메뉴 건너뛰기




Volumn 89, Issue 23, 2015, Pages 12084-12095

Single neutralizing monoclonal antibodies targeting the VP1 GH loop of enterovirus 71 inhibit both virus attachment and internalization during viral entry

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY C4; MONOCLONAL ANTIBODY D5; P SELECTIN GLYCOPROTEIN LIGAND 1; PROTEIN VP1; UNCLASSIFIED DRUG; VIRUS RNA; GLYCYL-THREONYL-ALANYL-METHIONYL-ARGINYL-ISOLEUCYL-LEUCYL-GLYCYL-GLYCYL-VALYL-ISOLEUCINE; NEUTRALIZING ANTIBODY; OLIGOPEPTIDE; PRIMER DNA;

EID: 84949685281     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02189-15     Document Type: Article
Times cited : (42)

References (54)
  • 1
  • 3
    • 84874793082 scopus 로고    scopus 로고
    • Progress on the research and development of human enterovirus 71 (EV71) vaccines
    • Liang Z, Mao Q, Gao F, Wang J. 2013. Progress on the research and development of human enterovirus 71 (EV71) vaccines. FrontMed7:111-121.http://dx.doi.org/10.1007/s11684-012-0237-z.
    • (2013) FrontMed , vol.7 , pp. 111-121
    • Liang, Z.1    Mao, Q.2    Gao, F.3    Wang, J.4
  • 6
    • 84889687397 scopus 로고    scopus 로고
    • The enteroviruses: problems in need of treatments
    • Abzug MJ. 2014. The enteroviruses: problems in need of treatments. J Infect 68(Suppl 1):S108-S114. http://dx.doi.org/10.1016/j.jinf.2013.09.020.
    • (2014) J Infect , vol.68 , pp. S108-S114
    • Abzug, M.J.1
  • 8
    • 84861975966 scopus 로고    scopus 로고
    • Crystal structure of human enterovirus 71
    • Plevka P, Perera R, Cardosa J, Kuhn RJ, Rossmann MG. 2012. Crystal structure of human enterovirus 71. Science 336:1274. http://dx.doi.org/10.1126/science.1218713.
    • (2012) Science , vol.336 , pp. 1274
    • Plevka, P.1    Perera, R.2    Cardosa, J.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 9
    • 84881461260 scopus 로고    scopus 로고
    • Picornavirus entry
    • Bergelson JM, Coyne CB. 2013. Picornavirus entry. Adv Exp Med Biol 790:24-41. http://dx.doi.org/10.1007/978-1-4614-7651-1_2.
    • (2013) Adv Exp Med Biol , vol.790 , pp. 24-41
    • Bergelson, J.M.1    Coyne, C.B.2
  • 10
    • 84875993737 scopus 로고    scopus 로고
    • The enterovirus 71 A-particle forms a gateway to allow genome release: a cryoEM study of picornavirus uncoating
    • Shingler KL, Yoder JL, Carnegie MS, Ashley RE, Makhov AM, Conway JF, Hafenstein S. 2013. The enterovirus 71 A-particle forms a gateway to allow genome release: a cryoEM study of picornavirus uncoating. PLoS Pathog 9:e1003240. http://dx.doi.org/10.1371/journal.ppat.1003240.
    • (2013) PLoS Pathog , vol.9
    • Shingler, K.L.1    Yoder, J.L.2    Carnegie, M.S.3    Ashley, R.E.4    Makhov, A.M.5    Conway, J.F.6    Hafenstein, S.7
  • 11
    • 84874324124 scopus 로고    scopus 로고
    • Cellular receptors for human enterovirus species A
    • Nishimura Y, Shimizu H. 2012. Cellular receptors for human enterovirus species A. Front Microbiol 3:105. http://dx.doi.org/10.3389/fmicb.2012.00105.
    • (2012) Front Microbiol , vol.3 , pp. 105
    • Nishimura, Y.1    Shimizu, H.2
  • 12
    • 84902215812 scopus 로고    scopus 로고
    • Demystifying heparan sulfate-protein interactions
    • Xu D, Esko JD. 2014. Demystifying heparan sulfate-protein interactions. Annu Rev Biochem 83:129-157. http://dx.doi.org/10.1146/annurev-biochem-060713-035314.
    • (2014) Annu Rev Biochem , vol.83 , pp. 129-157
    • Xu, D.1    Esko, J.D.2
  • 13
    • 84871962446 scopus 로고    scopus 로고
    • Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor
    • Tan CW, Poh CL, Sam IC, Chan YF. 2013. Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor. J Virol 87:611-620. http://dx.doi.org/10.1128/JVI.02226-12.
