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The Enterovirus A71 (EV-A71) capsid protein VP1 GH loop epitope is a critical antigenic region located on the surface of the EV-A71 virus (Lyu et al., 2015, DOI: 10.1128/JVI.01926-14). EV-A71 is a primary causative agent of hand, foot, and mouth disease (HFMD), which can progress to severe neurological complications such as encephalitis and pulmonary edema, particularly in young children (Puenpa et al., 2019, DOI: 10.3390/v11040347). The VP1 protein is the most exposed of the four capsid proteins (VP1-VP4) and plays a pivotal role in viral attachment to host cell receptors, including SCARB2 and PSGL-1 (Yamayoshi et al., 2009, DOI: 10.1038/nm.1992). The GH loop, spanning approximately residues 208 to 222 of the VP1 protein, is a highly conserved and immunodominant neutralization epitope (Kiener et al., 2014, DOI: 10.1371/journal.pone.0094579). Therapeutic strategies targeting this epitope primarily involve the development of inactivated vaccines and neutralizing monoclonal antibodies (Zhu et al., 2014, DOI: 10.1016/S0140-6736(13)62305-4). These agents work by binding to the GH loop, thereby blocking the virus's ability to dock with host receptors or preventing the structural transitions necessary for viral uncoating and genome release (Lyu et al., 2015). Consequently, the VP1 GH loop is a focal point for both diagnostic assays and the development of preventative and therapeutic interventions against EV-A71 infection.
Neutralizing antibodies bind to the GH loop to sterically hinder viral attachment to host receptors or interfere with the conformational changes required for viral uncoating.
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