Recombinant soluble low-density lipoprotein receptor fragment inhibits common cold infection

Marlovits, Thomas C.; Zechmeister, Thomas; Schwihla, Herwig; Ronacher, Bernhard; Blaas, Dieter

doi:10.1002/(sici)1099-1352(199812)11:1/6<49::aid-jmr388>3.0.co;2-3

Cited by 9 publications

(4 citation statements)

References 14 publications

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“…The LDLR, LDLR-related protein (LRP), and very low density lipoprotein receptor (VLDLR) have been identified as receptors for minor group HRVs by their ability to block virus binding to cultured cells (Hofer et al 1994; Marlovits et al 1998a, b, c). These receptors comprise an extracellular domain of 7 (LDLR), 8 (VLDLR), or 31 (LRP) ligand-binding repeats, a transmembrane domain, and a cytoplasmic domain.…”

Section: Picornavirus Receptorsmentioning

confidence: 99%

“…The minor group HRVs use members of the LDLR family for cell entry (Hofer et al 1994; Marlovits et al 1998c). The C-terminal cytoplasmic domains of LDLRs contain tyrosine- and di-leucine-based internalization signals and are responsible for the clustering of LDLRs in clathrin-coated pits (Chen et al 1990; Glickman et al 1989; Pearse 1988).…”

Section: Endocytosis and Sites Of Uncoatingmentioning

confidence: 99%

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Picornaviruses

Tuthill

Groppelli

Hogle

et al. 2010

Current Topics in Microbiology and Immunology

169

218

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The picornavirus family consists of a large number of small RNA viruses, many of which are significant pathogens of humans and livestock. They are amongst the simplest of vertebrate viruses comprising a single stranded positive sense RNA genome within a T = 1 (quasi T = 3) icosahedral protein capsid of approximately 30 nm diameter. The structures of a number of picornaviruses have been determined at close to atomic resolution by X-ray crystallography. The structures of cell entry intermediate particles and complexes of virus particles with receptor molecules or antibodies have also been obtained by X-ray crystallography or at a lower resolution by cryo-electron microscopy. Many of the receptors used by different picornaviruses have been identified, and it is becoming increasingly apparent that many use co-receptors and alternative receptors to bind to and infect cells. However, the mechanisms by which these viruses release their genomes and transport them across a cellular membrane to gain access to the cytoplasm are still poorly understood. Indeed, detailed studies of cell entry mechanisms have been made only on a few members of the family, and it is yet to be established how broadly the results of these are applicable across the full spectrum of picornaviruses. Working models of the cell entry process are being developed for the best studied picornaviruses, the enteroviruses. These viruses maintain particle integrity throughout the infection process and function as genome delivery modules. However, there is currently no model to explain how viruses such as cardio- and aphthoviruses that appear to simply dissociate into subunits during uncoating deliver their genomes into the cytoplasm.

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Section: Picornavirus Receptorsmentioning

confidence: 99%

Section: Endocytosis and Sites Of Uncoatingmentioning

confidence: 99%

Picornaviruses

Tuthill

Groppelli

Hogle

et al. 2010

Current Topics in Microbiology and Immunology

169

218

View full text Add to dashboard Cite

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“…A soluble form of ICAM-1 (sICAM-1) administered intra nasally, six times daily, to subjects beginning either 7 h before or 12 h after experimental HRV infection reduced symptom scores and nasal secretion weights, and reduced viral titer [29]. A similar proof-of-concept was also established using soluble fragments of the LDL receptor, which inhibited infection [30]. Practical issues of dosing and cost, however, have limited the clinical utility and development of these biological inhibitors of receptor binding.…”

Section: Future Virologymentioning

confidence: 98%

Host Response to Human Rhinovirus Infection: Toward Targeted Treatment Strategies

Proud

2009

Future Virol.

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“…1A). The cDNAs coding for the three proteins contained sequences coding for a C-terminal hexahistidine tail and were subcloned into the pTM1 vector [22], harbouring the baculoviral polyhedrin promotor sequence (ATGbiosynthetics, Merzhausen, Germany). HHM 0 was expressed in Spodoptera frugiperda (Sf9) insect cell line, whereas HHM 1 and HHM 2 were expressed in Trichoplusia ni (High Five) insect cells [23].…”

Section: Expression In Baculovirus-infected Insect Cells and Purification Of Recombinant Glycoproteinsmentioning

confidence: 99%

Recombinant Glycoproteins Resembling Carbohydrate-Specific IgE Epitopes from Plants, Venoms and Mites

et al. 2018

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Background: N-linked glycans present in venoms, pollen and mites are recognized by IgE antibodies from N20% of allergic patients but have low or no allergenic activity. Objectives: To engineer recombinant glycoproteins resembling carbohydrate-specific IgE epitopes from venoms, pollen and mites which can discriminate carbohydrate-specific IgE from allergenic, peptide-specific IgE. Methods: One or two N-glycosylation sites were engineered into the N-terminus of the non-allergenic protein horse heart myoglobin (HHM) using synthetic gene technology. HHM 1 and HHM 2 containing one or two Nglycosylation sites were expressed in baculovirus-infected High-Five™ insect cells and a non-glycosylated version (HHM 0) was obtained by mutating the glycosylation motif. Recombinant HHM proteins were analyzed regarding fold and aggregation by circular dichroism and gel filtration, respectively. IgE reactivity was assessed by ELISA, immunoblotting and quantitative ImmunoCAP measurements. IgE inhibition assays were performed to study cross-reactivity with venom, plant and mite-derived carbohydrate IgE epitopes. Results: HHM-glycovariants were expressed and purified from insect cells as monomeric and folded proteins. The HHM-glycovariants exhibited strictly carbohydrate-specific IgE reactivity, designed to quantify carbohydratespecific IgE and resembled IgE epitopes of pollen, venom and mite-derived carbohydrates. IgE-reactivity and inhibition experiments established a hierarchy of plant glcyoallergens (nPhl p 4 N nCyn d 1 N nPla a 2 N nJug r 2 N nCup a 1 N nCry j 1) indicating a hitherto unknown heterogeneity of carbohydrate IgE epitopes in plants which were completely represented by HHM 2. Conclusion: Defined recombinant HHM-glycoproteins resembling carbohydrate-specific IgE epitopes from plants, venoms and mites were engineered which made it possible to discriminate carbohydrate-from peptide-specific IgE reactivity.

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Recombinant soluble low-density lipoprotein receptor fragment inhibits common cold infection

Cited by 9 publications

References 14 publications

Picornaviruses

Picornaviruses

Host Response to Human Rhinovirus Infection: Toward Targeted Treatment Strategies

Recombinant Glycoproteins Resembling Carbohydrate-Specific IgE Epitopes from Plants, Venoms and Mites

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