    • (2013) J Virol , vol.87 , pp. 611-620
    • Tan, C.W.1    Poh, C.L.2    Sam, I.C.3    Chan, Y.F.4
  • 14
    • 84874742838 scopus 로고    scopus 로고
    • Functional comparison of SCARB2 and PSGL1 as receptors for enterovirus 71
    • Yamayoshi S, Ohka S, Fujii K, Koike S. 2013. Functional comparison of SCARB2 and PSGL1 as receptors for enterovirus 71. J Virol 87:3335-3347. http://dx.doi.org/10.1128/JVI.02070-12.
    • (2013) J Virol , vol.87 , pp. 3335-3347
    • Yamayoshi, S.1    Ohka, S.2    Fujii, K.3    Koike, S.4
  • 16
    • 84863116544 scopus 로고    scopus 로고
    • Molecular determinants of enterovirus 71 viral entry: cleft around GLN-172 on VP1 protein interacts with variable region on scavenge receptor B 2
    • Chen P, Song Z, Qi Y, Feng X, Xu N, Sun Y, Wu X, Yao X, Mao Q, Li X, Dong W, Wan X, Huang N, Shen X, Liang Z, Li W. 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 Chem 287:6406-6420. http://dx.doi.org/10.1074/jbc. M111.301622.
    • (2012) J Biol Chem , vol.287 , pp. 6406-6420
    • Chen, P.1    Song, Z.2    Qi, Y.3    Feng, X.4    Xu, N.5    Sun, Y.6    Wu, X.7    Yao, X.8    Mao, Q.9    Li, X.10    Dong, W.11    Wan, X.12    Huang, N.13    Shen, X.14    Liang, Z.15    Li, W.16
  • 17
    • 0037334339 scopus 로고    scopus 로고
    • At the acidic edge: emerging functions for lysosomal membrane proteins
    • Eskelinen EL, Tanaka Y, Saftig P. 2003. At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol 13:137-145. http://dx.doi.org/10.1016/S0962-8924(03)00005-9.
    • (2003) Trends Cell Biol , vol.13 , pp. 137-145
    • Eskelinen, E.L.1    Tanaka, Y.2    Saftig, P.3
  • 19
    • 84884804710 scopus 로고    scopus 로고
    • Enterovirus 71 binding to PSGL-1 on leukocytes: VP1-145 acts as a molecular switch to control receptor interaction
    • Nishimura Y, Lee H, Hafenstein S, Kataoka C, Wakita T, Bergelson JM, Shimizu H. 2013. Enterovirus 71 binding to PSGL-1 on leukocytes: VP1-145 acts as a molecular switch to control receptor interaction. PLoS Pathog 9:e1003511. http://dx.doi.org/10.1371/journal.ppat.1003511.
    • (2013) PLoS Pathog , vol.9
    • Nishimura, Y.1    Lee, H.2    Hafenstein, S.3    Kataoka, C.4    Wakita, T.5    Bergelson, J.M.6    Shimizu, H.7
  • 20
    • 67650491431 scopus 로고    scopus 로고
    • Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71
    • 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 Med 15:794-797. http://dx.doi.org/10.1038/nm.1961.
    • (2009) Nat Med , vol.15 , pp. 794-797
    • Nishimura, Y.1    Shimojima, M.2    Tano, Y.3    Miyamura, T.4    Wakita, T.5    Shimizu, H.6
  • 21
    • 84890876293 scopus 로고    scopus 로고
    • Chimeric virus-like particle vaccines displaying conserved enterovirus 71 epitopes elicit protective neutralizing antibodies in mice through divergent mechanisms
    • Ye X, Ku Z, Liu Q, Wang X, Shi J, Zhang Y, Kong L, Cong Y, Huang Z. 2014. Chimeric virus-like particle vaccines displaying conserved enterovirus 71 epitopes elicit protective neutralizing antibodies in mice through divergent mechanisms. J Virol 88:72-81. http://dx.doi.org/10.1128/JVI.01848-13.
