Modelling of the human intercellular adhesion molecule‐1, the human rhinovirus major group receptor

A model has been built of the amino‐terminal domain of the intercellular adhesion molecule‐1 (ICAM‐1), the receptor for most human rhinovirus serotypes. The model was based on sequence and presumed structural homology to immunoglobulin constant domains. It fits well into the putative receptors attachment site, the canyon, on the human rhinovirus‐14 (HRV14) surface in a manner consistent with most of the mutational data for ICMA‐1 (Staunton, D. E., Dustin, M. L., Erickson, H. P., Springer, T. A. Cell, in press, 1989) and HRV14 (Colonno, R. J., Condra, J. H., Mizutani, S., Callahan, P. L., Davies, M. E., Murcko, M. A. Proc. Natl. Acad. Sci. U.S.A. 85: 5449‐5453, 1988).

[1]  T. A. Jones,et al.  Using known substructures in protein model building and crystallography. , 1986, The EMBO journal.

[2]  M. Rossmann,et al.  What does the molecular structure of viruses tell us about viral functions? , 1987, Microbiological sciences.

[3]  M G Rossmann,et al.  Structural analysis of a series of antiviral agents complexed with human rhinovirus 14. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[4]  D. Staunton,et al.  A soluble form of intercellular adhesion molecule-1 inhibits rhinovirus infection , 1990, Nature.

[5]  M. Rossmann,et al.  Conservation of the putative receptor attachment site in picornaviruses. , 1988, Virology.

[6]  M. Murcko,et al.  Evidence for the direct involvement of the rhinovirus canyon in receptor binding. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[7]  Thomas J. Smith.  MACINPLOT– a program to display electron density and atomic models on the Macintosh personal computer , 1990 .

[8]  Robin A. Weiss,et al.  The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain , 1986, Cell.

[9]  M S Chapman,et al.  Crystal structure of human rhinovirus serotype 1A (HRV1A). , 1989, Journal of molecular biology.

[10]  E. Wimmer,et al.  Cellular receptor for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily , 1989, Cell.

[11]  John E. Johnson,et al.  Structure of a human common cold virus and functional relationship to other picornaviruses , 1985, Nature.

[12]  J. E. McQueen,et al.  Computer manipulation of (macro)molecules with the method of local change , 1974 .

[13]  D. Littman,et al.  Viral receptors of the immunoglobulin superfamily , 1989, Cell.

[14]  J. Tomassini,et al.  Biochemical characterization of a glycoprotein required for rhinovirus attachment. , 1989, The Journal of biological chemistry.

[15]  T. A. Jones,et al.  A graphics model building and refinement system for macromolecules , 1978 .

[16]  G Vriend,et al.  The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. , 1986, Science.

[17]  Michael Loran Dustin,et al.  Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families , 1988, Cell.

[18]  Michael Loran Dustin,et al.  Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1 , 1989, Nature.

[19]  G. Vriend,et al.  Common cold viruses , 1987 .

[20]  M G Rossmann,et al.  Comparison of protein structures. , 1985, Methods in enzymology.

[21]  R. Colonno,et al.  Isolation of a monoclonal antibody that blocks attachment of the major group of human rhinoviruses , 1986, Journal of virology.

[22]  A. Treasurywala,et al.  Conformational change in the floor of the human rhinovirus canyon blocks adsorption to HeLa cell receptors , 1989, Journal of virology.

[23]  J. Deisenhofer.  Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. , 1981, Biochemistry.

[24]  D. Staunton,et al.  A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses , 1989, Cell.

[25]  A. F. Williams,et al.  The immunoglobulin superfamily--domains for cell surface recognition. , 1988, Annual review of immunology.

[26]  A. Mcclelland,et al.  The major human rhinovirus receptor is ICAM-1 , 1989, Cell.

[27]  P Argos,et al.  Exploring structural homology of proteins. , 1976, Journal of molecular biology.

[28]  S J Remington,et al.  A general method to assess similarity of protein structures, with applications to T4 bacteriophage lysozyme. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[29]  Michael G. Rossmann,et al.  Chemical and biological evolution of a nucleotide-binding protein , 1974, Nature.

[30]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[31]  A. D. McLachlan,et al.  Profile analysis: detection of distantly related proteins. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[32]  B. Seed,et al.  ICAM, an adhesion ligand of LFA-1, is homologous to the neural cell adhesion molecule NCAM , 1988, Nature.