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Volumn 9, Issue 10, 2015, Pages

Loss of Glycosaminoglycan Receptor Binding after Mosquito Cell Passage Reduces Chikungunya Virus Infectivity

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; GLYCOSAMINOGLYCAN RECEPTOR; HEPARIN; TUNICAMYCIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RECEPTOR; VIRUS RNA;

EID: 84959212852     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0004139     Document Type: Article
Times cited : (28)

References (96)
  • 1
    • 84866911884 scopus 로고    scopus 로고
    • Simple clinical and laboratory predictors of Chikungunya versus dengue infections in adults
    • 23029573, . ().:
    • Lee VJ, Chow A, Zheng X, Carrasco LR, Cook AR, et al. (2012) Simple clinical and laboratory predictors of Chikungunya versus dengue infections in adults. PLoS Negl Trop Dis6: e1786. doi: 10.1371/journal.pntd.000178623029573
    • (2012) PLoS Negl Trop Dis , vol.6 , pp. 1786
    • Lee, V.J.1    Chow, A.2    Zheng, X.3    Carrasco, L.R.4    Cook, A.R.5
  • 2
    • 84875987775 scopus 로고    scopus 로고
    • Chikungunya virus-associated long-term arthralgia: a 36-month prospective longitudinal study
    • 23556021, . ().:
    • Schilte C, Staikowsky F, Couderc T, Madec Y, Carpentier F, et al. (2013) Chikungunya virus-associated long-term arthralgia: a 36-month prospective longitudinal study. PLoS Negl Trop Dis7: e2137. doi: 10.1371/journal.pntd.000213723556021
    • (2013) PLoS Negl Trop Dis , vol.7 , pp. 2137
    • Schilte, C.1    Staikowsky, F.2    Couderc, T.3    Madec, Y.4    Carpentier, F.5
  • 4
    • 69649101103 scopus 로고    scopus 로고
    • Systemic involvements and fatalities during Chikungunya epidemic in India, 2006
    • 19640780, . ().:–
    • Tandale BV, Sathe PS, Arankalle VA, Wadia RS, Kulkarni R, et al. (2009) Systemic involvements and fatalities during Chikungunya epidemic in India, 2006. J Clin Virol46: 145–149. doi: 10.1016/j.jcv.2009.06.02719640780
    • (2009) J Clin Virol , vol.46 , pp. 145-149
    • Tandale, B.V.1    Sathe, P.S.2    Arankalle, V.A.3    Wadia, R.S.4    Kulkarni, R.5
  • 5
    • 84865176501 scopus 로고    scopus 로고
    • Severe forms of chikungunya virus infection in a pediatric intensive care unit on Reunion Island
    • . () [].Spec No:–
    • Pellot AS, Alessandri JL, Robin S, Samperiz S, Attali T, et al. (2012) [Severe forms of chikungunya virus infection in a pediatric intensive care unit on Reunion Island]. Med Trop (Mars)72 Spec No: 88–93.
    • (2012) Med Trop (Mars) , vol.72 , pp. 88-93
    • Pellot, A.S.1    Alessandri, J.L.2    Robin, S.3    Samperiz, S.4    Attali, T.5
  • 6
    • 84884694439 scopus 로고    scopus 로고
    • Chikungunya fever: epidemiology, clinical syndrome, pathogenesis and therapy
    • 23811281, . ().:–
    • Thiberville SD, Moyen N, Dupuis-Maguiraga L, Nougairede A, Gould EA, et al. (2013) Chikungunya fever: epidemiology, clinical syndrome, pathogenesis and therapy. Antiviral Res99: 345–370. doi: 10.1016/j.antiviral.2013.06.00923811281
    • (2013) Antiviral Res , vol.99 , pp. 345-370
    • Thiberville, S.D.1    Moyen, N.2    Dupuis-Maguiraga, L.3    Nougairede, A.4    Gould, E.A.5
  • 7
    • 51349141686 scopus 로고    scopus 로고
    • Estimating Chikungunya prevalence in La Reunion Island outbreak by serosurveys: two methods for two critical times of the epidemic
    • 18662384, . ().:
    • Gerardin P, Guernier V, Perrau J, Fianu A, Le Roux K, et al. (2008) Estimating Chikungunya prevalence in La Reunion Island outbreak by serosurveys: two methods for two critical times of the epidemic. BMC Infect Dis8: 99. doi: 10.1186/1471-2334-8-9918662384
    • (2008) BMC Infect Dis , vol.8 , pp. 99
    • Gerardin, P.1    Guernier, V.2    Perrau, J.3    Fianu, A.4    Le Roux, K.5
  • 8
    • 41349109780 scopus 로고    scopus 로고
    • Increased mortality rate associated with chikungunya epidemic, Ahmedabad, India
    • 18325255, ().:–
    • Mavalankar D, Shastri P, Bandyopadhyay T, Parmar J, Ramani KV, (2008) Increased mortality rate associated with chikungunya epidemic, Ahmedabad, India. Emerg Infect Dis14: 412–415. doi: 10.3201/eid1403.07072018325255
    • (2008) Emerg Infect Dis , vol.14 , pp. 412-415
    • Mavalankar, D.1    Shastri, P.2    Bandyopadhyay, T.3    Parmar, J.4    Ramani, K.V.5
  • 9
    • 84863478516 scopus 로고    scopus 로고
    • Arthritogenic alphaviruses—an overview
    • 22565316, ().:–
    • Suhrbier A, Jaffar-Bandjee MC, Gasque P, (2012) Arthritogenic alphaviruses—an overview. Nat Rev Rheumatol8: 420–429. doi: 10.1038/nrrheum.2012.6422565316
    • (2012) Nat Rev Rheumatol , vol.8 , pp. 420-429
    • Suhrbier, A.1    Jaffar-Bandjee, M.C.2    Gasque, P.3
  • 10
    • 34247262629 scopus 로고    scopus 로고
    • Spread of the tiger: global risk of invasion by the mosquito Aedes albopictus
    • 17417960, ().:–
    • Benedict MQ, Levine RS, Hawley WA, Lounibos LP, (2007) Spread of the tiger: global risk of invasion by the mosquito Aedes albopictus. Vector Borne Zoonotic Dis7: 76–85. 17417960
    • (2007) Vector Borne Zoonotic Dis , vol.7 , pp. 76-85
    • Benedict, M.Q.1    Levine, R.S.2    Hawley, W.A.3    Lounibos, L.P.4
  • 11
    • 84870737712 scopus 로고    scopus 로고
    • Modeling dynamic introduction of Chikungunya virus in the United States
    • 23209859, ().:
    • Ruiz-Moreno D, Vargas IS, Olson KE, Harrington LC, (2012) Modeling dynamic introduction of Chikungunya virus in the United States. PLoS Negl Trop Dis6: e1918. doi: 10.1371/journal.pntd.000191823209859
    • (2012) PLoS Negl Trop Dis , vol.6 , pp. 1918
    • Ruiz-Moreno, D.1    Vargas, I.S.2    Olson, K.E.3    Harrington, L.C.4
  • 13
    • 84935471856 scopus 로고    scopus 로고
    • Towards antivirals against chikungunya virus
    • 26119058, ().:–
    • Abdelnabi R, Neyts J, Delang L, (2015) Towards antivirals against chikungunya virus. Antiviral Res121: 59–68. doi: 10.1016/j.antiviral.2015.06.01726119058
    • (2015) Antiviral Res , vol.121 , pp. 59-68
    • Abdelnabi, R.1    Neyts, J.2    Delang, L.3
  • 14
