scholarly journals An Outbreak of Exanthematous Disease due to Coxsackievirus A9 in a Nursery in Yamagata, Japan, from February to March 2012

2012 ◽  
Vol 65 (4) ◽  
pp. 367-369 ◽  
Author(s):  
Yoko Aoki ◽  
Akiko Abe ◽  
Tatsuya Ikeda ◽  
Chieko Abiko ◽  
Katsumi Mizuta ◽  
...  
Keyword(s):  
Coxsackievirus A9

scholarly journals 1140 THE EFFECT OF AN ANTIVIRAL AGENT (WIN 51,711) ON COXSACKIEVIRUS A9 INFECTION IN SUCKLING MICE

1985 ◽  
Vol 19 (4) ◽  
pp. 300A-300A
Author(s):  
Ross E McKinney ◽  
Thomas J Maroon ◽  
Catherine M Wilfert
Keyword(s):  
Antiviral Agent ◽  
Suckling Mice ◽  
Coxsackievirus A9

scholarly journals THE ROLE OF THE NEONATAL FC RECEPTOR IN THE UNCOATING OF ECHOVIRUSES AND COXSACKIEVIRUS A9

2019 ◽  
Vol 64 (3) ◽  
pp. 132-139
Author(s):  
P. S. Usoltseva ◽  
A. V. Alimov ◽  
A. V. Rezaykin ◽  
A. G. Sergeev ◽  
A. V. Novoselov
Keyword(s):  
Protective Effect ◽  
Cellular Receptor ◽  
Protective Effects ◽  
Neonatal Fc Receptor ◽  
Receptor Specificity ◽  
Cellular Receptors ◽  
Coxsackievirus A9 ◽  
Rd Cells ◽  
Adenovirus Receptor

The aim of this study was to determine the role of the human neonatal receptor for the Fc fragment of IgG (hFcRn) as a common uncoating cellular receptor for echoviruses and coxsackievirus A9 during infection of human rhabdomyosarcoma (RD) cells. Material and methods. The protective effect of the human serum albumin, purified from globulins, (HSA-GF) and antibodies to hFcRn was studied in RD cells infected with several strains and clones of species B enteroviruses possessing different receptor specificity (echoviruses 3, 9, 11, 30 and coxsackieviruses A9, B4, B5). Results. It was shown that HSA-GF at concentrations of 4% or less protected RD cells from infection with echoviruses 3, 9, 11 and coxsackievirus A9. The antibodies to hFcRn at concentrations of 2.5 ug/mL or less demonstrated the similar spectrum of protective activity in RD cells against infection with echoviruses 3, 9, 11, 30 and coxsackievirus A9. The protective effect of HSA-GF or the antibodies to hFcRn was not observed in RD cells infected with coxsackieviruses B4 and B5 that need coxsackievirus-adenovirus receptor for uncoating. Discussion. The usage of the previously characterized echovirus 11 clonal variants with different receptor specificity allowed us to define the function of hFcRn as a canyon-binding uncoating receptor in RD cells. The kinetics and magnitude of the observed protective effects correlated with receptor specificity of the enteroviruses used in this work supporting the two-step interaction of DAF-dependent echoviruses with the cellular receptors. Conclusions. In this study, the function of hFcRn was defined in RD cells as a canyon-binding and uncoating receptor for echoviruses and coxsackievirus A9. The two-step interaction of DAF-dependent echoviruses during entry into the cells was confirmed: initially with the binding receptor DAF and subsequently with the uncoating receptor hFcRn.

scholarly journals The crystal structure of coxsackievirus A9: new insights into the uncoating mechanisms of enteroviruses

Structure ◽  
1999 ◽  
Vol 7 (12) ◽  
pp. 1527-1538 ◽  
Author(s):  
Elaine Hendry ◽  
Hideki Hatanaka ◽  
Elizabeth Fry ◽  
Michael Smyth ◽  
John Tate ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Coxsackievirus A9

scholarly journals Endocytosis of Integrin-Binding Human Picornaviruses

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Pirjo Merilahti ◽  
Satu Koskinen ◽  
Outi Heikkilä ◽  
Eveliina Karelehto ◽  
Petri Susi
Keyword(s):  
Economic Importance ◽  
Integrin Receptors ◽  
Human Parechovirus ◽  
Collagen Binding ◽  
Cellular Receptors ◽  
Disease Symptoms ◽  
Receptor Endocytosis ◽  
Wide Range ◽  
Coxsackievirus A9 ◽  
Picornavirus Infection

