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Volumn 209, Issue , 2015, Pages 67-75

Immune modulation by virus-encoded secreted chemokine binding proteins

Author keywords

Chemokine binding proteins; Chemokines; Glycosaminoglycans; Herpesviruses; Immune evasion; Poxviruses

Indexed keywords

BINDING PROTEIN; CHEMOKINE; CHEMOKINE BINDING PROTEIN; UNCLASSIFIED DRUG; DNA VIRUS; PROTEIN BINDING;

EID: 84959542315     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2015.02.028     Document Type: Article
Times cited : (37)

References (98)
  • 1
    • 0037271850 scopus 로고    scopus 로고
    • Viral mimicry of cytokines, chemokines and their receptors
    • Alcami A. Viral mimicry of cytokines, chemokines and their receptors. Nat. Rev. Immunol. 2003, 3(1):36-50.
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.1 , pp. 36-50
    • Alcami, A.1
  • 2
    • 0033831421 scopus 로고    scopus 로고
    • Viral mechanisms of immune evasion
    • Alcami A., Koszinowski U.H. Viral mechanisms of immune evasion. Immunol. Today 2000, 21(9):447-455.
    • (2000) Immunol. Today , vol.21 , Issue.9 , pp. 447-455
    • Alcami, A.1    Koszinowski, U.H.2
  • 3
    • 0031964453 scopus 로고    scopus 로고
    • Blockade of chemokine activity by a soluble chemokine binding protein from vaccinia virus
    • Alcami A., Symons J.A., Collins P.D., Williams T.J., Smith G.L. Blockade of chemokine activity by a soluble chemokine binding protein from vaccinia virus. J. Immunol. 1998, 160(2):624-633.
    • (1998) J. Immunol. , vol.160 , Issue.2 , pp. 624-633
    • Alcami, A.1    Symons, J.A.2    Collins, P.D.3    Williams, T.J.4    Smith, G.L.5
  • 4
  • 6
    • 37549041251 scopus 로고    scopus 로고
    • Dual GPCR and GAG mimicry by the M3 chemokine decoy receptor
    • Alexander-Brett J.M., Fremont D.H. Dual GPCR and GAG mimicry by the M3 chemokine decoy receptor. J. Exp. Med. 2007, 204(13):3157-3172.
    • (2007) J. Exp. Med. , vol.204 , Issue.13 , pp. 3157-3172
    • Alexander-Brett, J.M.1    Fremont, D.H.2
  • 7
    • 77958454272 scopus 로고    scopus 로고
    • SECRET domain of variola virus CrmB protein can be a member of poxviral type II chemokine-binding proteins family
    • Antonets D.V., Nepomnyashchikh T.S., Shchelkunov S.N. SECRET domain of variola virus CrmB protein can be a member of poxviral type II chemokine-binding proteins family. BMC Res. Notes 2010, 3:271.
    • (2010) BMC Res. Notes , vol.3 , pp. 271
    • Antonets, D.V.1    Nepomnyashchikh, T.S.2    Shchelkunov, S.N.3
  • 8
    • 33746215102 scopus 로고    scopus 로고
    • Structural determinants of chemokine binding by an Ectromelia virus-encoded decoy receptor
    • Arnold P.L., Fremont D.H. Structural determinants of chemokine binding by an Ectromelia virus-encoded decoy receptor. J. Virol. 2006, 80(15):7439-7449.
    • (2006) J. Virol. , vol.80 , Issue.15 , pp. 7439-7449
    • Arnold, P.L.1    Fremont, D.H.2
  • 9
    • 0032499260 scopus 로고    scopus 로고
    • Chemokines and leukocyte traffic
    • Baggiolini M. Chemokines and leukocyte traffic. Nature 1998, 392(6676):565-568.
    • (1998) Nature , vol.392 , Issue.6676 , pp. 565-568
    • Baggiolini, M.1
  • 11
    • 0028229074 scopus 로고
    • An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoproteins gG, gE, gI or the putative gJ
    • Balan P., Davis-Poynter N., Bell S., Atkinson H., Browne H., Minson T. An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoproteins gG, gE, gI or the putative gJ. J. Gen. Virol. 1994, 75(Pt 6):1245-1258.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1245-1258
    • Balan, P.1    Davis-Poynter, N.2    Bell, S.3    Atkinson, H.4    Browne, H.5    Minson, T.6
  • 12
    • 84888197295 scopus 로고    scopus 로고
    • Defining the anti-inflammatory activity of a potent myxomaviral chemokine modulating protein, M-T7, through site directed mutagenesis
    • Bartee M.Y., Chen H., Dai E., Liu L.Y., Davids J.A., Lucas A. Defining the anti-inflammatory activity of a potent myxomaviral chemokine modulating protein, M-T7, through site directed mutagenesis. Cytokine 2013, 65(1):79-87.