    • (2014) J Virol , vol.88 , pp. 72-81
    • Ye, X.1    Ku, Z.2    Liu, Q.3    Wang, X.4    Shi, J.5    Zhang, Y.6    Kong, L.7    Cong, Y.8    Huang, Z.9
  • 22
    • 0035852349 scopus 로고    scopus 로고
    • Protection against lethal enterovirus 71 infection in newborn mice by passive immunization with subunit VP1 vaccines and inactivated virus
    • Wu CN, Lin YC, Fann C, Liao NS, Shih SR, Ho MS. 2001. Protection against lethal enterovirus 71 infection in newborn mice by passive immunization with subunit VP1 vaccines and inactivated virus. Vaccine 20:895-904.http://dx.doi.org/10.1016/S0264-410X(01)00385-1.
    • (2001) Vaccine , vol.20 , pp. 895-904
    • Wu, C.N.1    Lin, Y.C.2    Fann, C.3    Liao, N.S.4    Shih, S.R.5    Ho, M.S.6
  • 23
    • 0033773155 scopus 로고    scopus 로고
    • Neutralizing antibody provided protection against enterovirus type 71 lethal challenge in neonatal mice
    • Yu CK, Chen CC, Chen CL, Wang JR, Liu CC, Yan JJ, Su IJ. 2000. Neutralizing antibody provided protection against enterovirus type 71 lethal challenge in neonatal mice. J Biomed Sci 7:523-528. http://dx.doi.org/10.1007/BF02253368.
    • (2000) J Biomed Sci , vol.7 , pp. 523-528
    • Yu, C.K.1    Chen, C.C.2    Chen, C.L.3    Wang, J.R.4    Liu, C.C.5    Yan, J.J.6    Su, I.J.7
  • 24
    • 84875237748 scopus 로고    scopus 로고
    • Monoclonal antibodies for prophylactic and therapeutic use against viral infections
    • Both L, Banyard AC, van Dolleweerd C, Wright E, Ma JK, Fooks AR. 2013. Monoclonal antibodies for prophylactic and therapeutic use against viral infections. Vaccine 31:1553-1559. http://dx.doi.org/10.1016/j.vaccine.2013.01.025.
    • (2013) Vaccine , vol.31 , pp. 1553-1559
    • Both, L.1    Banyard, A.C.2    van Dolleweerd, C.3    Wright, E.4    Ma, J.K.5    Fooks, A.R.6
  • 25
    • 36849087921 scopus 로고    scopus 로고
    • The growth and potential of human antiviral monoclonal antibody therapeutics
    • Marasco WA, Sui J. 2007. The growth and potential of human antiviral monoclonal antibody therapeutics. Nat Biotechnol 25:1421-1434. http://dx.doi.org/10.1038/nbt1363.
    • (2007) Nat Biotechnol , vol.25 , pp. 1421-1434
    • Marasco, W.A.1    Sui, J.2
  • 26
    • 84855963963 scopus 로고    scopus 로고
    • Characterization of an isotype-dependent monoclonal antibody against linear neutralizing epitope effective for prophylaxis of enterovirus 71 infection
    • Lim XF, Jia Q, Khong WX, Yan B, Premanand B, Alonso S, Chow VT, Kwang J. 2012. Characterization of an isotype-dependent monoclonal antibody against linear neutralizing epitope effective for prophylaxis of enterovirus 71 infection. PLoS One 7:e29751. http://dx.doi.org/10.1371/journal.pone.0029751.
    • (2012) PLoS One , vol.7
    • Lim, X.F.1    Jia, Q.2    Khong, W.X.3    Yan, B.4    Premanand, B.5    Alonso, S.6    Chow, V.T.7    Kwang, J.8
  • 27
    • 77952625762 scopus 로고    scopus 로고
    • Monoclonal antibody induced with inactivated EV71-Hn2 virus protects mice against lethal EV71-Hn2 virus infection
    • Chang GH, Luo YJ, Wu XY, Si BY, Lin L, Zhu QY. 2010. Monoclonal antibody induced with inactivated EV71-Hn2 virus protects mice against lethal EV71-Hn2 virus infection. Virol J 7:106. http://dx.doi.org/10.1186/1743-422X-7-106.
    • (2010) Virol J , vol.7 , pp. 106
    • Chang, G.H.1    Luo, Y.J.2    Wu, X.Y.3    Si, B.Y.4    Lin, L.5    Zhu, Q.Y.6
  • 28
    • 84939435860 scopus 로고    scopus 로고
    • In vivo time-related evaluation of a therapeutic neutralization monoclonal antibody against lethal enterovirus 71 infection in a mouse model
    • Li Z, Xu L, He D, Yang L, Liu C, Chen Y, Shih JW, Zhang J, Zhao Q, Cheng T, Xia N. 2014. In vivo time-related evaluation of a therapeutic neutralization monoclonal antibody against lethal enterovirus 71 infection in a mouse model. PLoS One 9:e109391. http://dx.doi.org/10.1371/journal.pone.0109391.
