Human Rhinovirus

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Tapani Hovi - One of the best experts on this subject based on the ideXlab platform.

  • phylogenetic analysis of Human Rhinovirus capsid protein vp1 and 2a protease coding sequences confirms shared genus like relationships with Human enteroviruses
    Journal of General Virology, 2005
    Co-Authors: Pia Laine, Carita Savolainen, Soile Blomqvist, Tapani Hovi
    Abstract:

    Phylogenetic analysis of the capsid protein VP1 coding sequences of all 101 Human Rhinovirus (HRV) prototype strains revealed two major genetic clusters, similar to that of the previously reported VP4/VP2 coding sequences, representing the established two species, Human Rhinovirus A (HRV-A) and Human Rhinovirus B (HRV-B). Pairwise nucleotide identities varied from 61 to 98 % within and from 46 to 55 % between the two HRV species. Interserotypic sequence identities in both HRV species were more variable than those within any Human enterovirus (HEV) species in the same family. This means that unequivocal serotype identification by VP1 sequence analysis used for HEV strains may not always be possible for HRV isolates. On the other hand, a comprehensive insight into the relationships between VP1 and partial 2A sequences of HRV and HEV revealed a genus-like situation. Distribution of pairwise nucleotide identity values between these genera varied from 41 to 54 % in the VP1 coding region, similar to those between heterologous members of the two HRV species. Alignment of the deduced amino acid sequences revealed more fully conserved amino acid residues between HRV-B and polioviruses than between the two HRV species. In phylogenetic trees, where all HRVs and representatives from all HEV species were included, the two HRV species did not cluster together but behaved like members of the same genus as the HEVs. In conclusion, from a phylogenetic point of view, there are no good reasons to keep these two Human picornavirus genera taxonomically separated.

  • phylogenetic analysis of Human Rhinovirus capsid protein vp1 and 2a protease coding sequences confirms shared genus like relationships with Human enteroviruses
    Journal of General Virology, 2005
    Co-Authors: Pia Laine, Carita Savolainen, Soile Blomqvist, Tapani Hovi
    Abstract:

    Phylogenetic analysis of the capsid protein VP1 coding sequences of all 101 Human Rhinovirus (HRV) prototype strains revealed two major genetic clusters, similar to that of the previously reported VP4/VP2 coding sequences, representing the established two species, Human Rhinovirus A (HRV-A) and Human Rhinovirus B (HRV-B). Pairwise nucleotide identities varied from 61 to 98 % within and from 46 to 55 % between the two HRV species. Interserotypic sequence identities in both HRV species were more variable than those within any Human enterovirus (HEV) species in the same family. This means that unequivocal serotype identification by VP1 sequence analysis used for HEV strains may not always be possible for HRV isolates. On the other hand, a comprehensive insight into the relationships between VP1 and partial 2A sequences of HRV and HEV revealed a genus-like situation. Distribution of pairwise nucleotide identity values between these genera varied from 41 to 54 % in the VP1 coding region, similar to those between heterologous members of the two HRV species. Alignment of the deduced amino acid sequences revealed more fully conserved amino acid residues between HRV-B and polioviruses than between the two HRV species. In phylogenetic trees, where all HRVs and representatives from all HEV species were included, the two HRV species did not cluster together but behaved like members of the same genus as the HEVs. In conclusion, from a phylogenetic point of view, there are no good reasons to keep these two Human picornavirus genera taxonomically separated.

Q. May Wang - One of the best experts on this subject based on the ideXlab platform.

  • Synthesis and evaluation of tripeptidyl α-Ketoamides as Human Rhinovirus 3C protease inhibitors
    Bioorganic & medicinal chemistry letters, 2003
    Co-Authors: Shu-hui Chen, Mark Wakulchik, Beverly A. Heinz, Jason Eric Lamar, Frantz Victor, Nancy June Snyder, Robert B. Johnson, Q. May Wang
    Abstract:

    Abstract We describe herein the synthesis and biological evaluation of a series of tripeptidyl α-ketoamides as Human Rhinovirus (HRV) 3C protease inhibitors. The most potent inhibitor discussed in this manuscript, 4I, exhibited impressive enzyme inhibitory activity as well as antiviral activity against HRV-14.