    • (2013) Cytokine , vol.65 , Issue.1 , pp. 79-87
    • Bartee, M.Y.1    Chen, H.2    Dai, E.3    Liu, L.Y.4    Davids, J.A.5    Lucas, A.6
  • 13
    • 0035900713 scopus 로고    scopus 로고
    • The viral CC chemokine-binding protein vCCI inhibits monocyte chemoattractant protein-1 activity by masking its CCR2B-binding site
    • Beck C.G., Studer C., Zuber J.F., Demange B.J., Manning U., Urfer R. The viral CC chemokine-binding protein vCCI inhibits monocyte chemoattractant protein-1 activity by masking its CCR2B-binding site. J. Biol. Chem. 2001, 276(46):43270-43276.
    • (2001) J. Biol. Chem. , vol.276 , Issue.46 , pp. 43270-43276
    • Beck, C.G.1    Studer, C.2    Zuber, J.F.3    Demange, B.J.4    Manning, U.5    Urfer, R.6
  • 15
    • 0034954034 scopus 로고    scopus 로고
    • Interferons alpha and beta as immune regulators - a new look
    • Biron C.A. Interferons alpha and beta as immune regulators - a new look. Immunity 2001, 14(6):661-664.
    • (2001) Immunity , vol.14 , Issue.6 , pp. 661-664
    • Biron, C.A.1
  • 16
    • 0037799237 scopus 로고    scopus 로고
    • The core domain of chemokines binds CCR5 extracellular domains while their amino terminus interacts with the transmembrane helix bundle
    • Blanpain C., Doranz B.J., Bondue A., Govaerts C., De Leener A., Vassart G., Doms R.W., Proudfoot A., Parmentier M. The core domain of chemokines binds CCR5 extracellular domains while their amino terminus interacts with the transmembrane helix bundle. J. Biol. Chem. 2003, 278(7):5179-5187.
    • (2003) J. Biol. Chem. , vol.278 , Issue.7 , pp. 5179-5187
    • Blanpain, C.1    Doranz, B.J.2    Bondue, A.3    Govaerts, C.4    De Leener, A.5    Vassart, G.6    Doms, R.W.7    Proudfoot, A.8    Parmentier, M.9
  • 18
    • 0035817385 scopus 로고    scopus 로고
    • A secreted chemokine binding protein encoded by murine gammaherpesvirus-68 is necessary for the establishment of a normal latent load
    • Bridgeman A., Stevenson P.G., Simas J.P., Efstathiou S. A secreted chemokine binding protein encoded by murine gammaherpesvirus-68 is necessary for the establishment of a normal latent load. J. Exp. Med. 2001, 194(3):301-312.
    • (2001) J. Exp. Med. , vol.194 , Issue.3 , pp. 301-312
    • Bridgeman, A.1    Stevenson, P.G.2    Simas, J.P.3    Efstathiou, S.4
  • 19
    • 0037450769 scopus 로고    scopus 로고
    • Glycoprotein G isoforms from some alphaherpesviruses function as broad-spectrum chemokine binding proteins
    • Bryant N.A., Davis-Poynter N., Vanderplasschen A., Alcami A. Glycoprotein G isoforms from some alphaherpesviruses function as broad-spectrum chemokine binding proteins. EMBO J. 2003, 22(4):833-846.
    • (2003) EMBO J. , vol.22 , Issue.4 , pp. 833-846
    • Bryant, N.A.1    Davis-Poynter, N.2    Vanderplasschen, A.3    Alcami, A.4
  • 20
    • 77956940247 scopus 로고    scopus 로고
    • Pan-CC chemokine neutralization restricts splenocyte egress and reduces inflammation in a model of arthritis
    • Buatois V., Fagete S., Magistrelli G., Chatel L., Fischer N., Kosco-Vilbois M.H., Ferlin W.G. Pan-CC chemokine neutralization restricts splenocyte egress and reduces inflammation in a model of arthritis. J. Immunol. 2010, 185(4):2544-2554.