    • (2014) PLoS One , vol.9
    • Li, Z.1    Xu, L.2    He, D.3    Yang, L.4    Liu, C.5    Chen, Y.6    Shih, J.W.7    Zhang, J.8    Zhao, Q.9    Cheng, T.10    Xia, N.11
  • 30
    • 84869081301 scopus 로고    scopus 로고
    • Development of murine monoclonal antibodies with potent neutralization effects on enterovirus 71
    • Ku Z, Shi J, Liu Q, Huang Z. 2012. Development of murine monoclonal antibodies with potent neutralization effects on enterovirus 71. J Virol Methods 186:193-197. http://dx.doi.org/10.1016/j.jviromet.2012.06.025.
    • (2012) J Virol Methods , vol.186 , pp. 193-197
    • Ku, Z.1    Shi, J.2    Liu, Q.3    Huang, Z.4
  • 31
    • 84928582510 scopus 로고    scopus 로고
    • High-yield production of recombinant virus-like particles of enterovirus 71 in Pichia pastoris and their protective efficacy against oral viral challenge in mice
    • Zhang C, Ku Z, Liu Q, Wang X, Chen T, Ye X, Li D, Jin X, Huang Z. 2015. High-yield production of recombinant virus-like particles of enterovirus 71 in Pichia pastoris and their protective efficacy against oral viral challenge in mice. Vaccine 33:2335-2341. http://dx.doi.org/10.1016/j.vaccine.2015.03.034.
    • (2015) Vaccine , vol.33 , pp. 2335-2341
    • Zhang, C.1    Ku, Z.2    Liu, Q.3    Wang, X.4    Chen, T.5    Ye, X.6    Li, D.7    Jin, X.8    Huang, Z.9
  • 32
    • 84874332378 scopus 로고    scopus 로고
    • Neutralizing antibodies induced by recombinant virus-like particles of enterovirus 71 genotype C4 inhibit infection at pre-and postattachment steps
    • Ku Z, Ye X, Huang X, Cai Y, Liu Q, Li Y, Su Z, Huang Z. 2013. Neutralizing antibodies induced by recombinant virus-like particles of enterovirus 71 genotype C4 inhibit infection at pre-and postattachment steps. PLoS One 8:e57601. http://dx.doi.org/10.1371/journal.pone.0057601.
    • (2013) PLoS One , vol.8
    • Ku, Z.1    Ye, X.2    Huang, X.3    Cai, Y.4    Liu, Q.5    Li, Y.6    Su, Z.7    Huang, Z.8
  • 33
    • 26944454471 scopus 로고    scopus 로고
    • Structural basis of West Nile virus neutralization by a therapeutic antibody
    • Nybakken GE, Oliphant T, Johnson S, Burke S, Diamond MS, Fremont DH. 2005. Structural basis of West Nile virus neutralization by a therapeutic antibody. Nature 437:764-769. http://dx.doi.org/10.1038/nature03956.
    • (2005) Nature , vol.437 , pp. 764-769
    • Nybakken, G.E.1    Oliphant, T.2    Johnson, S.3    Burke, S.4    Diamond, M.S.5    Fremont, D.H.6
  • 34
    • 67249101590 scopus 로고    scopus 로고
    • A therapeutic antibody against West Nile virus neutralizes infection by blocking fusion within endosomes
    • Thompson BS, Moesker B, Smit JM, Wilschut J, Diamond MS, Fremont DH. 2009. A therapeutic antibody against West Nile virus neutralizes infection by blocking fusion within endosomes. PLoS Pathog 5:e1000453. http://dx.doi.org/10.1371/journal.ppat.1000453.
    • (2009) PLoS Pathog , vol.5
    • Thompson, B.S.1    Moesker, B.2    Smit, J.M.3    Wilschut, J.4    Diamond, M.S.5    Fremont, D.H.6
  • 37
    • 84874747938 scopus 로고    scopus 로고
    • Unraveling of a neutralization mechanism by two human antibodies against conserved epitopes in the globular head of H5 hemagglutinin
    • Qian M, Hu H, Zuo T, Wang G, Zhang L, Zhou P. 2013. Unraveling of a neutralization mechanism by two human antibodies against conserved epitopes in the globular head of H5 hemagglutinin. J Virol 87:3571-3577. http://dx.doi.org/10.1128/JVI.01292-12.