Picornaviruses that infect humans form one of the largest virus groups with almost three hundred virus types. They include significant enteroviral pathogens such as rhino-, polio-, echo-, and coxsackieviruses and human parechoviruses that cause wide range of disease symptoms. Despite the economic importance of picornaviruses, there are no antivirals. More than ten cellular receptors are known to participate in picornavirus infection, but experimental evidence of their role in cellular infection has been shown for only about twenty picornavirus types. Three enterovirus types and one parechovirus have experimentally been shown to bind and use integrin receptors in cellular infection. These include coxsackievirus A9 (CV-A9), echovirus 9, and human parechovirus 1 that are among the most common and epidemic human picornaviruses and bind toαV-integrins via RGD motif that resides on virus capsid. In contrast, echovirus 1 (E-1) has no RGD and uses integrinα2β1 as cellular receptor. Endocytosis of CV-A9 has recently been shown to occur via a novel Arf6- and dynamin-dependent pathways, while, contrary to collagen binding, E-1 binds inactiveβ1 integrin and enters via macropinocytosis. In this paper, we review what is known about receptors and endocytosis of integrin-binding human picornaviruses.

scholarly journals Inhibition of coxsackievirus B3 and related enteroviruses by antiviral short interfering RNA pools produced using φ6 RNA-dependent RNA polymerase

2009 ◽  
Vol 90 (10) ◽  
pp. 2468-2473 ◽  
Author(s):  
Michaela Nygårdas ◽  
Tytti Vuorinen ◽  
Antti P. Aalto ◽  
Dennis H. Bamford ◽  
Veijo Hukkanen
Keyword(s):  
Rna Polymerase ◽  
Genomic Sequence ◽  
Coxsackievirus B3 ◽  
Human Enterovirus ◽  
Rna Dependent Rna Polymerase ◽  
Coxsackievirus B4 ◽  
Novel Approach ◽  
Experimental Therapies ◽  
Coxsackievirus A9 ◽  
Interfering Rna

Coxsackievirus B3 (CBV3) is a member of the human enterovirus B species and a common human pathogen. Even though much is known about the enteroviral life cycle, no specific drugs are available to treat enterovirus infections. RNA interference (RNAi) has evolved to be an important tool for antiviral experimental therapies and gene function studies. We describe here a novel approach for RNAi against CBVs by using a short interfering (siRNA) pool covering 3.5 kb of CBV3 genomic sequence. The RNA-dependent RNA polymerase (RdRP) of bacteriophage φ6 was used to synthesize long double-stranded RNA (dsRNA) from a cloned region (nt 3837–7399) of the CBV3 genome. The dsRNA was cleaved using Dicer, purified and introduced to cells by transfection. The siRNA pool synthesized using the φ6 RdRP (φ6–siRNAs) was considerably more effective than single-site siRNAs. The φ6–siRNA pool also inhibited replication of other enterovirus B species, such as coxsackievirus B4 and coxsackievirus A9.

scholarly journals Foot-and-mouth disease virus can utilize the C-terminal extension of coxsackievirus A9 VP1 for cell infection

2001 ◽  
Vol 82 (7) ◽  
pp. 1703-1711 ◽  
Author(s):  
Martina Leippert ◽  
Eberhard Pfaff
Keyword(s):  
Amino Acid ◽  
Disease Virus ◽  
Genetically Modified ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Cell Infection ◽  
Bhk Cells ◽  
Mouth Disease Virus ◽  
Coxsackievirus A9 ◽  
Foot And Mouth

Foot-and-mouth disease virus (FMDV) is known to employ the conserved Arg–Gly–Asp (RGD) tripeptide located on the variable βG–βH loop of the VP1 capsid protein for binding to cells. Coxsackievirus A9 (CAV9) also carries an RGD sequence, but on a short C-terminal extension of its VP1 and in a different amino acid context. This apparent relationship raised the question of whether insertion of the heterologous CAV9 sequence into FMDV would influence infection by the genetically modified FMDV. Four VP1 mutants were generated by PCR mutagenesis of a full-length FMDV cDNA plasmid. After transfection of BHK-21 cells, viral protein synthesis and virus particle formation could be detected. Two of the four mutants, mV9b and mV9d, could be propagated in BHK-21 cells, but not in CV-1 cells. Both of these mutants contained 17 amino acids of the C terminus of CAV9 VP1. Infection of BHK cells could be specifically inhibited by rabbit immune serum raised against a synthetic peptide representing the amino acid sequence of the C-terminal extension of CAV9 VP1. This demonstrated the direct involvement of the inserted sequence in cell infection. In fact, genetically modified FMDV O1K was capable of employing the VP1 C-terminal RGD region of CAV9 for infection of BHK cells. In addition, these results show that, even in cell culture-adapted viruses, the RGD-containing βG–βH loop plays an important role in virus infectivity.

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