    • (2010) J. Immunol. , vol.185 , Issue.4 , pp. 2544-2554
    • Buatois, V.1    Fagete, S.2    Magistrelli, G.3    Chatel, L.4    Fischer, N.5    Kosco-Vilbois, M.H.6    Ferlin, W.G.7
  • 21
    • 0037169511 scopus 로고    scopus 로고
    • Comprehensive mapping of poxvirus vCCI chemokine-binding protein. Expanded range of ligand interactions and unusual dissociation kinetics
    • Burns J.M., Dairaghi D.J., Deitz M., Tsang M., Schall T.J. Comprehensive mapping of poxvirus vCCI chemokine-binding protein. Expanded range of ligand interactions and unusual dissociation kinetics. J. Biol. Chem. 2002, 277(4):2785-2789.
    • (2002) J. Biol. Chem. , vol.277 , Issue.4 , pp. 2785-2789
    • Burns, J.M.1    Dairaghi, D.J.2    Deitz, M.3    Tsang, M.4    Schall, T.J.5
  • 23
    • 0033607216 scopus 로고    scopus 로고
    • Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus
    • Carfi A., Smith C.A., Smolak P.J., McGrew J., Wiley D.C. Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus. Proc. Natl. Acad. Sci. U.S.A. 1999, 96(22):12379-12383.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , Issue.22 , pp. 12379-12383
    • Carfi, A.1    Smith, C.A.2    Smolak, P.J.3    McGrew, J.4    Wiley, D.C.5
  • 24
    • 30344463834 scopus 로고    scopus 로고
    • Deletion of gene A41L enhances vaccinia virus immunogenicity and vaccine efficacy
    • Clark R.H., Kenyon J.C., Bartlett N.W., Tscharke D.C., Smith G.L. Deletion of gene A41L enhances vaccinia virus immunogenicity and vaccine efficacy. J. Gen. Virol. 2006, 87(Pt 1):29-38.
    • (2006) J. Gen. Virol. , vol.87 , pp. 29-38
    • Clark, R.H.1    Kenyon, J.C.2    Bartlett, N.W.3    Tscharke, D.C.4    Smith, G.L.5
  • 25
    • 28044464024 scopus 로고    scopus 로고
    • Both soluble and membrane-anchored forms of felid herpesvirus 1 glycoprotein G function as a broad-spectrum chemokine-binding protein
    • Costes B., Ruiz-Arguello M.B., Bryant N.A., Alcami A., Vanderplasschen A. Both soluble and membrane-anchored forms of felid herpesvirus 1 glycoprotein G function as a broad-spectrum chemokine-binding protein. J. Gen. Virol. 2005, 86(Pt 12):3209-3214.
    • (2005) J. Gen. Virol. , vol.86 , pp. 3209-3214
    • Costes, B.1    Ruiz-Arguello, M.B.2    Bryant, N.A.3    Alcami, A.4    Vanderplasschen, A.5
  • 28
    • 0032499791 scopus 로고    scopus 로고
    • Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 "fusin" coreceptor
    • Dealwis C., Fernandez E.J., Thompson D.A., Simon R.J., Siani M.A., Lolis E. Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 "fusin" coreceptor. Proc. Natl. Acad. Sci. U.S.A. 1998, 95(12):6941-6946.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , Issue.12 , pp. 6941-6946
    • Dealwis, C.1    Fernandez, E.J.2    Thompson, D.A.3    Simon, R.J.4    Siani, M.A.5    Lolis, E.6
  • 30
    • 34147096573 scopus 로고    scopus 로고
    • Glycoprotein G deficient infectious laryngotracheitis virus is a candidate attenuated vaccine
    • Devlin J.M., Browning G.F., Hartley C.A., Gilkerson J.R. Glycoprotein G deficient infectious laryngotracheitis virus is a candidate attenuated vaccine. Vaccine 2007, 25(18):3561-3566.
    • (2007) Vaccine , vol.25 , Issue.18 , pp. 3561-3566
    • Devlin, J.M.1    Browning, G.F.2    Hartley, C.A.3    Gilkerson, J.R.4
  • 31
    • 74149090246 scopus 로고    scopus 로고
    • Evaluation of immunological responses to a glycoprotein G deficient candidate vaccine strain of infectious laryngotracheitis virus
    • Devlin J.M., Viejo-Borbolla A., Browning G.F., Noormohammadi A.H., Gilkerson J.R., Alcami A., Hartley C.A. Evaluation of immunological responses to a glycoprotein G deficient candidate vaccine strain of infectious laryngotracheitis virus. Vaccine 2010, 28(5):1325-1332.