    • 84932621645 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of chikungunya pathogenesis
    • 26092642, ().:–
    • Lum FM, Ng LF, (2015) Cellular and molecular mechanisms of chikungunya pathogenesis. Antiviral Res120: 165–174. doi: 10.1016/j.antiviral.2015.06.00926092642
    • (2015) Antiviral Res , vol.120 , pp. 165-174
    • Lum, F.M.1    Ng, L.F.2
  • 16
    • 0028088152 scopus 로고
    • The alphaviruses: gene expression, replication, and evolution
    • 7968923, ().:–
    • Strauss JH, Strauss EG, (1994) The alphaviruses: gene expression, replication, and evolution. Microbiol Rev58: 491–562. 7968923
    • (1994) Microbiol Rev , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 17
    • 0032924195 scopus 로고    scopus 로고
    • Genetic and fitness changes accompanying adaptation of an arbovirus to vertebrate and invertebrate cells
    • 10196330, ().:–
    • Weaver SC, Brault AC, Kang W, Holland JJ, (1999) Genetic and fitness changes accompanying adaptation of an arbovirus to vertebrate and invertebrate cells. J Virol73: 4316–4326. 10196330
    • (1999) J Virol , vol.73 , pp. 4316-4326
    • Weaver, S.C.1    Brault, A.C.2    Kang, W.3    Holland, J.J.4
  • 18
    • 37849052513 scopus 로고    scopus 로고
    • A single mutation in chikungunya virus affects vector specificity and epidemic potential
    • 18069894, ().:
    • Tsetsarkin KA, Vanlandingham DL, McGee CE, Higgs S, (2007) A single mutation in chikungunya virus affects vector specificity and epidemic potential. PLoS Pathog3: e201. 18069894
    • (2007) PLoS Pathog , vol.3 , pp. 201
    • Tsetsarkin, K.A.1    Vanlandingham, D.L.2    McGee, C.E.3    Higgs, S.4
  • 19
    • 33847199327 scopus 로고    scopus 로고
    • The Old World and New World alphaviruses use different virus-specific proteins for induction of transcriptional shutoff
    • 17108023, . ().:–
    • Garmashova N, Gorchakov R, Volkova E, Paessler S, Frolova E, et al. (2007) The Old World and New World alphaviruses use different virus-specific proteins for induction of transcriptional shutoff. J Virol81: 2472–2484. 17108023
    • (2007) J Virol , vol.81 , pp. 2472-2484
    • Garmashova, N.1    Gorchakov, R.2    Volkova, E.3    Paessler, S.4    Frolova, E.5
  • 20
    • 22544443363 scopus 로고    scopus 로고
    • Inhibition of transcription and translation in Sindbis virus-infected cells
    • 16014903, ().:–
    • Gorchakov R, Frolova E, Frolov I, (2005) Inhibition of transcription and translation in Sindbis virus-infected cells. J Virol79: 9397–9409. 16014903
    • (2005) J Virol , vol.79 , pp. 9397-9409
    • Gorchakov, R.1    Frolova, E.2    Frolov, I.3
  • 21
    • 84870310514 scopus 로고    scopus 로고
    • Chikungunya virus induces a more moderate cytopathic effect in mosquito cells than in mammalian cells
    • 22907160, . ().:–
    • Li YG, Siripanyaphinyo U, Tumkosit U, Noranate N, An A, et al. (2013) Chikungunya virus induces a more moderate cytopathic effect in mosquito cells than in mammalian cells. Intervirology56: 6–12. doi: 10.1159/00033998522907160
    • (2013) Intervirology , vol.56 , pp. 6-12
    • Li, Y.G.1    Siripanyaphinyo, U.2    Tumkosit, U.3    Noranate, N.4    An, A.5
  • 22
    • 0013951807 scopus 로고
    • Cytopathic effect of Semliki Forest virus in the mosquito Aedes aegypti
    • 5917634, ().:–
    • Mims CA, Day MF, Marshall ID, (1966) Cytopathic effect of Semliki Forest virus in the mosquito Aedes aegypti. Am J Trop Med Hyg15: 775–784. 5917634
    • (1966) Am J Trop Med Hyg , vol.15 , pp. 775-784
    • Mims, C.A.1    Day, M.F.2    Marshall, I.D.3
  • 23
    • 0015750989 scopus 로고
    • The growth of Semliki Forest virus in cultured mosquito cells: ultrastructural observations
    • 4793529, ().:–
    • Raghow RS, Davey MW, Dalgarno L, (1973) The growth of Semliki Forest virus in cultured mosquito cells: ultrastructural observations. Arch Gesamte Virusforsch43: 165–168. 4793529
    • (1973) Arch Gesamte Virusforsch , vol.43 , pp. 165-168
    • Raghow, R.S.1    Davey, M.W.2    Dalgarno, L.3
  • 24
    • 0015902862 scopus 로고
    • Ross River virus replication in cultured mosquito and mammalian cells: virus growth and correlated ultrastructural changes
    • 4357368, ().:–
    • Raghow RS, Grace TD, Filshie BK, Bartley W, Dalgarno L, (1973) Ross River virus replication in cultured mosquito and mammalian cells: virus growth and correlated ultrastructural changes. J Gen Virol21: 109–122. 4357368
    • (1973) J Gen Virol , vol.21 , pp. 109-122
    • Raghow, R.S.1    Grace, T.D.2    Filshie, B.K.3    Bartley, W.4    Dalgarno, L.5
  • 25
    • 0030051091 scopus 로고    scopus 로고
    • Differential processing of sindbis virus glycoprotein PE2 in cultured vertebrate and arthropod cells
    • 8627739, ().:–
    • Heidner HW, Knott TA, Johnston RE, (1996) Differential processing of sindbis virus glycoprotein PE2 in cultured vertebrate and arthropod cells. J Virol70: 2069–2073. 8627739
    • (1996) J Virol , vol.70 , pp. 2069-2073
    • Heidner, H.W.1    Knott, T.A.2    Johnston, R.E.3
  • 26
    • 0017356042 scopus 로고
    • Tunicamycin inhibits glycosylation and multiplication of Sindbis and vesicular stomatitis viruses
    • 189071, ().:–
    • Leavitt R, Schlesinger S, Kornfeld S, (1977) Tunicamycin inhibits glycosylation and multiplication of Sindbis and vesicular stomatitis viruses. J Virol21: 375–385. 189071
    • (1977) J Virol , vol.21 , pp. 375-385
    • Leavitt, R.1    Schlesinger, S.2    Kornfeld, S.3
  • 27
    • 34250854515 scopus 로고    scopus 로고
    • Essential role of dengue virus envelope protein N glycosylation at asparagine-67 during viral propagation
    • 17459925, ().:–
    • Mondotte JA, Lozach PY, Amara A, Gamarnik AV, (2007) Essential role of dengue virus envelope protein N glycosylation at asparagine-67 during viral propagation. J Virol81: 7136–7148. 17459925
    • (2007) J Virol , vol.81 , pp. 7136-7148
    • Mondotte, J.A.1    Lozach, P.Y.2    Amara, A.3    Gamarnik, A.V.4
  • 28
    • 66149114468 scopus 로고    scopus 로고
