Initial evidence on differences among Enterovirus 71, Coxsackievirus A16 and Coxsackievirus B4 in binding to cell surface hepaan sulphate

Journal article


Pourianfar, Hamid Reza, Kirk, Kristin and Grollo, Lara. (2014). Initial evidence on differences among Enterovirus 71, Coxsackievirus A16 and Coxsackievirus B4 in binding to cell surface hepaan sulphate. VirusDisease. 25(3), pp. 277 - 284. https://doi.org/10.1007/s13337-013-0172-x
AuthorsPourianfar, Hamid Reza, Kirk, Kristin and Grollo, Lara
Abstract

Cell surface heparan sulphate (HS) mediates infection for many viruses from diverse families. We demonstrated significant antiviral potencies for a number of HS mimetics against a cloned strain of Enterovirus 71 (EV71) in a previous study. Thus, the involvement of HS in mediating viral infection of isolates of human enteroviruses was investigated in Vero and human neural cells in the present work. In both cell lines, heparin and pentosan polysulphate significantly inhibited both infection and attachment of low passage clinical isolates of EV71 and Coxsackievirus A16 (CVA16) but showed no affect on Coxsackievirus B4 (CVB4) (p < 0.05). In addition, enzymatic removal of cell surface HS by heparinase I prevented binding of the clinical EV71 by nearly 50 % but failed to significantly inhibit CVA16 or CVB4 binding in Vero cells. Overall, the findings of this study provides evidence that whilst highly sulphated domains of HS serve as an essential attachment co-receptor for EV71, HS might be used as an alternative attachment receptor by the other member of Human Enterovirus group A, CVA16. In addition, HS may not mediate early infection in CVB4.

Keywordshuman enterovirus 71; heparan sulphate; viral attachment; virus receptor
Year2014
JournalVirusDisease
Journal citation25 (3), pp. 277 - 284
PublisherSpringer (India) Private Ltd.
ISSN2347-3517
Digital Object Identifier (DOI)https://doi.org/10.1007/s13337-013-0172-x
Page range277 - 284
Research GroupSchool of Behavioural and Health Sciences
Publisher's version
File Access Level
Controlled
Place of publicationIndia
EditorsB. Mandal
Permalink -

https://acuresearchbank.acu.edu.au/item/87zz8/initial-evidence-on-differences-among-enterovirus-71-coxsackievirus-a16-and-coxsackievirus-b4-in-binding-to-cell-surface-hepaan-sulphate

Restricted files

Publisher's version

  • 94
    total views
  • 0
    total downloads
  • 1
    views this month
  • 0
    downloads this month
These values are for the period from 19th October 2020, when this repository was created.

Export as

Related outputs

Salivary blockade protects the lower respiratory tract of mice from lethal influenza virus infection
Ivinson, Karen, Deliyannis, Georgia, McNabb, Leanne, Grollo, Lara, Gilbertson, Brad, Jackson, David and Brown, Lorena E.. (2017). Salivary blockade protects the lower respiratory tract of mice from lethal influenza virus infection. Journal of Virology. 91(14), pp. 1 - 12. https://doi.org/10.1128/JVI.00624-17
Synthetic B-Cell epitopes eliciting cross-neutralizing antibodies: Strategies for future dengue vaccine
Ramanathan, Babu, Poh, Chit L., Kirk, Kristin, McBride, William John Hannan, Aaskov, John and Grollo, Lara. (2016). Synthetic B-Cell epitopes eliciting cross-neutralizing antibodies: Strategies for future dengue vaccine. PLoS ONE. 11(5), pp. 1 - 22. https://doi.org/10.1371/journal.pone.0155900
Enterovirus-specific anti-peptide antibodies
Poh, Chit Laa, Kirk, Katherine, Chua, Hui Na and Grollo, Lara. (2015). Enterovirus-specific anti-peptide antibodies. In In Houen, Gunnar (Ed.). Peptide antibodies methods and protocols pp. 341-350 Humana Press. https://doi.org/10.1007/978-1-4939-2999-3_29
Development of antiviral agents toward enterovirus 71 infection
Pourianfar, Hamid Reza and Grollo, Lara. (2015). Development of antiviral agents toward enterovirus 71 infection. Journal of Microbiology Immunology and Infection. 48(1), pp. 1 - 8. https://doi.org/10.1016/j.jmii.2013.11.011
Evidence of synergistic activity of medicinal plant extracts against neuraminidase inhibitor resistant strains of influenza
Rajasekaran, Dhivya, Palombo, Enzo, Yeo, Tiong Chia, Ley, Diana, Tu, Chu Lee, Malherbe, Francois and Grollo, Lara. (2014). Evidence of synergistic activity of medicinal plant extracts against neuraminidase inhibitor resistant strains of influenza. Advances in Microbiology. 4(16), pp. 1260 - 1277. https://doi.org/10.4236/aim.2014.416136
Global impact of heparin on gene expression profiles in neural cells infected by Enterovirus 71
Pourianfar, H. R., Palombo, E. and Grollo, L.. (2014). Global impact of heparin on gene expression profiles in neural cells infected by Enterovirus 71. Intervirology: international journal of basic and medical virology. 57(2), pp. 93 - 100. https://doi.org/10.1159/000355872
Identification of traditional medicinal plant extracts with novel anti-influenza activity
Rajasekaran, Dhivya, Palombo, Enzo, Yeo, Tiong Chia, Ley, Diana, Tu, Chu, Malherbe, Francois and Grollo, Lara. (2013). Identification of traditional medicinal plant extracts with novel anti-influenza activity. PLoS One (online). 8(11), pp. 1 - 15. https://doi.org/10.1371/journal.pone.0079293
In vitro evaluation of the antiviral activity of heparan sulfate mimetic compounds against Enterovirus 71
Pourianfar, Hamid, Poh, Chit Laa, Fecondo, John and Grollo, Lara. (2012). In vitro evaluation of the antiviral activity of heparan sulfate mimetic compounds against Enterovirus 71. Virus Research. 169(1), pp. 22 - 29. https://doi.org/10.1016/j.virusres.2012.06.025
A colorimetric-based accurate method for the determination of enterovirus 71 titer
Pourianfar, Hamid Reza, Javadi, Arman and Grollo, Lara. (2012). A colorimetric-based accurate method for the determination of enterovirus 71 titer. Indian Journal of Virology. 23(3), pp. 303 - 310. https://doi.org/10.1007/s13337-012-0105-0
Cross-reactive neutralizing antibody epitopes against Enterovirus 71 identified by an in silico approach
Kirk, Kristin, Poh, Chit Lau, Fecondo, John, Shaw, Jillian and Grollo, Lara. (2012). Cross-reactive neutralizing antibody epitopes against Enterovirus 71 identified by an in silico approach. Vaccine. 30(49), pp. 7105 - 7110. https://doi.org/10.1016/j.vaccine.2012.09.030