    • (2010) Vaccine , vol.28 , Issue.5 , pp. 1325-1332
    • Devlin, J.M.1    Viejo-Borbolla, A.2    Browning, G.F.3    Noormohammadi, A.H.4    Gilkerson, J.R.5    Alcami, A.6    Hartley, C.A.7
  • 32
    • 77949535212 scopus 로고    scopus 로고
    • Structural basis of chemokine sequestration by a tick chemokine binding protein: the crystal structure of the complex between Evasin-1 and CCL3
    • Dias J.M., Losberger C., Deruaz M., Power C.A., Proudfoot A.E., Shaw J.P. Structural basis of chemokine sequestration by a tick chemokine binding protein: the crystal structure of the complex between Evasin-1 and CCL3. PLoS ONE 2009, 4(12):e8514.
    • (2009) PLoS ONE , vol.4 , Issue.12 , pp. e8514
    • Dias, J.M.1    Losberger, C.2    Deruaz, M.3    Power, C.A.4    Proudfoot, A.E.5    Shaw, J.P.6
  • 34
  • 35
    • 32944462309 scopus 로고    scopus 로고
    • Anti-immunology: evasion of the host immune system by bacterial and viral pathogens
    • Finlay B.B., McFadden G. Anti-immunology: evasion of the host immune system by bacterial and viral pathogens. Cell 2006, 124(4):767-782.
    • (2006) Cell , vol.124 , Issue.4 , pp. 767-782
    • Finlay, B.B.1    McFadden, G.2
  • 37
    • 77957872381 scopus 로고    scopus 로고
    • Immunogenic profiling in mice of a HIV/AIDS vaccine candidate (MVA-B) expressing four HIV-1 antigens and potentiation by specific gene deletions
    • Garcia-Arriaza J., Najera J.L., Gomez C.E., Sorzano C.O., Esteban M. Immunogenic profiling in mice of a HIV/AIDS vaccine candidate (MVA-B) expressing four HIV-1 antigens and potentiation by specific gene deletions. PLoS ONE 2010, 5(8):e12395.
    • (2010) PLoS ONE , vol.5 , Issue.8 , pp. e12395
    • Garcia-Arriaza, J.1    Najera, J.L.2    Gomez, C.E.3    Sorzano, C.O.4    Esteban, M.5
  • 38
    • 0036828085 scopus 로고    scopus 로고
    • Comparison of the complete DNA sequences of the Oka varicella vaccine and its parental virus
    • Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K. Comparison of the complete DNA sequences of the Oka varicella vaccine and its parental virus. J. Virol. 2002, 76(22):11447-11459.
    • (2002) J. Virol. , vol.76 , Issue.22 , pp. 11447-11459
    • Gomi, Y.1    Sunamachi, H.2    Mori, Y.3    Nagaike, K.4    Takahashi, M.5    Yamanishi, K.6
  • 39
    • 33745824286 scopus 로고    scopus 로고
    • Chemokine scavenging by D6: a movable feast?
    • Graham G.J., McKimmie C.S. Chemokine scavenging by D6: a movable feast?. Trends Immunol. 2006, 27(8):381-386.
    • (2006) Trends Immunol. , vol.27 , Issue.8 , pp. 381-386
    • Graham, G.J.1    McKimmie, C.S.2
  • 41
    • 0034255119 scopus 로고    scopus 로고
    • Cytokine-mediated control of viral infections
    • Guidotti L.G., Chisari F.V. Cytokine-mediated control of viral infections. Virology 2000, 273(2):221-227.
    • (2000) Virology , vol.273 , Issue.2 , pp. 221-227
    • Guidotti, L.G.1    Chisari, F.V.2
  • 42
    • 0032744451 scopus 로고    scopus 로고
    • Immunomodulation by virulence proteins of the parapoxvirus orf virus
    • Haig D.M., Fleming S. Immunomodulation by virulence proteins of the parapoxvirus orf virus. Vet. Immunol. Immunopathol. 1999, 72(1-2):81-86.