    • Role of N-linked glycosylation for sindbis virus infection and replication in vertebrate and invertebrate systems
    • 19297464, ().:–
    • Knight RL, Schultz KL, Kent RJ, Venkatesan M, Griffin DE, (2009) Role of N-linked glycosylation for sindbis virus infection and replication in vertebrate and invertebrate systems. J Virol83: 5640–5647. doi: 10.1128/JVI.02427-0819297464
    • (2009) J Virol , vol.83 , pp. 5640-5647
    • Knight, R.L.1    Schultz, K.L.2    Kent, R.J.3    Venkatesan, M.4    Griffin, D.E.5
  • 29
    • 34247530859 scopus 로고    scopus 로고
    • Virus glycosylation: role in virulence and immune interactions
    • 17398101, ().:–
    • Vigerust DJ, Shepherd VL, (2007) Virus glycosylation: role in virulence and immune interactions. Trends Microbiol15: 211–218. 17398101
    • (2007) Trends Microbiol , vol.15 , pp. 211-218
    • Vigerust, D.J.1    Shepherd, V.L.2
  • 30
    • 63549121737 scopus 로고    scopus 로고
    • West Nile virus envelope protein glycosylation is required for efficient viral transmission by Culex vectors
    • 19249803, ().:–
    • Moudy RM, Zhang B, Shi PY, Kramer LD, (2009) West Nile virus envelope protein glycosylation is required for efficient viral transmission by Culex vectors. Virology387: 222–228. doi: 10.1016/j.virol.2009.01.03819249803
    • (2009) Virology , vol.387 , pp. 222-228
    • Moudy, R.M.1    Zhang, B.2    Shi, P.Y.3    Kramer, L.D.4
  • 31
    • 0242363253 scopus 로고    scopus 로고
    • DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses
    • 14581539, ().:–
    • Klimstra WB, Nangle EM, Smith MS, Yurochko AD, Ryman KD, (2003) DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses. J Virol77: 12022–12032. 14581539
    • (2003) J Virol , vol.77 , pp. 12022-12032
    • Klimstra, W.B.1    Nangle, E.M.2    Smith, M.S.3    Yurochko, A.D.4    Ryman, K.D.5
  • 32
    • 31144445030 scopus 로고    scopus 로고
    • West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection
    • 16415006, . ().:–
    • Davis CW, Nguyen HY, Hanna SL, Sanchez MD, Doms RW, et al. (2006) West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection. J Virol80: 1290–1301. 16415006
    • (2006) J Virol , vol.80 , pp. 1290-1301
    • Davis, C.W.1    Nguyen, H.Y.2    Hanna, S.L.3    Sanchez, M.D.4    Doms, R.W.5
  • 33
    • 84868675349 scopus 로고    scopus 로고
    • Crucial role of the N-glycans on the viral E-envelope glycoprotein in DC-SIGN-mediated dengue virus infection
    • 23124109, ().:–
    • Alen MM, Dallmeier K, Balzarini J, Neyts J, Schols D, (2012) Crucial role of the N-glycans on the viral E-envelope glycoprotein in DC-SIGN-mediated dengue virus infection. Antiviral Res96: 280–287. doi: 10.1016/j.antiviral.2012.10.00723124109
    • (2012) Antiviral Res , vol.96 , pp. 280-287
    • Alen, M.M.1    Dallmeier, K.2    Balzarini, J.3    Neyts, J.4    Schols, D.5
  • 34
    • 33845800843 scopus 로고    scopus 로고
    • Differential induction of type I interferon responses in myeloid dendritic cells by mosquito and mammalian-cell-derived alphaviruses
    • 17079324, . ().:–
    • Shabman RS, Morrison TE, Moore C, White L, Suthar MS, et al. (2007) Differential induction of type I interferon responses in myeloid dendritic cells by mosquito and mammalian-cell-derived alphaviruses. J Virol81: 237–247. 17079324
    • (2007) J Virol , vol.81 , pp. 237-247
    • Shabman, R.S.1    Morrison, T.E.2    Moore, C.3    White, L.4    Suthar, M.S.5
  • 35
    • 37049005384 scopus 로고    scopus 로고
    • Differential activation of human monocyte-derived and plasmacytoid dendritic cells by West Nile virus generated in different host cells
    • 17913823, ().:–
    • Silva MC, Guerrero-Plata A, Gilfoy FD, Garofalo RP, Mason PW, (2007) Differential activation of human monocyte-derived and plasmacytoid dendritic cells by West Nile virus generated in different host cells. J Virol81: 13640–13648. 17913823
    • (2007) J Virol , vol.81 , pp. 13640-13648
    • Silva, M.C.1    Guerrero-Plata, A.2    Gilfoy, F.D.3    Garofalo, R.P.4    Mason, P.W.5
  • 36
    • 0036139068 scopus 로고    scopus 로고
    • Cell surface heparan sulfate and its roles in assisting viral infections
    • 11746174, ().:–
    • Liu J, Thorp SC, (2002) Cell surface heparan sulfate and its roles in assisting viral infections. Med Res Rev22: 1–25. 11746174
    • (2002) Med Res Rev , vol.22 , pp. 1-25
    • Liu, J.1    Thorp, S.C.2
  • 37
    • 20344381822 scopus 로고    scopus 로고
    • Glycoconjugate glycans as viral receptors
    • 16019714, ().:–
    • Olofsson S, Bergstrom T, (2005) Glycoconjugate glycans as viral receptors. Ann Med37: 154–172. 16019714
    • (2005) Ann Med , vol.37 , pp. 154-172
    • Olofsson, S.1    Bergstrom, T.2
  • 38
    • 84895727739 scopus 로고    scopus 로고
    • Deliberate attenuation of chikungunya virus by adaptation to heparan sulfate-dependent infectivity: a model for rational arboviral vaccine design
    • 24587470, . ().:
    • Gardner CL, Hritz J, Sun C, Vanlandingham DL, Song TY, et al. (2014) Deliberate attenuation of chikungunya virus by adaptation to heparan sulfate-dependent infectivity: a model for rational arboviral vaccine design. PLoS Negl Trop Dis8: e2719. doi: 10.1371/journal.pntd.000271924587470
    • (2014) PLoS Negl Trop Dis , vol.8 , pp. 2719
    • Gardner, C.L.1    Hritz, J.2    Sun, C.3    Vanlandingham, D.L.4    Song, T.Y.5
  • 39
    • 0034633834 scopus 로고    scopus 로고
    • Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice
    • 11021998, ().:–
    • Bernard KA, Klimstra WB, Johnston RE, (2000) Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice. Virology276: 93–103. 11021998
    • (2000) Virology , vol.276 , pp. 93-103
    • Bernard, K.A.1    Klimstra, W.B.2    Johnston, R.E.3
  • 40
    • 84894187925 scopus 로고    scopus 로고
    • A single-amino-acid polymorphism in Chikungunya virus E2 glycoprotein influences glycosaminoglycan utilization
    • 24371059, . ().:–
    • Silva LA, Khomandiak S, Ashbrook AW, Weller R, Heise MT, et al. (2014) A single-amino-acid polymorphism in Chikungunya virus E2 glycoprotein influences glycosaminoglycan utilization. J Virol88: 2385–2397. doi: 10.1128/JVI.03116-1324371059
