Mechanism of entry of human rhinovirus 2 into HeLa cells

Neubauer, Christoph; Frasel, Lela; Kuechler, Ernst; Blaas, Dieter

doi:10.1016/0042-6822(87)90264-9

Cited by 97 publications

(113 citation statements)

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“…These structural alterations of the capsid are thought to be a prerequisite for uncoating (Lonberg-Holm & Whiteley, 1976;Neubauer et al, 1987). This change of structure has also been observed in vitro upon incubation of virions at low pH or at 56 °C (Korant et al, 1972;Kowalski et al, 1989).…”

mentioning

confidence: 73%

“…Changes induced by incubation at low pH in vitro were monitored using monoclonal antibody (MAb) 2G2. This MAb has been shown to recognize an antigenic determinant that appears upon incubation of HRV-2 at a pH of around 5-5 but which is absent on native virions (Neubauer et al, 1987). The compounds were selected to cover a wide range of minimal inhibitory concentrations (MICs) against HRV-2.…”

mentioning

confidence: 99%

“…[3SS]methionine-labelled HRV-2 (Neubauer et al, 1987) was preincubated with or without the antiviral compounds for 60 min at 20 °C in 300 rtl phosphate-buffered saline. The pH was adjusted with 1 M-sodium acetate buffer to the values shown in Fig.…”

mentioning

confidence: 99%

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Stabilization of human rhinovirus serotype 2 against pH-induced conformational change by antiviral compounds

Gruenberger

Pevear²,

Diana

et al. 1991

Journal of General Virology

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Four WIN compounds with anti-picornavirus activities were tested for their ability to stabilize human rhinovirus serotype 2 (HRV-2) against low pH-induced conformational changes in vitro, as determined by specific immunoprecipitation. These results were compared to the minimal inhibitory concentration (MIC) as measured in a plaque reduction assay. A direct relationship was observed between the concentration of the compound that prevented the low pH-induced conformational changes and the MIC, indicating that stabilization is an important element in the mode of action of these drugs against HRV-2.

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confidence: 73%

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confidence: 99%

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Stabilization of human rhinovirus serotype 2 against pH-induced conformational change by antiviral compounds

Gruenberger

Pevear²,

Diana

et al. 1991

Journal of General Virology

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“…We therefore used a similar approach to assess the specificity of these serotypes for the LDL receptor family. Virus was metabolically radiolabeled with [ 35 S]cysteine-methionine (23). In order to increase the sensitivity of the assay, immortalized mouse fibroblasts (M4), deficient in endogenous LDLR and LRP (13,39), that had been stably transfected to express a truncated version of human LDLR were used.…”

Section: Resultsmentioning

confidence: 99%

“…As a consequence of the deletion of the amino acid sequence motif responsible for clathrin-mediated endocytosis, large amounts of the receptor accumulate at the plasma membrane, thereby increasing the sensitivity of the assay (28); plasma membrane extracts from immortalized M1 mouse wild-type (wt) fibroblasts were used to compare virus binding to the mouse and the human receptor homologues. Virus overlay blotting was carried out as detailed by Mischak and colleagues (21) using 35 S-labeled HRVs (23), and virus binding to the receptor was revealed by exposure of the blot to Kodak X-ray film.…”

Section: Methodsmentioning

confidence: 99%

The Minor Receptor Group of Human Rhinovirus (HRV) Includes HRV23 and HRV25, but the Presence of a Lysine in the VP1 HI Loop Is Not Sufficient for Receptor Binding

