Detection of major group rhinoviruses by soluble intercellular adhesion molecule-1 (sICAM-1)

Last-Barney, Kathleen; Marlin, Steven D.; McNally, Eugene J.; Cahill, Carol; Jeanfavre, Deborah D.; Faanes, Ronald B.; Merluzzi, Vincent J.

doi:10.1016/0166-0934(91)90067-a

Cited by 9 publications

(5 citation statements)

References 9 publications

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“…Soluble ICAM-1 and LDLR materials can bind their appropriate RV-A and RV-B isolates to inhibit virus infection of susceptible cells [43–45]. The soluble recombinant CDHR3 protein panel was tested for its ability to inhibit C15 infection of stably transduced fCR3Y cells.…”

Section: Resultsmentioning

confidence: 99%

CDHR3 extracellular domains EC1-3 mediate rhinovirus C interaction with cells and as recombinant derivatives, are inhibitory to virus infection

Watters

Palmenberg

2018

PLoS Pathog

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Viruses in the rhinovirus C species (RV-C) are more likely to cause severe wheezing illnesses and asthma exacerbations in children than related isolates of the RV-A or RV-B. The RV-C capsid is structurally distinct from other rhinoviruses and does not bind ICAM-1 or LDL receptors. The RV-C receptor is instead, human cadherin-related family member 3 (CDHR3), a protein unique to the airway epithelium. A single nucleotide polymorphism (rs6967330, encoding C529Y) in CDHR3 regulates the display density of CDHR3 on cell surfaces and is among the strongest known genetic correlates for childhood virus-induced asthma susceptibility. CDHR3 immunoprecipitations from transfected or transduced cell lysates were used to characterize the RV-C interaction requirements. The C529 and Y529 variations in extracellular repeat domain 5 (EC5), bound equivalently to virus. Glycosylase treatment followed by mass spectrometry mapped 3 extracellular N-linked modification sites, and further detected surface-dependent, α2–6 sialyation unique to the Y529 format. None of these modifications were required for RV-C recognition, but removal or even dilution of structurally stabilizing calcium ions from the EC junctions irreversibly abrogated virus binding. CDHR3 deletions expressed in HeLa cells or as bacterial recombinant proteins, mapped the amino-terminal EC1 unit as the required virus contact. Derivatives containing the EC1 domain, could not only recapitulate virus:receptor interactions in vitro, but also directly inhibit RV-C infection of susceptible cells for several virus genotypes (C02, C15, C41, and C45). We propose that all RV-C use the same EC1 landing pad, interacting with putative EC3-mediated multimerization formats of CDHR3.

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Section: Resultsmentioning

confidence: 99%

CDHR3 extracellular domains EC1-3 mediate rhinovirus C interaction with cells and as recombinant derivatives, are inhibitory to virus infection

Watters

Palmenberg

2018

PLoS Pathog

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“…To investigate whether acquiring a new receptor specificity is accompanied by the loss of the capability to attach to ICAM-1, soluble recombinant ICAM-1 was used to coat a microtiter plate and the binding of the HRVs was determined by an assay similar to the ELISA described by Last-Barney and colleagues (21). All iso- lates exhibited ICAM-1 binding very similar to that of wt virus (data not shown).…”

Section: Single Clones Of Hep-2 Cell-adapted Hrv89 Replicate In Cos-7mentioning

confidence: 99%

Viral Evolution toward Change in Receptor Usage: Adaptation of a Major Group Human Rhinovirus To Grow in ICAM-1-Negative Cells

Reischl

Reithmayer

Winsauer

et al. 2001

J Virol

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Major receptor group common cold virus HRV89 was adapted to grow in HEp-2 cells, which are permissive for minor group human rhinoviruses (HRVs) but which only marginally support growth of major-group viruses. After 32 blind passages in these cells, each alternating with boosts of the recovered virus in HeLa cells, HRV89 acquired the capacity to effectively replicate in HEp-2 cells, attaining virus titers comparable to those in HeLa cells although no cytopathic effect was observed. Several clones were isolated and shown to replicate in HeLa cells whose ICAM-1 was blocked with monoclonal antibody R6.5 and in COS-7 cells, which are devoid of ICAM-1. Blocking experiments with recombinant very-low-density lipoprotein receptor fragments and enzyme-linked immunosorbent assays indicated that the mutants bound a receptor different from that used by minor-group viruses. Determination of the genomic RNA sequence encoding the capsid protein region revealed no changes in amino acid residues at positions equivalent to those involved in the interaction of HRV14 or HRV16 with ICAM-1. One mutation was within the footprint of a very-low-density lipoprotein receptor fragment bound to minor-group virus HRV2. Since ICAM-1 not only functions as a vehicle for cell entry but has also a "catalytic" function in uncoating, the use of other receptors must have important consequences for the entry pathway and demonstrates the plasticity of these viruses.Human rhinoviruses (HRVs), a major cause of mild upper respiratory infections generally recognized as common colds, are small icosahedral particles with a capsid composed of four viral proteins, VP1 through VP4 (for a review see reference 9). The capsid encases a genomic RNA of about 7,500 nucleotides encoding a polyprotein which is cotranslationally and autocatalytically processed by three viral proteinases, P2A, P3C, and P3CD (the precursor of P3C). A final maturation cleavage of VP0 to VP2 and VP4 occurs concomitantly with encapsidation by an as yet unidentified protease. With one exception (HRV87), the serotypes can be divided into a major group, using intercellular adhesion molecule 1 (ICAM-1) as the viral receptor, and a minor group, attaching to the cell via members of the low-density lipoprotein receptor (LDLR) family including LDLR, the very-low-density lipoprotein receptor (VLDLR), and LDLR-related protein (LRP) (16,27). The nature of the HRV87 receptor is unknown (50). Whereas major-group viruses are highly specific for human ICAM-1 and fail to attach to the homologue of other species, minor-group viruses bind to a variety of LDLRs, most likely due to the high evolutionary conservation of these membrane proteins. Replication usually does not occur in nonhuman cells even when suitable receptors are present, and adaptation of HRV2 to growth in mouse cells has been shown to be correlated with mutations in nonstructural proteins P2B and P2C (23).As HRVs of both receptor groups are very similar with respect to the amino acid sequence and the three-dimensional structure of the viral cap...

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“…The reported serotype recognition of these antibodies ranged from 52 to 68% of the serotypes tested. Another approach to HRV detection utilized soluble ICAM-l, the cell surface receptor for the major subgroup of HRV, as both the capture and detection reagent in a 4-h format (Last-Barney et al, 1991). While this assay would be predicted to recognize all major subgroup serotypes, it may not be specific for HRV because all ICAM-l binding molecules would give a positive result.…”

Section: Discussionmentioning

confidence: 99%

Rapid multiserotype detection of human rhinoviruses on optically coated silicon surfaces

Ostroff¹,

Ettinger²,

La³

et al. 2001

Journal of Clinical Virology

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Detection of major group rhinoviruses by soluble intercellular adhesion molecule-1 (sICAM-1)

Cited by 9 publications

References 9 publications

CDHR3 extracellular domains EC1-3 mediate rhinovirus C interaction with cells and as recombinant derivatives, are inhibitory to virus infection

CDHR3 extracellular domains EC1-3 mediate rhinovirus C interaction with cells and as recombinant derivatives, are inhibitory to virus infection

Viral Evolution toward Change in Receptor Usage: Adaptation of a Major Group Human Rhinovirus To Grow in ICAM-1-Negative Cells

Rapid multiserotype detection of human rhinoviruses on optically coated silicon surfaces

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