    • (2014) J Virol , vol.88 , pp. 2385-2397
    • Silva, L.A.1    Khomandiak, S.2    Ashbrook, A.W.3    Weller, R.4    Heise, M.T.5
  • 41
    • 80053154735 scopus 로고    scopus 로고
    • Heparan sulfate binding by natural eastern equine encephalitis viruses promotes neurovirulence
    • 21896745, ().:–
    • Gardner CL, Ebel GD, Ryman KD, Klimstra WB, (2011) Heparan sulfate binding by natural eastern equine encephalitis viruses promotes neurovirulence. Proc Natl Acad Sci U S A108: 16026–16031. doi: 10.1073/pnas.111061710821896745
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 16026-16031
    • Gardner, C.L.1    Ebel, G.D.2    Ryman, K.D.3    Klimstra, W.B.4
  • 42
    • 33947365512 scopus 로고    scopus 로고
    • Heparan sulfate binding can contribute to the neurovirulence of neuroadapted and nonneuroadapted Sindbis viruses
    • 17215278, . ().:–
    • Ryman KD, Gardner CL, Burke CW, Meier KC, Thompson JM, et al. (2007) Heparan sulfate binding can contribute to the neurovirulence of neuroadapted and nonneuroadapted Sindbis viruses. J Virol81: 3563–3573. 17215278
    • (2007) J Virol , vol.81 , pp. 3563-3573
    • Ryman, K.D.1    Gardner, C.L.2    Burke, C.W.3    Meier, K.C.4    Thompson, J.M.5
  • 43
    • 0020607967 scopus 로고
    • Host-dependent variation of asparagine-linked oligosaccharides at individual glycosylation sites of Sindbis virus glycoproteins
    • 6822574, ().:–
    • Hsieh P, Rosner MR, Robbins PW, (1983) Host-dependent variation of asparagine-linked oligosaccharides at individual glycosylation sites of Sindbis virus glycoproteins. J Biol Chem258: 2548–2554. 6822574
    • (1983) J Biol Chem , vol.258 , pp. 2548-2554
    • Hsieh, P.1    Rosner, M.R.2    Robbins, P.W.3
  • 44
    • 84878386885 scopus 로고    scopus 로고
    • Mouse embryonic stem cells are deficient in type I interferon expression in response to viral infections and double-stranded RNA
    • 23580653, . ().:–
    • Wang R, Wang J, Paul AM, Acharya D, Bai F, et al. (2013) Mouse embryonic stem cells are deficient in type I interferon expression in response to viral infections and double-stranded RNA. J Biol Chem288: 15926–15936. doi: 10.1074/jbc.M112.42143823580653
    • (2013) J Biol Chem , vol.288 , pp. 15926-15936
    • Wang, R.1    Wang, J.2    Paul, A.M.3    Acharya, D.4    Bai, F.5
  • 45
    • 15544387798 scopus 로고    scopus 로고
    • Use of RNA interference to prevent lethal murine west nile virus infection
    • 15747251, . ().:–
    • Bai F, Wang T, Pal U, Bao F, Gould LH, et al. (2005) Use of RNA interference to prevent lethal murine west nile virus infection. J Infect Dis191: 1148–1154. 15747251
    • (2005) J Infect Dis , vol.191 , pp. 1148-1154
    • Bai, F.1    Wang, T.2    Pal, U.3    Bao, F.4    Gould, L.H.5
  • 46
    • 34047123776 scopus 로고    scopus 로고
    • The differential expression of corticosteroid receptor isoforms in corticosteroid-resistant and -sensitive patients with rheumatoid arthritis
    • ().:–
    • Kozaci DL, Chernajovsky Y, Chikanza IC, (2007) The differential expression of corticosteroid receptor isoforms in corticosteroid-resistant and -sensitive patients with rheumatoid arthritis. Rheumatology (Oxford)46: 579–585.
    • (2007) Rheumatology (Oxford) , vol.46 , pp. 579-585
    • Kozaci, D.L.1    Chernajovsky, Y.2    Chikanza, I.C.3
  • 47
    • 84904437500 scopus 로고    scopus 로고
    • Delivery of antiviral small interfering RNA with gold nanoparticles inhibits dengue virus infection in vitro
    • 24828333, . ().:–
    • Paul AM, Shi Y, Acharya D, Douglas JR, Cooley A, et al. (2014) Delivery of antiviral small interfering RNA with gold nanoparticles inhibits dengue virus infection in vitro. J Gen Virol95: 1712–1722. doi: 10.1099/vir.0.066084-024828333
    • (2014) J Gen Virol , vol.95 , pp. 1712-1722
    • Paul, A.M.1    Shi, Y.2    Acharya, D.3    Douglas, J.R.4    Cooley, A.5
  • 48
    • 77955008245 scopus 로고    scopus 로고
    • Chikungunya virus arthritis in adult wild-type mice
    • 20519386, . ().:–
    • Gardner J, Anraku I, Le TT, Larcher T, Major L, et al. (2010) Chikungunya virus arthritis in adult wild-type mice. J Virol84: 8021–8032. doi: 10.1128/JVI.02603-0920519386
    • (2010) J Virol , vol.84 , pp. 8021-8032
    • Gardner, J.1    Anraku, I.2    Le, T.T.3    Larcher, T.4    Major, L.5
  • 49
    • 84871827425 scopus 로고    scopus 로고
    • A pathogenic role for CD4+ T cells during Chikungunya virus infection in mice
    • 23209328, . ().:–
    • Teo TH, Lum FM, Claser C, Lulla V, Lulla A, et al. (2013) A pathogenic role for CD4+ T cells during Chikungunya virus infection in mice. J Immunol190: 259–269. doi: 10.4049/jimmunol.120217723209328
    • (2013) J Immunol , vol.190 , pp. 259-269
    • Teo, T.H.1    Lum, F.M.2    Claser, C.3    Lulla, V.4    Lulla, A.5
  • 50
    • 84870518676 scopus 로고    scopus 로고
    • Viperin restricts chikungunya virus replication and pathology
    • 23160199, . ().:–
    • Teng TS, Foo SS, Simamarta D, Lum FM, Teo TH, et al. (2012) Viperin restricts chikungunya virus replication and pathology. J Clin Invest122: 4447–4460. doi: 10.1172/JCI6312023160199
    • (2012) J Clin Invest , vol.122 , pp. 4447-4460
    • Teng, T.S.1    Foo, S.S.2    Simamarta, D.3    Lum, F.M.4    Teo, T.H.5
  • 51
    • 0020307672 scopus 로고
    • Monensin inhibits Semliki Forest virus penetration into culture cells
    • 6957864, ().:–
    • Marsh M, Wellsteed J, Kern H, Harms E, Helenius A, (1982) Monensin inhibits Semliki Forest virus penetration into culture cells. Proc Natl Acad Sci U S A79: 5297–5301. 6957864
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 5297-5301
    • Marsh, M.1    Wellsteed, J.2    Kern, H.3    Harms, E.4    Helenius, A.5
  • 52
    • 0020042010 scopus 로고
    • Inhibition of Semliki forest virus penetration by lysosomotropic weak bases
    • ().:–
    • Helenius A, Marsh M, White J, (1982) Inhibition of Semliki forest virus penetration by lysosomotropic weak bases. J Gen Virol58Pt 1: 47–61.
