The molecular basis of PSGL-1-dependent viral replication and pathogenesis in enterovirus 71 infection

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Enterovirus 71 (EV71) is a major causative agent of hand, foot, and mouth disease, and causes various neurological diseases, including fatal encephalitis. In this study, we investigated the molecular basis of the interaction between EV71 and PSGL-1, a functional cellular receptor for EV71. We demonstrated that tyrosine sulfation at the N-terminal region of PSGL-1 plays a critical role in the PSGL-1-binding to EV71. An amino acid residue of the capsid protein VP1 of EV71 (VP1-145) controls virus tropism by changing the accessibility of VP1-244 to the sulfated N-terminus of PSGL-1, thus suggesting the involvement of VP1-145 in a PSGL-1-dependent viral replication and pathogenesis in EV71 infection.