    • (1999) Vet. Immunol. Immunopathol. , vol.72 , Issue.1-2 , pp. 81-86
    • Haig, D.M.1    Fleming, S.2
  • 43
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - as exemplified by chemokines
    • Handel T.M., Johnson Z., Crown S.E., Lau E.K., Proudfoot A.E. Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu. Rev. Biochem. 2005, 74:385-410.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 44
    • 0028059613 scopus 로고
    • Cowpox virus contains two copies of an early gene encoding a soluble secreted form of the type II TNF receptor
    • Hu F.Q., Smith C.A., Pickup D.J. Cowpox virus contains two copies of an early gene encoding a soluble secreted form of the type II TNF receptor. Virology 1994, 204(1):343-356.
    • (1994) Virology , vol.204 , Issue.1 , pp. 343-356
    • Hu, F.Q.1    Smith, C.A.2    Pickup, D.J.3
  • 46
    • 27144468308 scopus 로고    scopus 로고
    • Interaction of chemokines and glycosaminoglycans: a new twist in the regulation of chemokine function with opportunities for therapeutic intervention
    • Johnson Z., Proudfoot A.E., Handel T.M. Interaction of chemokines and glycosaminoglycans: a new twist in the regulation of chemokine function with opportunities for therapeutic intervention. Cytokine Growth Factor Rev. 2005, 16(6):625-636.
    • (2005) Cytokine Growth Factor Rev. , vol.16 , Issue.6 , pp. 625-636
    • Johnson, Z.1    Proudfoot, A.E.2    Handel, T.M.3
  • 47
    • 0026476623 scopus 로고
    • Role of different genes in the virulence and pathogenesis of Aujeszky's disease virus
    • Kimman T.G., Pol J.M., de Wind N., Oei-Lie N., Berns A.J., Gielkens A.L. Role of different genes in the virulence and pathogenesis of Aujeszky's disease virus. Vet. Microbiol. 1992, 33(1-4):45-52.
    • (1992) Vet. Microbiol. , vol.33 , Issue.1-4 , pp. 45-52
    • Kimman, T.G.1    Pol, J.M.2    de Wind, N.3    Oei-Lie, N.4    Berns, A.J.5    Gielkens, A.L.6
  • 48
    • 84896790507 scopus 로고    scopus 로고
    • Structural insights into the interaction between a potent anti-inflammatory protein, viral CC chemokine inhibitor (vCCI), and the human CC chemokine, Eotaxin-1
    • Kuo N.W., Gao Y.G., Schill M.S., Isern N., Dupureur C.M., Liwang P.J. Structural insights into the interaction between a potent anti-inflammatory protein, viral CC chemokine inhibitor (vCCI), and the human CC chemokine, Eotaxin-1. J. Biol. Chem. 2014, 289(10):6592-6603.
    • (2014) J. Biol. Chem. , vol.289 , Issue.10 , pp. 6592-6603
    • Kuo, N.W.1    Gao, Y.G.2    Schill, M.S.3    Isern, N.4    Dupureur, C.M.5    Liwang, P.J.6
  • 49
    • 0031010760 scopus 로고    scopus 로고
    • The purified myxoma virus gamma interferon receptor homolog M-T7 interacts with the heparin-binding domains of chemokines
    • Lalani A.S., Graham K., Mossman K., Rajarathnam K., Clark-Lewis I., Kelvin D., McFadden G. The purified myxoma virus gamma interferon receptor homolog M-T7 interacts with the heparin-binding domains of chemokines. J. Virol. 1997, 71(6):4356-4363.
    • (1997) J. Virol. , vol.71 , Issue.6 , pp. 4356-4363
    • Lalani, A.S.1    Graham, K.2    Mossman, K.3    Rajarathnam, K.4    Clark-Lewis, I.5    Kelvin, D.6    McFadden, G.7
  • 50
    • 0033541380 scopus 로고    scopus 로고
    • Role of the myxoma virus soluble CC-chemokine inhibitor glycoprotein, M-T1, during myxoma virus pathogenesis
    • Lalani A.S., Masters J., Graham K., Liu L., Lucas A., McFadden G. Role of the myxoma virus soluble CC-chemokine inhibitor glycoprotein, M-T1, during myxoma virus pathogenesis. Virology 1999, 256(2):233-245.