    • (1982) J Gen Virol , vol.58 , pp. 47-61
    • Helenius, A.1    Marsh, M.2    White, J.3
  • 53
    • 77149120482 scopus 로고    scopus 로고
    • Type I IFN controls chikungunya virus via its action on nonhematopoietic cells
    • 20123960, . ().:–
    • Schilte C, Couderc T, Chretien F, Sourisseau M, Gangneux N, et al. (2010) Type I IFN controls chikungunya virus via its action on nonhematopoietic cells. J Exp Med207: 429–442. doi: 10.1084/jem.2009085120123960
    • (2010) J Exp Med , vol.207 , pp. 429-442
    • Schilte, C.1    Couderc, T.2    Chretien, F.3    Sourisseau, M.4    Gangneux, N.5
  • 55
    • 57349092182 scopus 로고    scopus 로고
    • Ross River virus envelope glycans contribute to type I interferon production in myeloid dendritic cells
    • 18922878, ().:–
    • Shabman RS, Rogers KM, Heise MT, (2008) Ross River virus envelope glycans contribute to type I interferon production in myeloid dendritic cells. J Virol82: 12374–12383. doi: 10.1128/JVI.00985-0818922878
    • (2008) J Virol , vol.82 , pp. 12374-12383
    • Shabman, R.S.1    Rogers, K.M.2    Heise, M.T.3
  • 56
    • 77649188957 scopus 로고    scopus 로고
    • Viral pathogenesis in mice is similar for West Nile virus derived from mosquito and mammalian cells
    • 20167345, ().:–
    • Lim PY, Louie KL, Styer LM, Shi PY, Bernard KA, (2010) Viral pathogenesis in mice is similar for West Nile virus derived from mosquito and mammalian cells. Virology400: 93–103. doi: 10.1016/j.virol.2010.01.02920167345
    • (2010) Virology , vol.400 , pp. 93-103
    • Lim, P.Y.1    Louie, K.L.2    Styer, L.M.3    Shi, P.Y.4    Bernard, K.A.5
  • 57
    • 84857034750 scopus 로고    scopus 로고
    • Interferon-alpha/beta deficiency greatly exacerbates arthritogenic disease in mice infected with wild-type chikungunya virus but not with the cell culture-adapted live-attenuated 181/25 vaccine candidate
    • 22305131, ().:–
    • Gardner CL, Burke CW, Higgs ST, Klimstra WB, Ryman KD, (2012) Interferon-alpha/beta deficiency greatly exacerbates arthritogenic disease in mice infected with wild-type chikungunya virus but not with the cell culture-adapted live-attenuated 181/25 vaccine candidate. Virology425: 103–112. doi: 10.1016/j.virol.2011.12.02022305131
    • (2012) Virology , vol.425 , pp. 103-112
    • Gardner, C.L.1    Burke, C.W.2    Higgs, S.T.3    Klimstra, W.B.4    Ryman, K.D.5
  • 58
    • 0037345386 scopus 로고    scopus 로고
    • A role for glycoprotein C in pseudorabies virus entry that is independent of virus attachment to heparan sulfate and which involves the actin cytoskeleton
    • 12667810, ().:–
    • Rue CA, Ryan P, (2003) A role for glycoprotein C in pseudorabies virus entry that is independent of virus attachment to heparan sulfate and which involves the actin cytoskeleton. Virology307: 12–21. 12667810
    • (2003) Virology , vol.307 , pp. 12-21
    • Rue, C.A.1    Ryan, P.2
  • 59
    • 82455202374 scopus 로고    scopus 로고
    • Replication of alphaviruses: a review on the entry process of alphaviruses into cells
    • 22312336, ().:
    • Leung JY, Ng MM, Chu JJ, (2011) Replication of alphaviruses: a review on the entry process of alphaviruses into cells. Adv Virol2011: 249640. doi: 10.1155/2011/24964022312336
    • (2011) Adv Virol , vol.2011 , pp. 249640
    • Leung, J.Y.1    Ng, M.M.2    Chu, J.J.3
  • 60
    • 78049487538 scopus 로고    scopus 로고
    • Alphavirus Entry and Membrane Fusion
    • 21546978, ().:–
    • Kielian M, Chanel-Vos C, Liao M, (2010) Alphavirus Entry and Membrane Fusion. Viruses2: 796–825. 21546978
    • (2010) Viruses , vol.2 , pp. 796-825
    • Kielian, M.1    Chanel-Vos, C.2    Liao, M.3
  • 61
    • 0031026138 scopus 로고    scopus 로고
    • SFV infection in CHO cells: cell-type specific restrictions to productive virus entry at the cell surface
    • ().():–
    • Marsh M, Bron R, (1997) SFV infection in CHO cells: cell-type specific restrictions to productive virus entry at the cell surface. J Cell Sci110 (Pt 1): 95–103.
