Abstract
Enterovirus A71 (EV-A71) infection has grown to become a serious threat to global public health. It is one of the major causes of hand, foot, and mouth disease (HFMD) in infants and young children. EV-A71 can also infect the central nervous system (CNS) and induce diverse neurological complications, such as brainstem encephalitis, aseptic meningitis, and acute flaccid paralysis, or even death. Viral proteins play a crucial role in EV-A71 infection. Many recent studies have discussed the structure and function of EV-A71 proteins, and the findings reported will definitely aid the development of vaccines and therapeutic approaches. This article reviews the progress in the research on the structure and function of EV-A71 proteins. Available literature can provide a basis for studying the pathogenesis of EV-A71 infection in detail.
Highlights
Enterovirus A71 (EV-A71) is one of the major etiological agents causing hand, foot, and mouth disease (HFMD), which generally affects children aged five and below
After binding to the viral receptors and entering the host cell via receptormediated endocytosis, the EV-A71 genome is translated in a cap-independent manner into a large polyprotein (Thompson and Sarnow, 2003), which is subsequently processed by the viral proteases 2A proteinase (2Apro) and 3C protease (3Cpro) to form the structural capsid proteins (VP1–VP4) and the non-structural proteins (2A−2C, 3A−3D)
Ma et al recently confirmed that the polymorphisms of EVA71 3Cpro at the 79th amino acid position were associated with clinical severity and viral replication, which might be related to the interaction of 3Cpro with important host proteins such as tripartite motif-containing protein 21 (TRIM21) (Ma et al, 2017)
Summary
EV-A71 is one of the major etiological agents causing hand, foot, and mouth disease (HFMD), which generally affects children aged five and below. After binding to the viral receptors and entering the host cell via receptormediated endocytosis, the EV-A71 genome is translated in a cap-independent manner into a large polyprotein (Thompson and Sarnow, 2003), which is subsequently processed by the viral proteases 2Apro and 3Cpro to form the structural capsid proteins (VP1–VP4) and the non-structural proteins (2A−2C, 3A−3D).
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