  • S-nitrosothiols as novel, reversible inhibitors of Human Rhinovirus 3C protease.
    Bioorganic & medicinal chemistry letters, 2000
    Co-Authors: Ming Xian, Q. May Wang, Xinchao Chen, Kun Wang, Peng George Wang
    Abstract:

    Human Rhinovirus (HRV) 3C protease was inactivated by a series of S-nitrosothiols. These compounds exhibited different inhibitory activities in a time- and concentration-dependent manner with second-order rate constants (kinact/K(I)) ranging from 131 to 5360 M(-1) min(-1). The inactive enzyme could be re-activated by DTT, GSH and ascorbate, which indicated the inactivation mechanism was through an S-transnitrosylation process.

  • Identification and Characterization of Human Rhinovirus-14 3C Protease Deamidation Isoform
    The Journal of biological chemistry, 1999
    Co-Authors: Gregory A. Cox, Mark Wakulchik, Elcira C. Villarreal, Robert B. Johnson, James A. Cook, Melvin G. Johnson, Q. May Wang
    Abstract:

    A purified recombinant Human Rhinovirus-14 3C protease preparation contained only ∼50% active enzyme as titrated using specifically designed irreversible 3C protease inhibitors. Analysis of the purified 3C protein by isoelectric focusing showed differently charged 3C isoforms that had isoelectric points (pI) of 8.3 (55%) and 9.0 (45%), with the latter one being consistent with the predicted pI of the Human Rhinovirus-14 3C protein. Further analysis indicated that the pI 8.3 protein was the deamidated form of 3C, and it displayed ∼10-fold reduced cleavage activity relative to the original 3C protease sample. Peptide mapping followed by sequence analysis revealed that a single asparagine, Asn-164, was deamidated to aspartic acid in the pI 8.3 isoform. Converting Asn-164 to Asp by site-directed mutagenesis resulted in a mutated 3C protease with extremely low activity, as seen with the pI 8.3 isoform, indicating a role of Asn-164 in substrate recognition and binding. In addition, the deamidated 3C protease was found to be present in vivo, and its abundance was related to the viral replication cycle. Moreover, mutant virus carrying Asp-164 showed reduced viability in infected cells. Taken together, our data suggest that 3C protein deamidation plays a role in the regulation of its enzymatic activity.

  • Design, synthesis, and evaluation of azapeptides as substrates and inhibitors for Human Rhinovirus 3C protease.
    Bioorganic & medicinal chemistry letters, 1999
    Co-Authors: Shankar Venkatraman, Q. May Wang, Jian She Kong, Sanjay Nimkar, Jeffrey Aubé, Robert P. Hanzlik
    Abstract:

    A series of azapeptides was prepared and assessed as inhibitors of the Human Rhinovirus 3C protease. Boc-VLFaQ-OPh was a slow-turnover substrate that gave transient (ca. 1-2 h) inhibition as it underwent hydrolysis. Boc-VLFaG-OPh gave very slow but essentially irreversible inhibition.

Pia Laine - One of the best experts on this subject based on the ideXlab platform.

  • phylogenetic analysis of Human Rhinovirus capsid protein vp1 and 2a protease coding sequences confirms shared genus like relationships with Human enteroviruses
    Journal of General Virology, 2005
    Co-Authors: Pia Laine, Carita Savolainen, Soile Blomqvist, Tapani Hovi
    Abstract:

    Phylogenetic analysis of the capsid protein VP1 coding sequences of all 101 Human Rhinovirus (HRV) prototype strains revealed two major genetic clusters, similar to that of the previously reported VP4/VP2 coding sequences, representing the established two species, Human Rhinovirus A (HRV-A) and Human Rhinovirus B (HRV-B). Pairwise nucleotide identities varied from 61 to 98 % within and from 46 to 55 % between the two HRV species. Interserotypic sequence identities in both HRV species were more variable than those within any Human enterovirus (HEV) species in the same family. This means that unequivocal serotype identification by VP1 sequence analysis used for HEV strains may not always be possible for HRV isolates. On the other hand, a comprehensive insight into the relationships between VP1 and partial 2A sequences of HRV and HEV revealed a genus-like situation. Distribution of pairwise nucleotide identity values between these genera varied from 41 to 54 % in the VP1 coding region, similar to those between heterologous members of the two HRV species. Alignment of the deduced amino acid sequences revealed more fully conserved amino acid residues between HRV-B and polioviruses than between the two HRV species. In phylogenetic trees, where all HRVs and representatives from all HEV species were included, the two HRV species did not cluster together but behaved like members of the same genus as the HEVs. In conclusion, from a phylogenetic point of view, there are no good reasons to keep these two Human picornavirus genera taxonomically separated.

