title: Cell surface sialylation affects binding of enterovirus 71 to rhabdomyosarcoma and neuroblastoma cells.
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.
authors.affiliation: Department of Medical Laboratory Science and Biotechnology, National Cheng Kung University, Tainan, Taiwan.
authors.forename: Pei-Yi
authors.initials: PY
authors.lastname: Su
authors.forename: Yueh-Tung
authors.initials: YT
authors.lastname: Liu
authors.forename: Hsin-Yueh
authors.initials: HY
authors.lastname: Chang
authors.forename: Sheng-Wen
authors.initials: SW
authors.lastname: Huang
authors.forename: Ya-Fang
authors.initials: YF
authors.lastname: Wang
authors.forename: Chun-Keung
authors.initials: CK
authors.lastname: Yu
authors.forename: Jen-Ren
authors.initials: JR
authors.lastname: Wang
authors.forename: Chuan-Fa
authors.initials: CF
authors.lastname: Chang
mesh_terms: D000998:Antiviral Agents / Q000378:metabolism; D045744:Cell Line, Tumor; D029821:Enterovirus A, Human / Q000502:physiology*; D006031:Glycosylation; D006801:Humans; D037102:Lectins / Q000378:metabolism; D051907:Lysosomal Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D009439:Neuraminidase / Q000378:metabolism; D051116:Receptors, Scavenger / Q000737:chemistry / Q000378:metabolism; D011991:Receptors, Virus / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism*; D053585:Virus Attachment
chemical_list: D000998:Antiviral Agents; D037102:Lectins; D051907:Lysosomal Membrane Proteins; D051116:Receptors, Scavenger; D011991:Receptors, Virus; C074299:SCARB2 protein, human; D012794:Sialic Acids; D009439:Neuraminidase