds to leukocyte function-associated antigen (LFA-1) or macrophage-1 antigen (Mac-1). However, ICAM-1 is also used as a receptor by the major group of human rhinoviruses and is a catalyst for the subsequent viral uncoating during cell entry. The three-dimensional atomic structure of the two amino-terminal domains (D1 and D2) of ICAM-1 has been determined to 2.2-Å resolution and fitted into a cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex Rhinovirus attachment is confined to the BC, CD, DE, and FG loops of the amino-terminal Ig-like domains (D1) at the end distal to the cellular membrane. The loops are considerably different in structure to those of human ICAM-2 or murine ICAM-1, which do not bind rhinoviruses. There are extensive charge interactions between ICAM-1 and human rhinoviruses, which are mostly conserved in both major and minor receptor groups of rhinoviruses. The interaction of ICAMs with LFA-1 is known to be mediated by a divalent cation bound to the insertion (I)-domain on the a chain of LFA, I and the carboxyl group of a conserved glutamic acid residue on ICAMS. Domain D1 has been docked with the known structure of the I- domain. The resultant model is consistent with mutational data and provides a structural framework for the adhesion between these molecules.

Original languageEnglish
Pages (from-to)4140-4145
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number8
DOIs
Publication statusPublished - 14 Apr 1998
Externally publishedYes

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Rhinovirus
Lymphocyte Function-Associated Antigen-1
Intercellular Adhesion Molecule-1
Integrins
Ligands
Virus Uncoating
Macrophage-1 Antigen
Cryoelectron Microscopy
Divalent Cations
Glutamic Acid
Leukocytes
Endothelial Cells
Membranes
Wounds and Injuries

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand. / Bella, Jordi; Kolatkar, Prasanna; Marlor, Christopher W.; Greve, Jeffrey M.; Rossmann, Michael G.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, No. 8, 14.04.1998, p. 4140-4145.

Research output: Contribution to journalArticle

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abstract = "The normal function of human intercellular adhesion molecule-1 (ICAM-1) is to provide adhesion between endothelial cells and leukocytes after injury or stress. ICAM-1 binds to leukocyte function-associated antigen (LFA-1) or macrophage-1 antigen (Mac-1). However, ICAM-1 is also used as a receptor by the major group of human rhinoviruses and is a catalyst for the subsequent viral uncoating during cell entry. The three-dimensional atomic structure of the two amino-terminal domains (D1 and D2) of ICAM-1 has been determined to 2.2-{\AA} resolution and fitted into a cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex Rhinovirus attachment is confined to the BC, CD, DE, and FG loops of the amino-terminal Ig-like domains (D1) at the end distal to the cellular membrane. The loops are considerably different in structure to those of human ICAM-2 or murine ICAM-1, which do not bind rhinoviruses. There are extensive charge interactions between ICAM-1 and human rhinoviruses, which are mostly conserved in both major and minor receptor groups of rhinoviruses. The interaction of ICAMs with LFA-1 is known to be mediated by a divalent cation bound to the insertion (I)-domain on the a chain of LFA, I and the carboxyl group of a conserved glutamic acid residue on ICAMS. Domain D1 has been docked with the known structure of the I- domain. The resultant model is consistent with mutational data and provides a structural framework for the adhesion between these molecules.",
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