    • (1999) Virology , vol.256 , Issue.2 , pp. 233-245
    • Lalani, A.S.1    Masters, J.2    Graham, K.3    Liu, L.4    Lucas, A.5    McFadden, G.6
  • 51
    • 0032505546 scopus 로고    scopus 로고
    • Functional comparisons among members of the poxvirus T1/35kDa family of soluble CC-chemokine inhibitor glycoproteins
    • Lalani A.S., Ness T.L., Singh R., Harrison J.K., Seet B.T., Kelvin D.J., McFadden G., Moyer R.W. Functional comparisons among members of the poxvirus T1/35kDa family of soluble CC-chemokine inhibitor glycoproteins. Virology 1998, 250(1):173-184.
    • (1998) Virology , vol.250 , Issue.1 , pp. 173-184
    • Lalani, A.S.1    Ness, T.L.2    Singh, R.3    Harrison, J.K.4    Seet, B.T.5    Kelvin, D.J.6    McFadden, G.7    Moyer, R.W.8
  • 52
    • 67649221447 scopus 로고    scopus 로고
    • Orf virus-encoded chemokine-binding protein is a potent inhibitor of inflammatory monocyte recruitment in a mouse skin model
    • Lateef Z., Baird M.A., Wise L.M., Mercer A.A., Fleming S.B. Orf virus-encoded chemokine-binding protein is a potent inhibitor of inflammatory monocyte recruitment in a mouse skin model. J. Gen. Virol. 2009, 90(Pt 6):1477-1482.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1477-1482
    • Lateef, Z.1    Baird, M.A.2    Wise, L.M.3    Mercer, A.A.4    Fleming, S.B.5
  • 53
    • 77954247270 scopus 로고    scopus 로고
    • The chemokine-binding protein encoded by the poxvirus orf virus inhibits recruitment of dendritic cells to sites of skin inflammation and migration to peripheral lymph nodes
    • Lateef Z., Baird M.A., Wise L.M., Young S., Mercer A.A., Fleming S.B. The chemokine-binding protein encoded by the poxvirus orf virus inhibits recruitment of dendritic cells to sites of skin inflammation and migration to peripheral lymph nodes. Cell. Microbiol. 2010, 12(5):665-676.
    • (2010) Cell. Microbiol. , vol.12 , Issue.5 , pp. 665-676
    • Lateef, Z.1    Baird, M.A.2    Wise, L.M.3    Young, S.4    Mercer, A.A.5    Fleming, S.B.6
  • 58
    • 33845203351 scopus 로고    scopus 로고
    • Tuning inflammation and immunity by chemokine sequestration: decoys and more
    • Mantovani A., Bonecchi R., Locati M. Tuning inflammation and immunity by chemokine sequestration: decoys and more. Nat. Rev. Immunol. 2006, 6(12):907-918.
    • (2006) Nat. Rev. Immunol. , vol.6 , Issue.12 , pp. 907-918
    • Mantovani, A.1    Bonecchi, R.2    Locati, M.3
  • 59
    • 0028890737 scopus 로고
    • Mapping and investigation of the role in pathogenesis of the major unique secreted 35-kDa protein of rabbitpox virus
    • Martinez-Pomares L., Thompson J.P., Moyer R.W. Mapping and investigation of the role in pathogenesis of the major unique secreted 35-kDa protein of rabbitpox virus. Virology 1995, 206(1):591-600.
    • (1995) Virology , vol.206 , Issue.1 , pp. 591-600
    • Martinez-Pomares, L.1    Thompson, J.P.2    Moyer, R.W.3
  • 60
    • 0023845903 scopus 로고
    • Virulence of and establishment of latency by genetically engineered deletion mutants of herpes simplex virus 1
    • Meignier B., Longnecker R., Mavromara-Nazos P., Sears A.E., Roizman B. Virulence of and establishment of latency by genetically engineered deletion mutants of herpes simplex virus 1. Virology 1988, 162(1):251-254.
    • (1988) Virology , vol.162 , Issue.1 , pp. 251-254
    • Meignier, B.1    Longnecker, R.2    Mavromara-Nazos, P.3    Sears, A.E.4    Roizman, B.5
  • 61
    • 0030048279 scopus 로고    scopus 로고
    • Myxoma virus M-T7, a secreted homolog of the interferon-gamma receptor, is a critical virulence factor for the development of myxomatosis in European rabbits
    • Mossman K., Nation P., Macen J., Garbutt M., Lucas A., McFadden G. Myxoma virus M-T7, a secreted homolog of the interferon-gamma receptor, is a critical virulence factor for the development of myxomatosis in European rabbits. Virology 1996, 215(1):17-30.
