The cellular receptor for enterovirus 71

Yue Liu, Michael G. Rossmann

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Protein Cell ›› 2014, Vol. 5 ›› Issue (9) : 655-657. DOI: 10.1007/s13238-014-0092-6
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The cellular receptor for enterovirus 71

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Yue Liu, Michael G. Rossmann. The cellular receptor for enterovirus 71. Protein Cell, 2014, 5(9): 655‒657 https://doi.org/10.1007/s13238-014-0092-6

References

[1]
Bubeck D, Filman DJ, Cheng N, Steven AC, Hogle JM, Belnap DM (2005a) The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J Virol79: 7745-7755
[2]
Bubeck D, Filman DJ, Hogle JM (2005b) Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex. Nat Struct Mol Biol12: 615-618
[3]
Chen P, Song Z, Qi Y, Feng X, Xu N, Sun Y, Wu X, Yao X, Mao Q, Li X (2012) Molecular determinants of enterovirus 71 viral entry: cleft around GLN-172 on VP1 protein interacts with variable region on scavenge receptor B 2. J Biol Chem287: 6406-6420
[4]
Dang M, Wang X, Wang Q, Wang Y, Lin J, Sun Y, Li X, Zhang L, Lou Z, Wang J (2014) Molecular mechanism of SCARB2- mediated attachment and uncoating of EV71. Protein Cell
CrossRef Google scholar
[5]
Hogle JM, Chow M, Filman DJ (1985) Three-dimensional structure of poliovirus at 2.9 Å resolution. Science229: 1358-1365
[6]
Lin YW, Lin HY, Tsou YL, Chitra E, Hsiao KN, Shao HY, Liu CC, Sia C, Chong P, Chow YH (2012) Human SCARB2-mediated entry and endocytosis of EV71. PLoS One7: e30507
[7]
Neculai D, Schwake M, Ravichandran M, Zunke F, Collins RF, Peters J, Neculai M, Plumb J, Loppnau P, Pizarro JC (2013) Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36. Nature504: 172-176
[8]
Nishimura Y, Shimojima M, Tano Y, Miyamura T, Wakita T, Shimizu H (2009) Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71. Nat Med15: 794-797
[9]
Olson NH, Kolatkar PR, Oliveira MA, Cheng RH, Greve JM, McClelland A, Baker TS, Rossmann MG (1993) Structure of a human rhinovirus complexed with its receptor molecule. Proc Natl Acad Sci USA90: 507-511
[10]
Plevka P, Hafenstein S, Harris KG, Cifuente JO, Zhang Y, Bowman VD, Chipman PR, Bator CM, Lin F, Medof ME (2010) Interaction of decay-accelerating factor with echovirus 7. J Virol84: 12665-12674
[11]
Racaniello VR (2007) Picornaviridae: the viruses and their replication. In: Knipe DM, Howley PM(eds) Fields virology. Lippincott Williams & Wilkins, Philadelphia, pp 796-839
[12]
Rossmann MG (1989) The canyon hypothesis. Hiding the host cell receptor attachment site on a viral surface from immune surveillance. J Biol Chem264: 14587-14590
[13]
Rossmann MG (1994) Viral cell recognition and entry. Prot Sci3: 1712-1725
[14]
Rossmann MG, Arnold E, Erickson JW, Frankenberger EA, Grifflth JP, Hecht HJ, Johnson JE, Kamer G, Luo M, Mosser AG (1985) Structure of a human common cold virus and functional relationship to other picornaviruses. Nature317: 145-153
[15]
Rossmann MG, He Y, Kuhn RJ (2002) Picornavirus-receptor interactions. Trends Microbiol10: 324-331
[16]
Shakeel S, Seitsonen JJ, Kajander T, Laurinmaki P, Hyypia T, Susi P, Butcher SJ (2013) Structural and functional analysis of coxsackievirus A9 integrin alphavbeta6 binding and uncoating. J Virol87: 3943-3951
[17]
Smith TJ, Kremer MJ, Luo M, Vriend G, Arnold E, Kamer G, Rossmann MG, McKinlay MA, Diana GD, Otto MJ (1986) The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. Science233: 1286-1293
[18]
Tuthill TJ, Groppelli E, Hogle JM, Rowlands DJ (2010) Picornaviruses. Curr Top Microbiol Immunol343: 43-89
[19]
Xiao C, Bator Kelly CM, Rieder E, Chipman PR, Craig A, Kuhn RJ, Wimmer E, Rossmann MG (2005) The crystal structure of coxsackievirus A21 and its interaction with ICAM-1. Structure13: 1019-1033
[20]
Xiao C, McKinlay MA, Rossmann MG (2011) Design of capsidbinding antiviral agents against human rhinoviruses. In: Agbandje- McKenna M, McKenna R(eds)RSC Biomolecular Sciences Series, No 21, Structural Virology. Royal Society of Chemistry, London, pp 321-339
[21]
Yamayoshi S, Koike S (2011) Identiflcation of a human SCARB2 region that is important for enterovirus 71 binding and infection. J Virol85: 4937-4946
[22]
Yamayoshi S, Yamashita Y, Li J, Hanagata N, Minowa T, Takemura T, Koike S (2009) Scavenger receptor B2 is a cellular receptor for enterovirus 71. Nat Med15: 798-801
[23]
Yamayoshi S, Iizuka S, Yamashita T, Minagawa H, Mizuta K, Okamoto M, Nishimura H, Sanjoh K, Katsushima N, Itagaki T (2012) Human SCARB2-dependent infection by coxsackievirus A7, A14, and A16 and enterovirus 71. J Virol86: 5686-5696
[24]
Yamayoshi S, Ohka S, Fujii K, Koike S (2013) Functional comparison of SCARB2 and PSGL1 as receptors for enterovirus 71. J Virol87: 3335-3347
[25]
Yip CC, Lau SK, Woo PC, Yuen KY (2013) Human enterovirus 71 epidemics: what’s next? Emerg Health Threats J6: 19780
[26]
Zachos C, Blanz J, Saftig P, Schwake M (2012) A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand beta-glucocerebrosidase. Trafflc13: 1113-1123
[27]
Zhang P, Mueller S, Morais MC, Bator CM, Bowman VD, Hafenstein S, Wimmer E, Rossmann MG (2008) Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses. Proc Natl Acad Sci USA105: 18284-18289

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2014 This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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