    • (1997) J Cell Sci , vol.110 , pp. 95-103
    • Marsh, M.1    Bron, R.2
  • 62
    • 77955347331 scopus 로고    scopus 로고
    • Endocytosis of chikungunya virus into mammalian cells: role of clathrin and early endosomal compartments
    • 20628602, . ().:
    • Bernard E, Solignat M, Gay B, Chazal N, Higgs S, et al. (2010) Endocytosis of chikungunya virus into mammalian cells: role of clathrin and early endosomal compartments. PLoS One5: e11479. doi: 10.1371/journal.pone.001147920628602
    • (2010) PLoS One , vol.5 , pp. 11479
    • Bernard, E.1    Solignat, M.2    Gay, B.3    Chazal, N.4    Higgs, S.5
  • 63
    • 84880624223 scopus 로고    scopus 로고
    • Natural variation in the heparan sulfate binding domain of the eastern equine encephalitis virus E2 glycoprotein alters interactions with cell surfaces and virulence in mice
    • 23720725, . ().:–
    • Gardner CL, Choi-Nurvitadhi J, Sun C, Bayer A, Hritz J, et al. (2013) Natural variation in the heparan sulfate binding domain of the eastern equine encephalitis virus E2 glycoprotein alters interactions with cell surfaces and virulence in mice. J Virol87: 8582–8590. doi: 10.1128/JVI.00937-1323720725
    • (2013) J Virol , vol.87 , pp. 8582-8590
    • Gardner, C.L.1    Choi-Nurvitadhi, J.2    Sun, C.3    Bayer, A.4    Hritz, J.5
  • 64
    • 0031869503 scopus 로고    scopus 로고
    • Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor
    • 9696832, ().:–
    • Klimstra WB, Ryman KD, Johnston RE, (1998) Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor. J Virol72: 7357–7366. 9696832
    • (1998) J Virol , vol.72 , pp. 7357-7366
    • Klimstra, W.B.1    Ryman, K.D.2    Johnston, R.E.3
  • 65
    • 0021770329 scopus 로고
    • Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells
    • 6698972, ().:–
    • Hsieh P, Robbins P. W., (1984) Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells. J Biol Chem259: 2375–2382. 6698972
    • (1984) J Biol Chem , vol.259 , pp. 2375-2382
    • Hsieh, P.1    Robbins, P.W.2
  • 66
    • 78649817910 scopus 로고    scopus 로고
    • Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
    • 21124458, . ().:–
    • Voss JE, Vaney MC, Duquerroy S, Vonrhein C, Girard-Blanc C, et al. (2010) Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature468: 709–712. doi: 10.1038/nature0955521124458
    • (2010) Nature , vol.468 , pp. 709-712
    • Voss, J.E.1    Vaney, M.C.2    Duquerroy, S.3    Vonrhein, C.4    Girard-Blanc, C.5
  • 67
    • 25144469371 scopus 로고    scopus 로고
    • Effect of hemagglutinin glycosylation on influenza virus susceptibility to neuraminidase inhibitors
    • 16160169, ().:–
    • Mishin VP, Novikov D, Hayden FG, Gubareva LV, (2005) Effect of hemagglutinin glycosylation on influenza virus susceptibility to neuraminidase inhibitors. J Virol79: 12416–12424. 16160169
    • (2005) J Virol , vol.79 , pp. 12416-12424
    • Mishin, V.P.1    Novikov, D.2    Hayden, F.G.3    Gubareva, L.V.4
  • 68
    • 0019470313 scopus 로고
    • Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin
    • 7213699, ().:–
    • Butters TD, Hughes RC, Vischer P, (1981) Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin. Biochim Biophys Acta640: 672–686. 7213699
    • (1981) Biochim Biophys Acta , vol.640 , pp. 672-686
    • Butters, T.D.1    Hughes, R.C.2    Vischer, P.3
  • 69
    • 0014944344 scopus 로고
    • Carbohydrate content of the membrane protein of Sindbis virus
    • 5418165, . ().:–
    • Strauss JH, Jr.Burge B. W., Darnell J. E., . (1970) Carbohydrate content of the membrane protein of Sindbis virus. J Mol Biol47: 437–448. 5418165
    • (1970) J Mol Biol , vol.47 , pp. 437-448
    • Strauss, J.H.1    Burge, B.W.2    Darnell, J.E.3
  • 70
    • 84877348014 scopus 로고    scopus 로고
    • A tyrosine-to-histidine switch at position 18 of the Ross River virus E2 glycoprotein is a determinant of virus fitness in disparate hosts
    • 23514884, ().:–
    • Jupille HJ, Medina-Rivera M, Hawman DW, Oko L, Morrison TE, (2013) A tyrosine-to-histidine switch at position 18 of the Ross River virus E2 glycoprotein is a determinant of virus fitness in disparate hosts. J Virol87: 5970–5984. doi: 10.1128/JVI.03326-1223514884
    • (2013) J Virol , vol.87 , pp. 5970-5984
    • Jupille, H.J.1    Medina-Rivera, M.2    Hawman, D.W.3    Oko, L.4    Morrison, T.E.5
  • 71
    • 0034984146 scopus 로고    scopus 로고
    • An amino acid substitution in the coding region of the E2 glycoprotein adapts Ross River virus to utilize heparan sulfate as an attachment moiety
    • 11413296, ().:–
    • Heil ML, Albee A, Strauss JH, Kuhn RJ, (2001) An amino acid substitution in the coding region of the E2 glycoprotein adapts Ross River virus to utilize heparan sulfate as an attachment moiety. J Virol75: 6303–6309. 11413296
    • (2001) J Virol , vol.75 , pp. 6303-6309
    • Heil, M.L.1    Albee, A.2    Strauss, J.H.3    Kuhn, R.J.4
  • 72
    • 0036784563 scopus 로고    scopus 로고
    • Adaptation of alphaviruses to heparan sulfate: interaction of Sindbis and Semliki forest viruses with liposomes containing lipid-conjugated heparin
    • 12239287, . ().:–
    • Smit JM, Waarts BL, Kimata K, Klimstra WB, Bittman R, et al. (2002) Adaptation of alphaviruses to heparan sulfate: interaction of Sindbis and Semliki forest viruses with liposomes containing lipid-conjugated heparin. J Virol76: 10128–10137. 12239287
    • (2002) J Virol , vol.76 , pp. 10128-10137
    • Smit, J.M.1    Waarts, B.L.2    Kimata, K.3    Klimstra, W.B.4    Bittman, R.5
  • 73
    • 18844376135 scopus 로고    scopus 로고
    • An arthritogenic alphavirus uses the alpha1beta1 integrin collagen receptor
    • 15892964, . ().:–
    • La Linn M, Eble JA, Lubken C, Slade RW, Heino J, et al. (2005) An arthritogenic alphavirus uses the alpha1beta1 integrin collagen receptor. Virology336: 229–239. 15892964
    • (2005) Virology , vol.336 , pp. 229-239
    • La Linn, M.1    Eble, J.A.2    Lubken, C.3    Slade, R.W.4    Heino, J.5
  • 74
    • 0020987415 scopus 로고
    • Sterol-free eukaryotic cells from continuous cell lines of insects
    • 6667502, ().:–
    • Mitsuhashi J, Nakasone S., Horie Y, (1983) Sterol-free eukaryotic cells from continuous cell lines of insects. Cell Biol Int Rep7: 1057–1062. 6667502
    • (1983) Cell Biol Int Rep , vol.7 , pp. 1057-1062
    • Mitsuhashi, J.1    Nakasone, S.2    Horie, Y.3
  • 75
    • 84890320471 scopus 로고    scopus 로고
    • Human Immunodeficiency Virus and Heparan Sulfate: From Attachment to Entry Inhibition
