Cell surface nucleolin facilitates enterovirus 71 binding and infection

Pei Yi Su, Ya Fang Wang, Sheng Wen Huang, Yu Chih Lo, Ya Hui Wang, Shang Rung Wu, Dar Bin Shieh, Shun Hua Chen, Jen Ren Wang, Ming Der Lai, Chuan Fa Chang

研究成果: Article同行評審

66 引文 斯高帕斯(Scopus)


Because the pathogenesis of enterovirus 71 (EV71) remains mostly ambiguous, identifying the factors that mediate viral binding and entry to host cells is indispensable to ultimately uncover the mechanisms that underlie virus infection and pathogenesis. Despite the identification of several receptors/attachment molecules for EV71, the binding, entry, and infection mechanisms of EV71 remain unclear. Herein, we employed glycoproteomic approaches to identify human nucleolin as a novel binding receptor for EV71. Glycoproteins purified by lectin chromatography from the membrane extraction of human cells were treated with sialidase, followed by immunoprecipitation with EV71 particles. Among the 16 proteins identified by tandem mass spectrometry analysis, cell surface nucleolin attracted our attention. We found that EV71 interacted directly with nucleolin via the VP1 capsid protein and that an antinucleolin antibody reduced the binding of EV71 to human cells. In addition, the knockdown of cell surface nucleolin decreased EV71 binding, infection, and production in human cells. Furthermore, the expression of human nucleolin on the cell surface of a mouse cell line increased EV71 binding and conferred EV71 infection and production in the cells. These results strongly indicate that human nucleolin can mediate EV71 binding to and infection of cells. Our findings also demonstrate that the use of glycoproteomic approaches is a reliable methodology to discover novel receptors for pathogens.

頁(從 - 到)4527-4538
期刊Journal of Virology
出版狀態Published - 2015

All Science Journal Classification (ASJC) codes

  • 微生物學
  • 免疫學
  • 昆蟲科學
  • 病毒學


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