    • (2013) J Virol , vol.87 , pp. 3571-3577
    • Qian, M.1    Hu, H.2    Zuo, T.3    Wang, G.4    Zhang, L.5    Zhou, P.6
  • 38
    • 0036403802 scopus 로고    scopus 로고
    • Poliovirus cell entry: common structural themes in viral cell entry pathways
    • Hogle JM. 2002. Poliovirus cell entry: common structural themes in viral cell entry pathways. Annu Rev Microbiol 56:677-702. http://dx.doi.org/10.1146/annurev.micro.56.012302.160757.
    • (2002) Annu Rev Microbiol , vol.56 , pp. 677-702
    • Hogle, J.M.1
  • 40
    • 79955938192 scopus 로고    scopus 로고
    • Purification and characterization of enterovirus 71 viral particles produced from Vero cells grown in a serumfree microcarrier bioreactor system
    • Liu CC, Guo MS, Lin FH, Hsiao KN, Chang KH, Chou AH, Wang YC, Chen YC, Yang CS, Chong PC. 2011. Purification and characterization of enterovirus 71 viral particles produced from Vero cells grown in a serumfree microcarrier bioreactor system. PLoS One 6:e20005. http://dx.doi.org/10.1371/journal.pone.0020005.
    • (2011) PLoS One , vol.6
    • Liu, C.C.1    Guo, M.S.2    Lin, F.H.3    Hsiao, K.N.4    Chang, K.H.5    Chou, A.H.6    Wang, Y.C.7    Chen, Y.C.8    Yang, C.S.9    Chong, P.C.10
  • 41
    • 1842612607 scopus 로고    scopus 로고
    • Virus entry: molecular mechanisms and biomedical applications
    • Dimitrov DS. 2004. Virus entry: molecular mechanisms and biomedical applications. Nat Rev Microbiol 2:109-122. http://dx.doi.org/10.1038/nrmicro817.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 109-122
    • Dimitrov, D.S.1
  • 42
    • 0036711665 scopus 로고    scopus 로고
    • Occupancy and mechanism in antibodymediated neutralization of animal viruses
    • Klasse PJ, Sattentau QJ. 2002. Occupancy and mechanism in antibodymediated neutralization of animal viruses. J Gen Virol 83:2091-2108. http://dx.doi.org/10.1099/0022-1317-83-9-2091.
    • (2002) J Gen Virol , vol.83 , pp. 2091-2108
    • Klasse, P.J.1    Sattentau, Q.J.2
  • 43
    • 0034972940 scopus 로고    scopus 로고
    • A model for neutralization of viruses based on antibody coating of the virion surface
    • Burton DR, Saphire EO, Parren PW. 2001. A model for neutralization of viruses based on antibody coating of the virion surface. Curr Top Microbiol Immunol 260:109-143.
    • (2001) Curr Top Microbiol Immunol , vol.260 , pp. 109-143
    • Burton, D.R.1    Saphire, E.O.2    Parren, P.W.3
  • 44
    • 34249030028 scopus 로고    scopus 로고
    • Neutralization of animal virus infectivity by antibody
    • Reading SA, Dimmock NJ. 2007. Neutralization of animal virus infectivity by antibody. Arch Virol 152:1047-1059. http://dx.doi.org/10.1007/s00705-006-0923-8.
    • (2007) Arch Virol , vol.152 , pp. 1047-1059
    • Reading, S.A.1    Dimmock, N.J.2
  • 45
    • 0025295299 scopus 로고
    • Antibodies that block rhinovirus attachment map to domain 1 of the major group receptor
    • Lineberger DW, Graham DJ, Tomassini JE, Colonno RJ. 1990. Antibodies that block rhinovirus attachment map to domain 1 of the major group receptor. J Virol 64:2582-2587.
    • (1990) J Virol , vol.64 , pp. 2582-2587
    • Lineberger, D.W.1    Graham, D.J.2    Tomassini, J.E.3    Colonno, R.J.4
  • 47
    • 0028341259 scopus 로고
    • Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature
    • Li Q, Yafal AG, Lee YM, Hogle J, Chow M. 1994. Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature. J Virol 68:3965-3970.
    • (1994) J Virol , vol.68 , pp. 3965-3970
    • Li, Q.1    Yafal, A.G.2    Lee, Y.M.3    Hogle, J.4    Chow, M.5
  • 48
    • 0035159863 scopus 로고    scopus 로고
    • The N-terminal region of the VP1 protein of swine vesicular disease virus contains a neutralization site that arises upon cell attachment and is involved in viral entry
    • Jimenez-Clavero MA, Escribano-Romero E, Douglas AJ, Ley V. 2001. The N-terminal region of the VP1 protein of swine vesicular disease virus contains a neutralization site that arises upon cell attachment and is involved in viral entry. J Virol 75:1044-1047. http://dx.doi.org/10.1128/JVI.75.2.1044-1047.2001.