    • 24312095, ().:
    • Connell BJ, Lortat-Jacob H, (2013) Human Immunodeficiency Virus and Heparan Sulfate: From Attachment to Entry Inhibition. Front Immunol4: 385. doi: 10.3389/fimmu.2013.0038524312095
    • (2013) Front Immunol , vol.4 , pp. 385
    • Connell, B.J.1    Lortat-Jacob, H.2
  • 76
    • 0036438885 scopus 로고    scopus 로고
    • Glycosaminoglycan-binding ability is a feature of wild-type strains of herpes simplex virus type 1
    • 12441085, . ().:–
    • Trybala E, Roth A, Johansson M, Liljeqvist JA, Rekabdar E, et al. (2002) Glycosaminoglycan-binding ability is a feature of wild-type strains of herpes simplex virus type 1. Virology302: 413–419. 12441085
    • (2002) Virology , vol.302 , pp. 413-419
    • Trybala, E.1    Roth, A.2    Johansson, M.3    Liljeqvist, J.A.4    Rekabdar, E.5
  • 77
    • 0035031937 scopus 로고    scopus 로고
    • Echoviruses bind heparan sulfate at the cell surface
    • 11312365, ().:–
    • Goodfellow IG, Sioofy AB, Powell RM, Evans DJ, (2001) Echoviruses bind heparan sulfate at the cell surface. J Virol75: 4918–4921. 11312365
    • (2001) J Virol , vol.75 , pp. 4918-4921
    • Goodfellow, I.G.1    Sioofy, A.B.2    Powell, R.M.3    Evans, D.J.4
  • 78
    • 84886879612 scopus 로고    scopus 로고
    • Multiple heparan sulfate binding site engagements are required for the infectious entry of human papillomavirus type 16
    • 23966387, ().:–
    • Richards KF, Bienkowska-Haba M, Dasgupta J, Chen XS, Sapp M, (2013) Multiple heparan sulfate binding site engagements are required for the infectious entry of human papillomavirus type 16. J Virol87: 11426–11437. doi: 10.1128/JVI.01721-1323966387
    • (2013) J Virol , vol.87 , pp. 11426-11437
    • Richards, K.F.1    Bienkowska-Haba, M.2    Dasgupta, J.3    Chen, X.S.4    Sapp, M.5
  • 79
    • 0026345397 scopus 로고
    • Two mutations in the envelope glycoprotein E2 of Semliki Forest virus affecting the maturation and entry patterns of the virus alter pathogenicity for mice
    • 1660202, . ().:–
    • Glasgow GM, Sheahan BJ, Atkins GJ, Wahlberg JM, Salminen A, et al. (1991) Two mutations in the envelope glycoprotein E2 of Semliki Forest virus affecting the maturation and entry patterns of the virus alter pathogenicity for mice. Virology185: 741–748. 1660202
    • (1991) Virology , vol.185 , pp. 741-748
    • Glasgow, G.M.1    Sheahan, B.J.2    Atkins, G.J.3    Wahlberg, J.M.4    Salminen, A.5
  • 80
    • 0037229326 scopus 로고    scopus 로고
    • Glycosaminoglycan binding properties of natural venezuelan equine encephalitis virus isolates
    • 12502837, ().:–
    • Wang E, Brault AC, Powers AM, Kang W, Weaver SC, (2003) Glycosaminoglycan binding properties of natural venezuelan equine encephalitis virus isolates. J Virol77: 1204–1210. 12502837
    • (2003) J Virol , vol.77 , pp. 1204-1210
    • Wang, E.1    Brault, A.C.2    Powers, A.M.3    Kang, W.4    Weaver, S.C.5
  • 81
    • 0003680997 scopus 로고
    • Use of an Attenuated Strain of Venezuelan Equine Encephalomyelitis Virus for Immunization in Man
    • 14044773, ().:–
    • McKinney RW, Berge TO, Sawyer WD, Tigertt WD, Crozier D, (1963) Use of an Attenuated Strain of Venezuelan Equine Encephalomyelitis Virus for Immunization in Man. Am J Trop Med Hyg12: 597–603. 14044773
    • (1963) Am J Trop Med Hyg , vol.12 , pp. 597-603
    • McKinney, R.W.1    Berge, T.O.2    Sawyer, W.D.3    Tigertt, W.D.4    Crozier, D.5
  • 82
    • 56249086861 scopus 로고    scopus 로고
    • Yellow fever vaccine: past, present and future
    • 18847312, ().:–
    • Roukens AH, Visser LG, (2008) Yellow fever vaccine: past, present and future. Expert Opin Biol Ther8: 1787–1795. doi: 10.1517/14712598.8.11.178718847312
    • (2008) Expert Opin Biol Ther , vol.8 , pp. 1787-1795
    • Roukens, A.H.1    Visser, L.G.2
  • 83
    • 84867477389 scopus 로고    scopus 로고
    • US Military contributions to the global response to pandemic chikungunya
    • 22940380, . ().:–
    • Hoke CH, Jr.Pace-Templeton J, Pittman P, Malinoski FJ, Gibbs P, et al. (2012) US Military contributions to the global response to pandemic chikungunya. Vaccine30: 6713–6720. doi: 10.1016/j.vaccine.2012.08.02522940380
    • (2012) Vaccine , vol.30 , pp. 6713-6720
    • Hoke, C.H.1    Pace-Templeton, J.2    Pittman, P.3    Malinoski, F.J.4    Gibbs, P.5
  • 84
    • 0036239935 scopus 로고    scopus 로고
    • Mechanism of virulence attenuation of glycosaminoglycan-binding variants of Japanese encephalitis virus and Murray Valley encephalitis virus
    • 11967307, ().:–
    • Lee E, Lobigs M, (2002) Mechanism of virulence attenuation of glycosaminoglycan-binding variants of Japanese encephalitis virus and Murray Valley encephalitis virus. J Virol76: 4901–4911. 11967307
    • (2002) J Virol , vol.76 , pp. 4901-4911
    • Lee, E.1    Lobigs, M.2
  • 85
    • 44949131854 scopus 로고    scopus 로고
    • E protein domain III determinants of yellow fever virus 17D vaccine strain enhance binding to glycosaminoglycans, impede virus spread, and attenuate virulence
    • 18400851, ().:–
    • Lee E, Lobigs M, (2008) E protein domain III determinants of yellow fever virus 17D vaccine strain enhance binding to glycosaminoglycans, impede virus spread, and attenuate virulence. J Virol82: 6024–6033. doi: 10.1128/JVI.02509-0718400851
    • (2008) J Virol , vol.82 , pp. 6024-6033
    • Lee, E.1    Lobigs, M.2
  • 86
    • 84863613754 scopus 로고    scopus 로고
    • Attenuation of Chikungunya virus vaccine strain 181/clone 25 is determined by two amino acid substitutions in the E2 envelope glycoprotein
    • 22457519, . ().:–
    • Gorchakov R, Wang E, Leal G, Forrester NL, Plante K, et al. (2012) Attenuation of Chikungunya virus vaccine strain 181/clone 25 is determined by two amino acid substitutions in the E2 envelope glycoprotein. J Virol86: 6084–6096. doi: 10.1128/JVI.06449-1122457519
    • (2012) J Virol , vol.86 , pp. 6084-6096
    • Gorchakov, R.1    Wang, E.2    Leal, G.3    Forrester, N.L.4    Plante, K.5
  • 87
    • 84901801189 scopus 로고    scopus 로고
    • Chikungunya Vaccine Candidate Is Highly Attenuated and Protects Nonhuman Primates Against Telemetrically Monitored Disease Following a Single Dose
    • . ()
    • Roy CJ, Adams AP, Wang E, Plante K, Gorchakov R, et al. (2014) Chikungunya Vaccine Candidate Is Highly Attenuated and Protects Nonhuman Primates Against Telemetrically Monitored Disease Following a Single Dose. J Infect Dis.
