The dynamics of receptor recognition by human rhinoviruses

Casasnovas, José M.

doi:10.1016/s0966-842x(00)01749-2

Cited by 14 publications

(10 citation statements)

References 13 publications

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“…We observed that engagement and cross-linking of ICAM-1 with CD54 mAb RR1/1 did not trigger Sn expression on DC but inhibited HRV-induced Sn expression (data not shown). However, because one HRV capsid has 60 receptor binding sites and binds to ICAM-1 with high avidity (40,41), HRV particles might trigger pronounced cross-linking of ICAM-1 and subsequent signal transduction leading to Sn induction and up-regulation of B7-H1 expression. It is conceivable that this may not be achieved with Abs.…”

Section: Discussionmentioning

confidence: 99%

Human Rhinoviruses Inhibit the Accessory Function of Dendritic Cells by Inducing Sialoadhesin and B7-H1 Expression

Kirchberger

Majdic

Schmitz

et al. 2005

The Journal of Immunology

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Dendritic cells (DC) are professional APCs with an unmatched ability to interact with and activate T cells. There is accumulating evidence that DC not only efficiently stimulate T cell activation but also regulate T cell responses. However, little is known about cell surface structures on DC involved in the regulation of T cell responses. We demonstrate that human rhinoviruses (HRV) can efficiently inhibit the accessory function of DC through induction of inhibitory cell surface receptors. We observed that treatment of DC with HRV14 (R-DC), a member of the major group HRV family, diminished their T cell stimulatory capacity and induced a promiscuous and deep anergic state in cocultured T cells despite high levels of MHC molecules as well as costimulatory molecules, e.g., B7-1 (CD80) and B7-2 (CD86), and independent of inhibitory soluble factors such as IL-10. In contrast, expression of inhibitory B7-H1 molecules was up-regulated and R-DC de novo expressed sialoadhesin (Sn). Most importantly, blocking of B7-H1 and Sn on R-DC with specific mAbs against both receptors reverted the inhibitory phenotype. Thus, inhibitory signals delivered from R-DC to T cells via B7-H1 and Sn were critical for the induction of anergy. These observations suggest that an altered accessory molecule repertoire on DC upon interaction with HRV down-modulates adaptive immune responses during the viral infection.

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Section: Discussionmentioning

confidence: 99%

Human Rhinoviruses Inhibit the Accessory Function of Dendritic Cells by Inducing Sialoadhesin and B7-H1 Expression

Kirchberger

Majdic

Schmitz

et al. 2005

The Journal of Immunology

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“…The receptor binds conserved sequence motifs contributed by VP1 and VP3 that are exposed in the canyon and differ in HRV-A and HRV-B [89,90]. Where present, the pocket factor is expelled and the canyon widens allowing the receptor to penetrate more deeply and to contact residues at the canyon base; alternatively, it was proposed that an 'open' conformation of the virus temporally adopted during breathing was stabilised by ICAM-1 [91][92][93]. As shown for HRV3, binding to ICAM-1 is biphasic, which can be either interpreted as the presence of two different binding sites or as cooperative binding (i.e.…”

Section: Major Group Human Rhinoviruses Entry and Intracellular Traffmentioning

confidence: 99%

Uncoating of human rhinoviruses

Fuchs

Blaas

2010

Reviews in Medical Virology

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Human rhinoviruses (HRVs) are a major cause of the common cold. The more than one hundred serotypes, divided into species HRV-A and HRV-B, either bind intercellular adhesion molecule 1 (major group viruses) or members of the low-density lipoprotein receptor (minor group viruses) for cell entry. Some major group HRVs can also access the host cell via heparan sulphate proteoglycans. The cell attachment protein(s) of the recently discovered phylogenetic clade HRV-C is unknown. The respective receptors direct virus uptake via clathrin-dependent or independent endocytosis or via macropinocytosis. Triggered by ICAM-1 and/or the low pH environment in endosomes the virions undergo conformational alterations giving rise to hydrophobic subviral particles. These are handed over from the receptors to the endosomal membrane. According to the current view, the RNA genome is released through an opening at one of the fivefold axes of the icosahedral capsid and crosses the membrane through a pore presumably formed by viral proteins. Alternatively, the membrane may be ruptured allowing subviral particles and RNA to enter the cytosol. Whether a channel is formed or the membrane is disrupted most probably depends on the respective HRV receptor.

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“…We observed that engagement of ICAM-1 with CD54 mAb RR1/1 or R6.5 or its natural ligand fibrinogen did not stimulate monocyte aggregation in our test system (data not shown). However, since one HRV capsid has 60 receptor binding sites and binds to ICAM-1 with high avidity (Casasnovas, 2000;Casasnovas and Springer, 1995;Reisdorph et al, 2003;Smith and Baker, 1999;Xing et al, 2003), HRV particles might trigger pronounced cross-linking of ICAM-1 and subsequent signal transduction. It is conceivable that this may not be achieved by mAbs or by other ligands of ICAM-1.…”

Section: Discussionmentioning

confidence: 99%

“…One HRV capsid has 60 potential binding sites located in depressions of the viral protein coat, the so-called canyons (Casasnovas, 2000;Casasnovas and Springer, 1995;Reisdorph et al, 2003;Smith and Baker, 1999;Xing et al, 2003). The binding of HRV to ICAM-1 was found to be biphasic.…”

Section: Introductionmentioning

confidence: 99%