    • (2001) J Virol , vol.75 , pp. 1044-1047
    • Jimenez-Clavero, M.A.1    Escribano-Romero, E.2    Douglas, A.J.3    Ley, V.4
  • 49
    • 84872179443 scopus 로고    scopus 로고
    • Characterization of a novel monoclonal antibody reactive against the N-terminal region of enterovirus 71 VP1 capsid protein
    • Lim XF, Jia Q, Chow VT, Kwang J. 2013. Characterization of a novel monoclonal antibody reactive against the N-terminal region of enterovirus 71 VP1 capsid protein. J Virol Methods 188:76-82. http://dx.doi.org/10.1016/j.jviromet.2012.11.038.
    • (2013) J Virol Methods , vol.188 , pp. 76-82
    • Lim, X.F.1    Jia, Q.2    Chow, V.T.3    Kwang, J.4
  • 50
    • 78650957391 scopus 로고    scopus 로고
    • The essential role of clathrin-mediated endocytosis in the infectious entry of human enterovirus 71
    • Hussain KM, Leong KL, Ng MM, Chu JJ. 2011. The essential role of clathrin-mediated endocytosis in the infectious entry of human enterovirus 71. J Biol Chem 286:309-321. http://dx.doi.org/10.1074/jbc. M110.168468.
    • (2011) J Biol Chem , vol.286 , pp. 309-321
    • Hussain, K.M.1    Leong, K.L.2    Ng, M.M.3    Chu, J.J.4
  • 51
    • 84869022974 scopus 로고    scopus 로고
    • Symmetry-related clustering of positive charges is a common mechanism for heparan sulfate binding in enteroviruses
    • McLeish NJ, Williams CH, Kaloudas D, Roivainen MM, Stanway G. 2012. Symmetry-related clustering of positive charges is a common mechanism for heparan sulfate binding in enteroviruses. J Virol 86:11163-11170.http://dx.doi.org/10.1128/JVI.00640-12.
    • (2012) J Virol , vol.86 , pp. 11163-11170
    • McLeish, N.J.1    Williams, C.H.2    Kaloudas, D.3    Roivainen, M.M.4    Stanway, G.5
  • 52
    • 18144403168 scopus 로고    scopus 로고
    • Human rhinovirus type 89 variants use heparan sulfate proteoglycan for cell attachment
    • Vlasak M, Goesler I, Blaas D. 2005. Human rhinovirus type 89 variants use heparan sulfate proteoglycan for cell attachment. J Virol 79:5963-5970.http://dx.doi.org/10.1128/JVI.79.10.5963-5970.2005.
    • (2005) J Virol , vol.79 , pp. 5963-5970
    • Vlasak, M.1    Goesler, I.2    Blaas, D.3
  • 53
    • 0141681882 scopus 로고    scopus 로고
    • Heparan sulfates and coxsackievirus-adenovirus receptor: each one mediates coxsackievirus B3 PD infection
    • Zautner AE, Korner U, Henke A, BadorffC, Schmidtke M. 2003. Heparan sulfates and coxsackievirus-adenovirus receptor: each one mediates coxsackievirus B3 PD infection. J Virol 77:10071-10077. http://dx.doi.org/10.1128/JVI.77.18.10071-10077.2003.
    • (2003) J Virol , vol.77 , pp. 10071-10077
    • Zautner, A.E.1    Korner, U.2    Henke, A.3    Badorff, C.4    Schmidtke, M.5
  • 54
    • 79251515779 scopus 로고    scopus 로고
    • Adaptive mutations in the genomes of enterovirus 71 strains following infection of mouse cells expressing human P-selectin glycoprotein ligand-1
    • Miyamura K, Nishimura Y, Abo M, Wakita T, Shimizu H. 2011. Adaptive mutations in the genomes of enterovirus 71 strains following infection of mouse cells expressing human P-selectin glycoprotein ligand-1. J Gen Virol 92:287-291. http://dx.doi.org/10.1099/vir.0.022418-0.3
    • (2011) J Gen Virol , vol.92 , pp. 287-291
    • Miyamura, K.1    Nishimura, Y.2    Abo, M.3    Wakita, T.4    Shimizu, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.