    • (2014) J Infect Dis
    • Roy, C.J.1    Adams, A.P.2    Wang, E.3    Plante, K.4    Gorchakov, R.5
  • 88
    • 0034457916 scopus 로고    scopus 로고
    • Phase II safety and immunogenicity study of live chikungunya virus vaccine TSI-GSD-218
    • 11304054, . ().:–
    • Edelman R, Tacket CO, Wasserman SS, Bodison SA, Perry JG, et al. (2000) Phase II safety and immunogenicity study of live chikungunya virus vaccine TSI-GSD-218. Am J Trop Med Hyg62: 681–685. 11304054
    • (2000) Am J Trop Med Hyg , vol.62 , pp. 681-685
    • Edelman, R.1    Tacket, C.O.2    Wasserman, S.S.3    Bodison, S.A.4    Perry, J.G.5
  • 89
    • 33749067822 scopus 로고    scopus 로고
    • Virulence attenuation of Dengue virus due to augmented glycosaminoglycan-binding affinity and restriction in extraneural dissemination
    • 16963737, ().:–
    • Lee E, Wright PJ, Davidson A, Lobigs M, (2006) Virulence attenuation of Dengue virus due to augmented glycosaminoglycan-binding affinity and restriction in extraneural dissemination. J Gen Virol87: 2791–2801. 16963737
    • (2006) J Gen Virol , vol.87 , pp. 2791-2801
    • Lee, E.1    Wright, P.J.2    Davidson, A.3    Lobigs, M.4
  • 90
    • 80053353232 scopus 로고    scopus 로고
    • Implication of haematophagous arthropod salivary proteins in host-vector interactions
    • 21951834, . ().:
    • Fontaine A, Diouf I, Bakkali N, Misse D, Pages F, et al. (2011) Implication of haematophagous arthropod salivary proteins in host-vector interactions. Parasit Vectors4: 187. doi: 10.1186/1756-3305-4-18721951834
    • (2011) Parasit Vectors , vol.4 , pp. 187
    • Fontaine, A.1    Diouf, I.2    Bakkali, N.3    Misse, D.4    Pages, F.5
  • 91
    • 41749097836 scopus 로고    scopus 로고
    • The enhancement of arbovirus transmission and disease by mosquito saliva is associated with modulation of the host immune response
    • 18342898, ().:–
    • Schneider BS, Higgs S, (2008) The enhancement of arbovirus transmission and disease by mosquito saliva is associated with modulation of the host immune response. Trans R Soc Trop Med Hyg102: 400–408. doi: 10.1016/j.trstmh.2008.01.02418342898
    • (2008) Trans R Soc Trop Med Hyg , vol.102 , pp. 400-408
    • Schneider, B.S.1    Higgs, S.2
  • 92
    • 84863774074 scopus 로고    scopus 로고
    • Mosquito bite delivery of dengue virus enhances immunogenicity and pathogenesis in humanized mice
    • 22573866, ().:–
    • Cox J, Mota J, Sukupolvi-Petty S, Diamond MS, Rico-Hesse R, (2012) Mosquito bite delivery of dengue virus enhances immunogenicity and pathogenesis in humanized mice. J Virol86: 7637–7649. doi: 10.1128/JVI.00534-1222573866
    • (2012) J Virol , vol.86 , pp. 7637-7649
    • Cox, J.1    Mota, J.2    Sukupolvi-Petty, S.3    Diamond, M.S.4    Rico-Hesse, R.5
  • 93
    • 78951491635 scopus 로고    scopus 로고
    • Mosquito saliva causes enhancement of West Nile virus infection in mice
    • 21147918, . ().:–
    • Styer LM, Lim PY, Louie KL, Albright RG, Kramer LD, et al. (2011) Mosquito saliva causes enhancement of West Nile virus infection in mice. J Virol85: 1517–1527. doi: 10.1128/JVI.01112-1021147918
    • (2011) J Virol , vol.85 , pp. 1517-1527
    • Styer, L.M.1    Lim, P.Y.2    Louie, K.L.3    Albright, R.G.4    Kramer, L.D.5
  • 94
    • 0029979269 scopus 로고    scopus 로고
    • La Crosse viremias in white-tailed deer and chipmunks exposed by injection or mosquito bite
    • 8615443, ().:–
    • Osorio JE, Godsey MS, Defoliart GR, Yuill TM, (1996) La Crosse viremias in white-tailed deer and chipmunks exposed by injection or mosquito bite. Am J Trop Med Hyg54: 338–342. 8615443
    • (1996) Am J Trop Med Hyg , vol.54 , pp. 338-342
    • Osorio, J.E.1    Godsey, M.S.2    Defoliart, G.R.3    Yuill, T.M.4
  • 95
    • 77957927271 scopus 로고    scopus 로고
    • Host immune response to mosquito-transmitted chikungunya virus differs from that elicited by needle inoculated virus
    • 20711354, . ().:
    • Thangamani S, Higgs S, Ziegler S, Vanlandingham D, Tesh R, et al. (2010) Host immune response to mosquito-transmitted chikungunya virus differs from that elicited by needle inoculated virus. PLoS One5: e12137. doi: 10.1371/journal.pone.001213720711354
    • (2010) PLoS One , vol.5 , pp. 12137
    • Thangamani, S.1    Higgs, S.2    Ziegler, S.3    Vanlandingham, D.4    Tesh, R.5
  • 96
    • 84890863649 scopus 로고    scopus 로고
    • Mosquito saliva serine protease enhances dissemination of dengue virus into the mammalian host
    • 24131723, . ().:–
    • Conway MJ, Watson AM, Colpitts TM, Dragovic SM, Li Z, et al. (2014) Mosquito saliva serine protease enhances dissemination of dengue virus into the mammalian host. J Virol88: 164–175. doi: 10.1128/JVI.02235-1324131723
    • (2014) J Virol , vol.88 , pp. 164-175
    • Conway, M.J.1    Watson, A.M.2    Colpitts, T.M.3    Dragovic, S.M.4    Li, Z.5


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