  • phylogenetic analysis of Human Rhinovirus capsid protein vp1 and 2a protease coding sequences confirms shared genus like relationships with Human enteroviruses
    Journal of General Virology, 2005
    Co-Authors: Pia Laine, Carita Savolainen, Soile Blomqvist, Tapani Hovi
    Abstract:

    Phylogenetic analysis of the capsid protein VP1 coding sequences of all 101 Human Rhinovirus (HRV) prototype strains revealed two major genetic clusters, similar to that of the previously reported VP4/VP2 coding sequences, representing the established two species, Human Rhinovirus A (HRV-A) and Human Rhinovirus B (HRV-B). Pairwise nucleotide identities varied from 61 to 98 % within and from 46 to 55 % between the two HRV species. Interserotypic sequence identities in both HRV species were more variable than those within any Human enterovirus (HEV) species in the same family. This means that unequivocal serotype identification by VP1 sequence analysis used for HEV strains may not always be possible for HRV isolates. On the other hand, a comprehensive insight into the relationships between VP1 and partial 2A sequences of HRV and HEV revealed a genus-like situation. Distribution of pairwise nucleotide identity values between these genera varied from 41 to 54 % in the VP1 coding region, similar to those between heterologous members of the two HRV species. Alignment of the deduced amino acid sequences revealed more fully conserved amino acid residues between HRV-B and polioviruses than between the two HRV species. In phylogenetic trees, where all HRVs and representatives from all HEV species were included, the two HRV species did not cluster together but behaved like members of the same genus as the HEVs. In conclusion, from a phylogenetic point of view, there are no good reasons to keep these two Human picornavirus genera taxonomically separated.

Dieter Blaas - One of the best experts on this subject based on the ideXlab platform.

  • Mechanism of Human Rhinovirus infections
    Molecular and Cellular Pediatrics, 2016
    Co-Authors: Dieter Blaas, Renate Fuchs
    Abstract:

    About 150 Human Rhinovirus serotypes are responsible for more than 50 % of recurrent upper respiratory infections. Despite having similar 3D structures, some bind members of the low-density lipoprotein receptor family, some ICAM-1, and some use CDHR3 for host cell infection. This is also reflected in the pathways exploited for cellular entry. We found that even Rhinovirus serotypes binding the same receptor can travel along different endocytic pathways and release their RNA genome into the cytosol at different locations. How this may account for distinct immune responses elicited by various Rhinoviruses and the observed symptoms of the common cold is briefly discussed.

  • Nanoimaging, Molecular Interaction, and Nanotemplating of Human Rhinovirus
    Scanning Probe Microscopy in Nanoscience and Nanotechnology 2, 2010
    Co-Authors: Markus Kastner, Dieter Blaas, Christian Rankl, Andreas Ebner, Philipp D. Pollheimer, Stefan Howorka, Hermann J. Gruber, Peter Hinterdorfer
    Abstract:

    Capturing and detecting viruses require specialized platforms and analysis techniques. The atomic force microscope (AFM) offers not only tremendously high spatial and topographic resolution, but also allows localizing single molecules and determining their interaction on a molecular level. AFM makes possible (a) generating nanopatterned surfaces, (b) detecting protein and viral pathogen captured in these specific regions over time, and (c) gathering information about binding parameters. A section of this chapter describes, for instance, the measurement of kinetic parameters governing the first step of viral infection – the attachment of a Human Rhinovirus to a cell – at the single-molecule level. We review the principles of AFM and its applications in the analysis of nanopatterned surfaces and protein arrays, in the detection of proteins and viruses, and in the characterization of the interactions of these viruses with their cognate receptors under physiological conditions.

  • Induction of autophagy does not affect Human Rhinovirus type 2 production.
    Journal of virology, 2007
    Co-Authors: Marianne Brabec-zaruba, Dieter Blaas, Ursula Berka, Renate Fuchs
    Abstract:

    Induction of autophagy has been shown to be beneficial for the replication of poliovirus, a phenomenon that might also apply for other picornaviruses. We demonstrate that de novo synthesis of Human Rhinovirus type 2 (HRV2), an HRV of the minor receptor group, is unaffected by tamoxifen, rapamycin, and 3-methyladenine (3-MA), drugs either stimulating (tamoxifen and rapamycin) or inhibiting (3-MA) autophagic processes. Furthermore, LC3-positive vesicles (i.e., autophagosomes) are not induced upon infection. Therefore, multiplication of this particular picornavirus is not dependent on autophagy.

