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Open Access Highly Accessed Research article

Cell surface sialylation affects binding of enterovirus 71 to rhabdomyosarcoma and neuroblastoma cells

Pei-Yi Su23, Yueh-Tung Liu16, Hsin-Yueh Chang13, Sheng-Wen Huang123, Ya-Fang Wang13, Chun-Keung Yu2345, Jen-Ren Wang123 and Chuan-Fa Chang123*

Author Affiliations

1 Department of Medical Laboratory Science and Biotechnology, National Cheng Kung University, No. 1, University Road, Tainan 70101, Taiwan

2 Institute of Basic Medical Sciences, National Cheng Kung University, No. 1, University Road, Tainan 70101, Taiwan

3 Center of Infectious Disease and Signaling Research, Medical College, National Cheng Kung University, No. 1, University Road, Tainan 70101, Taiwan

4 Department of Microbiology and Immunology, National Cheng Kung University, No. 1, University Road, Tainan 70101, Taiwan

5 National Applied Research Laboratories, National Laboratory Animal Center, No. 128 Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan

6 Blood Bank, Kaohsiung Veterans General Hospital, No. 386, Ta-Chung 1st Road, Kaohsiung 81362, Taiwan

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BMC Microbiology 2012, 12:162  doi:10.1186/1471-2180-12-162

Published: 1 August 2012

Abstract

Background

Enterovirus 71 (EV71) is a major causative agent of hand-foot-and-mouth disease (HFMD), and infection of EV71 to central nerve system (CNS) may result in a high mortality in children less than 2 years old. Although there are two highly glycosylated membrane proteins, SCARB2 and PSGL-1, which have been identified as the cellular and functional receptors of EV71, the role of glycosylation in EV71 infection is still unclear.

Results

We demonstrated that the attachment of EV71 to RD and SK-N-SH cells was diminished after the removal of cell surface sialic acids by neuraminidase. Sialic acid specific lectins, Maackia amurensis (MAA) and Sambucus Nigra (SNA), could compete with EV71 and restrained the binding of EV71 significantly. Preincubation of RD cells with fetuin also reduced the binding of EV71. In addition, we found that SCARB2 was a sialylated glycoprotein and interaction between SCARB2 and EV71 was retarded after desialylation.

Conclusions

In this study, we demonstrated that cell surface sialic acids assist in the attachment of EV71 to host cells. Cell surface sialylation should be a key regulator that facilitates the binding and infection of EV71 to RD and SK-N-SH cells.

Keywords:
Enterovirus 71; Sialic acid; RD; SK-N-SH; Lectin affinity chromatography