In vitro Inhibitory Activity of Soluble ICAM-1 for the Numbered Serotypes of Human Rhinovirus

1993 ◽  
Vol 4 (6) ◽  
pp. 323-327 ◽  
Author(s):  
C. E. Crump ◽  
E. Arruda ◽  
F. G. Hayden
Keyword(s):  
Human Rhinovirus ◽  
Intercellular Adhesion Molecule ◽  
Yield Reduction ◽  
Inhibitory Effects ◽  
Intercellular Adhesion Molecule 1 ◽  
Human Embryonic Lung ◽  
Group Type ◽  
Hel Cells ◽  
Soluble Intercellular Adhesion Molecule

We studied the antirhinovirus activity of soluble intercellular adhesion molecule-1 (sICAM-1) against all 100 numbered human rhinovirus (HRV) serotypes in human embryonic lung fibroblast (HEL) cells. sICAM-1 inhibited replication of 88 of 90 HRVs belonging to the major receptor group with 50% effective concentrations (EC50) ranging from 0.1 to 41.1 μg ml−1 (~0.002 to 0.8 μM). No inhibition at 100 μg ml−1 (~2 μM) was observed for HRV belonging to the minor receptor group, type 87, and two serotypes of the major receptor group (types 23 and 25). Yield reduction assays done with five HRV serotypes in human adenoid expiants found that sICAM-1 had concentration-dependent inhibitory effects that correlated closely with the activity observed in HEL cells ( r2 = 0.99, P < 0.001).

scholarly journals Prevention of Human Rhinovirus Infection by Multivalent Fab Molecules Directed against ICAM-1

2003 ◽  
Vol 47 (5) ◽  
pp. 1503-1508 ◽  
Author(s):  
Catherine H. Charles ◽  
Guang X. Luo ◽  
Lori A. Kohlstaedt ◽  
Ianessa G. Morantte ◽  
Elliott Gorfain ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Dissociation Rate ◽  
Human Rhinovirus ◽  
Intercellular Adhesion Molecule ◽  
High Yield ◽  
Intercellular Adhesion Molecule 1 ◽  
Fab Fragment ◽  
Rhinovirus Infection ◽  
Recombinant Polypeptides

ABSTRACT We have developed a technology for improving avidity by making bivalent, trivalent, or tetravalent recombinant polypeptides. We designed tripartite proteins consisting of the Fab fragment of an antibody fused with a hinge derived from human immunoglobulin D that was further linked to polymerization domains derived from human coiled-coil proteins. We report here on the application of this method with a Fab domain directed against the major human rhinovirus receptor, intercellular adhesion molecule 1 (ICAM-1). Multivalent anti-ICAM-1 molecules were produced in bacteria and purified as soluble preassembled homogeneous proteins at high yield. These proteins successfully blocked rhinovirus infection in vitro, with the efficiency increasing from monomer to dimer, trimer, and tetramer. The diminished dissociation rate of these multivalent antibodies and their improved efficacy in preventing rhinovirus infection provide a foundation for producing prophylactic and therapeutic molecules against human rhinovirus, the causative agent of the majority of common colds.

scholarly journals Variability of Serum Soluble Intercellular Adhesion Molecule-1 Measurements Attributable to a Common Polymorphism

2004 ◽  
Vol 50 (11) ◽  
pp. 2185-2187 ◽  
Author(s):  
Thomas C Register ◽  
Kathryn P Burdon ◽  
Leon Lenchik ◽  
Donald W Bowden ◽  
Gregory A Hawkins ◽  
...  
Keyword(s):  
Adhesion Molecule ◽  
Intercellular Adhesion ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
Common Polymorphism ◽  
Soluble Intercellular Adhesion Molecule

scholarly journals Silibinin Inhibits ICAM-1 Expression via Regulation of N-Linked and O-Linked Glycosylation in ARPE-19 Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-13
Author(s):  
Yi-Hao Chen ◽  
Ching-Long Chen ◽  
Chang-Min Liang ◽  
Jy-Been Liang ◽  
Ming-Cheng Tai ◽  
...  
Keyword(s):  
Nuclear Translocation ◽  
Transmembrane Protein ◽  
Reporter Gene Assay ◽  
Intercellular Adhesion Molecule ◽  
Inhibitory Effects ◽  
Intercellular Adhesion Molecule 1 ◽  
Reporter Activity ◽  
Gene Assay ◽  
Stat1 Signaling ◽  
Necrosis Factor

To evaluate the effects of silibinin on intercellular adhesion molecule-1 (ICAM-1) expression, we used ARPE-19 cells as a model in which tumor necrosis factor (TNF-α) and interferon (IFN-γ) enhanced ICAM-1 expression. This upregulation was inhibited by silibinin. In an adherence assay using ARPE-19 and THP-1 cells, silibinin inhibited the cell adhesion function of ICAM-1. The inhibitory effects of silibinin on ICAM-1 expression were mediated via the blockage of nuclear translocation of p65 proteins in TNF-αand phosphorylation of STAT1 in IFN-γ-stimulated cells. In addition, silibinin altered the degree of N-linked glycosylation posttranslationally in ARPE-19 cells by significantly enhancingMGAT3gene expression. Silibinin can increase the O-GlcNAc levels of glycoproteins in ARPE-19 cells. In a reporter gene assay, PUGNAc, which can also increase O-GlcNAc levels, inhibited NF-κB reporter activity in TNF-α-induced ARPE-19 cells and this process was augmented by silibinin treatment. Overexpression ofOGTgene was associated with reduced TNF-α-induced ICAM-1 levels, which is consistent with that induced by silibinin treatment. Taken together, silibinin inhibits ICAM-1 expression and its function through altered O-linked glycosylation in NF-κB and STAT1 signaling pathways and decreases the N-linked glycosylation of ICAM-1 transmembrane protein in proinflammatory cytokine-stimulated ARPE-19 cells.

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