Vlasak

Roivainen

Reithmayer

et al. 2005

J Virol

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Like all 10 minor receptor group human rhinoviruses (HRVs), HRV23 and HRV25, previously classified as major group viruses, are neutralized by maltose binding protein (MBP)-V33333 (a soluble recombinant concatemer of five copies of repeat 3 of the very-low-density lipoprotein receptor fused to MBP), bind to low-density lipoprotein receptor in virus overlay blots, and replicate in intercellular adhesion molecule 1 (ICAM-1)-negative COS-7 cells. From phylogenetic analysis of capsid protein VP1-coding sequences, they are also known to cluster together with other minor group strains. Therefore, they belong to the minor group; there are now 12 minor group and 87 major group HRV serotypes. Sequence comparison of the VP1 capsid proteins of all HRVs revealed that the lysine in the HI loop, strictly conserved in the 12 minor group HRVs, is also present in 9 major group serotypes that are neutralized by soluble ICAM-1. Despite the presence of this lysine, they are not neutralized by MBP-V33333 and fail to replicate in COS-7 cells and in HeLa cells in the presence of an ICAM-1-blocking antibody. These nine serotypes are therefore "true" major group viruses.Human rhinoviruses (HRVs), the main causative agents of common cold, were originally classified as acid-sensitive picornaviruses (34). Later, based on competition for cellular binding sites, two different groups of viruses using nonidentical receptors for cell attachment were defined within the genus Rhinovirus (18). Subsequently, 24 (1) and finally 100 serotypes (counting the subtypes HRV1A and HRV1B as one strain) were assigned to the two receptor groups by using cross-competition and inhibition of cell binding by a monoclonal antibody recognizing intercellular adhesion molecule 1 (ICAM-1), the receptor of the major group of HRVs (32,33,35). According to these reports, 90 serotypes bind ICAM-1, whereas both subtypes of HRV1 (HRV1A and HRV1B) and 8 other serotypes were categorized as belonging to the minor group; they were later shown to use members of the low-density-lipoprotein receptor (LDLR) family for cell entry (12,20,36). HRV87 was noted to be an exception in that it binds a sialylated membrane protein. Based on comparison of nucleotide sequences in several genomic regions, HRV87 was subsequently classified as an acid-sensitive enterovirus and found to be a prime strain of enterovirus 68 that uses decay-accelerating factor as a receptor (2,27). By phylogenetic analysis of capsid protein VP4/VP2 coding sequences of all HRV prototype strains, 74 HRV serotypes, including all the minor receptor group ones, were classified as HRV species A, while the 25 remaining serotypes form HRV species B (27). In a paper from the Colonno group, primary data on the competition with an ICAM-1-blocking antibody were not explicitly presented for all serotypes, in particular not for HRV23 and HRV25, and the presumed allocation of all HRVs to either group was depicted only in the form of a summarizing figure (35). Despite this, it was generally accepted that 90 serotypes, including HRV23...

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Antigen processing and presentation of human rhinovirus to CD4 T cells is facilitated by binding to cellular receptors for virus

Hastings¹,

Francis²,

Rowlands³

et al. 1993

Eur J Immunol

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Human rhinovirus serotypes (HRV) fall into two distinct groups, major and minor, by virtue of their cell receptor-binding ability. In this study minor receptor-binding group viruses are demonstrated to bind directly to cells of the murine immune system, including lymphoid dendritic cells which act as antigen-presenting cells, although they do not produce a productive infection in murine cells. This binding is specific and can be blocked by other serotypes of minor-group HRV. Pre-treatment of HRV 1A, a minor-group virus, with HRV 1A-specific antibodies inhibited the cellular proliferation of murine virus primed T helper cells, whereas antibody treatment of HRV 15, a non-binding major serotype, gave no inhibition. The cell binding ability of minor-group HRV played a role in the overall immunogenicity of this virus group, which was shown to be enhanced compared to the immunogenicity of major-group viruses in mice.

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Mechanism of entry of human rhinovirus 2 into HeLa cells

Cited by 97 publications

References 20 publications

Stabilization of human rhinovirus serotype 2 against pH-induced conformational change by antiviral compounds

Stabilization of human rhinovirus serotype 2 against pH-induced conformational change by antiviral compounds

The Minor Receptor Group of Human Rhinovirus (HRV) Includes HRV23 and HRV25, but the Presence of a Lysine in the VP1 HI Loop Is Not Sufficient for Receptor Binding

Antigen processing and presentation of human rhinovirus to CD4 T cells is facilitated by binding to cellular receptors for virus

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