  • Wortmannin delays transfer of Human Rhinovirus serotype 2 to late endocytic compartments.
    Biochemical and biophysical research communications, 2006
    Co-Authors: Marianne Brabec, Dieter Blaas, Renate Fuchs
    Abstract:

    Abstract Human Rhinovirus 2 (HRV2) is internalized by members of the low-density lipoprotein receptor family into early endosomes (pH 6.2–6.0) where it dissociates from its receptors. After transfer into late endosomes, the virus undergoes a conformational change and RNA uncoating solely induced by pH

  • Fluorescence labeling of Human Rhinovirus capsid and analysis by capillary electrophoresis.
    Analytical chemistry, 2004
    Co-Authors: Leopold Kremser, Dieter Blaas, Tünde Konecsni, Ernst Kenndler
    Abstract:

    The capsid of Human Rhinovirus serotype 2, consisting of four viral proteins, was fluorescence-labeled with fluorescein isothiocyanate and analyzed by capillary electrophoresis using UV and laser-induced fluorescence detection. Heat denaturation, proteolytic digestion, and receptor binding were applied for confirmation of the identity of the peak with the labeled virus. Incomplete derivatization with the fluorophore preserved the affinity of the virus for its receptor, indicating that its cell entry pathway is unperturbed by this chemical modification; indeed, an infectivity assay confirms that the labeled virus samples are infectious. The results show that fluorescence labeling of the viral capsid might lead to a valuable probe for studying infection processes in the living cell.

Beverly A. Heinz - One of the best experts on this subject based on the ideXlab platform.

  • Synthesis and evaluation of tripeptidyl α-Ketoamides as Human Rhinovirus 3C protease inhibitors
    Bioorganic & medicinal chemistry letters, 2003
    Co-Authors: Shu-hui Chen, Mark Wakulchik, Beverly A. Heinz, Jason Eric Lamar, Frantz Victor, Nancy June Snyder, Robert B. Johnson, Q. May Wang
    Abstract:

    Abstract We describe herein the synthesis and biological evaluation of a series of tripeptidyl α-ketoamides as Human Rhinovirus (HRV) 3C protease inhibitors. The most potent inhibitor discussed in this manuscript, 4I, exhibited impressive enzyme inhibitory activity as well as antiviral activity against HRV-14.

  • Glutamine-derived aldehydes for the inhibition of Human Rhinovirus 3C protease
    Bioorganic & Medicinal Chemistry Letters, 1995
    Co-Authors: Stephen W. Kaldor, M. Hammond, Bruce A. Dressman, J. M. Labus, F. W. Chadwell, Allen D. Kline, Beverly A. Heinz
    Abstract:

    Peptide aldehydes have been synthesized and evaluated as inhibitors of Human Rhinovirus 3C protease. Those inhibitors containing a C-terminal glutamine aldehyde were prepared using newly developed methodology involving reduction of the corresponding glutarimide, which can be easily prepared from N-protected glutamine. Low molecular weight (

  • WIN 52035-2 inhibits both attachment and eclipse of Human Rhinovirus 14
    Journal of virology, 1993
    Co-Authors: D. Shepard, Beverly A. Heinz, Roland R. Rueckert
    Abstract:

    WIN compounds inhibit attachment of Human Rhinovirus 14 by binding to a hydrophobic pocket within the capsid and inducing conformational changes in the canyon floor, the region that binds the cellular receptor. To study the basis of drug resistance, we isolated and characterized a family of Human Rhinovirus 14 mutants resistant to WIN 52035-2. Thermostabilization data and single-cycle growth curves provided evidence for two classes of resistant mutants. One class, here called exclusion mutants, showed a marked decrease in drug-binding affinity and was characterized by substitution to bulkier amino acid side chains at two sites lining the hydrophobic pocket. The other class, called compensation mutants, displayed single-amino-acid substitutions in the drug-deformable regions of the canyon; these mutants were able to attach to cells despite the presence of bound drug. A delay in the rise period of the growth curves of compensation mutants indicated a second locus of drug action. WIN 52035-2 was found to inhibit the first step of uncoating, release of VP4. Attempts to identify this site of drug action by using single-step growth curves were obscured by abortive elution of a major fraction of cell-attached virus. The drug had no effect on the rate of this process but did affect the spectrum of particles produced.