Cellular receptor interactions of C-cluster human group A coxsackieviruses

Newcombe, Nicole G.; Andersson, Per; Johansson, E. Susanne; Au, Gough G.; Lindberg, Anders; Barry, Richard D.; Shafren, Darren R.

doi:10.1099/vir.0.19329-0

Cited by 43 publications

(31 citation statements)

References 37 publications

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“…Rhabdomyosarcoma cells stably transfected with human ICAM-1 (RD-ICAM), a kind gift of Darren Shafren (University of Newcastle, Australia), were cultured as previously described (25,36). HeLa-H1 cells were grown in minimal essential medium (MEM) supplemented with 10% heat-inactivated fetal calf serum (FCS), 100 U/ml penicillin, 100 g/ml streptomycin, and 2 mM L-glutamine.…”

Section: Cells and Virusesmentioning

confidence: 99%

Human Rhinovirus 14 Enters Rhabdomyosarcoma Cells Expressing ICAM-1 by a Clathrin-, Caveolin-, and Flotillin-Independent Pathway

Khan

Pickl‐Herk

Gajdzik

et al. 2010

J Virol

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Intercellular adhesion molecule 1 (ICAM-1) mediates binding and entry of major group human rhinoviruses (HRVs). Whereas the entry pathway of minor group HRVs has been studied in detail and is comparatively well understood, the pathway taken by major group HRVs is largely unknown. Use of immunofluorescence microscopy, colocalization with specific endocytic markers, dominant negative mutants, and pharmacological inhibitors allowed us to demonstrate that the major group virus HRV14 enters rhabdomyosarcoma cells transfected to express human ICAM-1 in a clathrin-, caveolin-, and flotillin-independent manner. Electron microscopy revealed that many virions accumulated in long tubular structures, easily distinguishable from clathrin-coated pits and caveolae. Virus entry was strongly sensitive to the Na ؉ /H ؉ ion exchange inhibitor amiloride and moderately sensitive to cytochalasin D. Thus, cellular uptake of HRV14 occurs via a pathway exhibiting some, but not all, characteristics of macropinocytosis and is similar to that recently described for adenovirus 3 entry via ␣ v integrin/CD46 in HeLa cells.

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Section: Cells and Virusesmentioning

confidence: 99%

Human Rhinovirus 14 Enters Rhabdomyosarcoma Cells Expressing ICAM-1 by a Clathrin-, Caveolin-, and Flotillin-Independent Pathway

Khan

Pickl‐Herk

Gajdzik

et al. 2010

J Virol

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“…Viral RNA was extracted from the CVA21 parental and CVA21-DAFv strains by using the QIAamp viral RNA mini kit, and the capsid-coding region was amplified by one-step reverse transcription-PCR (RT-PCR) (Qiagen OneStep RT-PCR kit) as specified by the manufacturer, using CVA21-specific primers (29). The nucleotide sequences were determined using purified PCR products (QIAquick gel extraction kit; QIAGEN GmbH) in a cycle-sequencing reaction using the ABI Prism BigDye terminator cycle-sequencing ready reaction kit (PE Biosystems) as specified by the manufacturer.…”

Section: Sedimentation Of Daf-and Icam-1-bound Virionsmentioning

confidence: 99%

Enhanced Cellular Receptor Usage by a Bioselected Variant of Coxsackievirus A21

Johansson

Cheng

et al. 2004

J Virol

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Decay-accelerating factor (DAF) functions as cell attachment receptor for a wide range of human enteroviruses. The Kuykendall prototype strain of coxsackievirus A21 (CVA21) attaches to DAF but requires interactions with intercellular cell adhesion molecule 1 (ICAM-1) to infect cells. We show here that a bioselected variant of CVA21 (CVA21-DAFv) generated by multiple passages in DAF-expressing, ICAM-1-negative rhabdomyosarcoma (RD) cells acquired the capacity to induce rapid and complete lysis of ICAM-1-deficient cells while retaining the capacity to bind ICAM-1. CVA21-DAFv binding to DAF on RD cells mediated lytic infection and was inhibited by either antibody blockade with a specific anti-DAF SCR1 monoclonal antibody (MAb) or soluble human DAF. Despite being bioselected in RD cells, CVA21-DAFv was able to lytically infect an additional ICAM-1-negative cancer cell line via DAF interactions alone. The finding that radiolabeled CVA21-DAFv virions are less readily eluted from surface-expressed DAF than are parental CVA21 virions during a competitive epitope challenge by an anti-DAF SCR1 MAb suggests that interactions between CVA21-DAFv and DAF are of higher affinity than those of the parental strain. Nucleotide sequence analysis of the capsid-coding region of the CVA21-DAFv revealed the presence of two amino acid substitutions in capsid protein VP3 (R96H and E101A), possibly conferring the enhanced DAF-binding phenotype of CVA21-DAFv. These residues are predicted to be embedded at the interface of VP1, VP2, and VP3 and are postulated to enhance the affinity of DAF interaction occurring outside the capsid canyon. Taken together, the data clearly demonstrate an enhanced DAF-using phenotype and expanded receptor utilization of CVA21-DAFv compared to the parental strain, further highlighting that capsid interactions with DAF alone facilitate rapid multicycle lytic cell infection.The attachment of viruses to cell surface molecules is the initial step of virus replication, and specific cellular virus receptors are therefore major determinants for virus tissue tropism. Decay-accelerating factor (DAF; CD55), a 70-kDa glycosylphosphatidylinositol-anchored complement-regulatory protein consisting of four extracellular short consensus repeats (SCRs) (25), serves as a membrane attachment protein for numerous human enteroviruses, including several echoviruses (EV) (4,20,36,48), coxsackie B viruses (CVB) (41) and coxsackievirus A21 (CVA21) (43). In general, viral binding to DAF alone is insufficient to permit enteroviral infections and interactions with DAF do not induce 135S altered (A) particles (34,35,39,43,45), which are considered to be a prerequisite for cell entry (2, 50). The physiological role of DAF for enteroviral infections is postulated to be that of a membrane concentration receptor that binds and clusters the infectious virus, resulting in increased opportunity for cell entry via interactions with a second functional cell entry receptor (30,43,45).As with many other picornaviruses (the polioviruses, the major-rece...

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“…Intercellular adhesion molecule 1 (ICAM-1) is used as a receptor by many pathogens, including the major group of human rhinoviruses (HRVs) (16,29) and some coxsackieviruses (e.g., CVA13, CVA15, CVA18, CVA20, and CVA21) (34,57). In addition, when erythrocytes are infected by the malarial parasite, Plasmodium falciparum, they gain the ability to bind cells expressing ICAM-1 (7,35).…”

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confidence: 99%