    • (1996) Virology , vol.215 , Issue.1 , pp. 17-30
    • Mossman, K.1    Nation, P.2    Macen, J.3    Garbutt, M.4    Lucas, A.5    McFadden, G.6
  • 62
    • 0028980327 scopus 로고
    • The myxoma virus-soluble interferon-gamma receptor homolog, M-T7, inhibits interferon-gamma in a species-specific manner
    • Mossman K., Upton C., McFadden G. The myxoma virus-soluble interferon-gamma receptor homolog, M-T7, inhibits interferon-gamma in a species-specific manner. J. Biol. Chem. 1995, 270(7):3031-3038.
    • (1995) J. Biol. Chem. , vol.270 , Issue.7 , pp. 3031-3038
    • Mossman, K.1    Upton, C.2    McFadden, G.3
  • 63
    • 0034845560 scopus 로고    scopus 로고
    • The vaccinia virus A41L protein is a soluble 30 kDa glycoprotein that affects virus virulence
    • Ng A., Tscharke D.C., Reading P.C., Smith G.L. The vaccinia virus A41L protein is a soluble 30 kDa glycoprotein that affects virus virulence. J. Gen. Virol. 2001, 82(Pt 9):2095-2105.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2095-2105
    • Ng, A.1    Tscharke, D.C.2    Reading, P.C.3    Smith, G.L.4
  • 64
    • 0028140143 scopus 로고
    • Multigenic evasion of inflammation by poxviruses
    • Palumbo G.J., Buller R.M., Glasgow W.C. Multigenic evasion of inflammation by poxviruses. J. Virol. 1994, 68(3):1737-1749.
    • (1994) J. Virol. , vol.68 , Issue.3 , pp. 1737-1749
    • Palumbo, G.J.1    Buller, R.M.2    Glasgow, W.C.3
  • 66
    • 0034142342 scopus 로고    scopus 로고
    • Vaccinia virus gene B7R encodes an 18-kDa protein that is resident in the endoplasmic reticulum and affects virus virulence
    • Price N., Tscharke D.C., Hollinshead M., Smith G.L. Vaccinia virus gene B7R encodes an 18-kDa protein that is resident in the endoplasmic reticulum and affects virus virulence. Virology 2000, 267(1):65-79.
    • (2000) Virology , vol.267 , Issue.1 , pp. 65-79
    • Price, N.1    Tscharke, D.C.2    Hollinshead, M.3    Smith, G.L.4
  • 67
    • 0036485214 scopus 로고    scopus 로고
    • Chemokine receptors: multifaceted therapeutic targets
    • Proudfoot A.E. Chemokine receptors: multifaceted therapeutic targets. Nat. Rev. Immunol. 2002, 2(2):106-115.
    • (2002) Nat. Rev. Immunol. , vol.2 , Issue.2 , pp. 106-115
    • Proudfoot, A.E.1
  • 68
    • 33745439311 scopus 로고    scopus 로고
    • The biological relevance of chemokine-proteoglycan interactions
    • Proudfoot A.E. The biological relevance of chemokine-proteoglycan interactions. Biochem. Soc. Trans. 2006, 34(Pt 3):422-426.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 422-426
    • Proudfoot, A.E.1
  • 69
    • 0037307820 scopus 로고    scopus 로고
    • A soluble chemokine-binding protein from vaccinia virus reduces virus virulence and the inflammatory response to infection
    • Reading P.C., Symons J.A., Smith G.L. A soluble chemokine-binding protein from vaccinia virus reduces virus virulence and the inflammatory response to infection. J. Immunol. 2003, 170(3):1435-1442.
    • (2003) J. Immunol. , vol.170 , Issue.3 , pp. 1435-1442
    • Reading, P.C.1    Symons, J.A.2    Smith, G.L.3
  • 71
    • 0034747807 scopus 로고    scopus 로고
    • CrmE, a novel soluble tumor necrosis factor receptor encoded by poxviruses
    • Saraiva M., Alcami A. CrmE, a novel soluble tumor necrosis factor receptor encoded by poxviruses. J. Virol. 2001, 75(1):226-233.
    • (2001) J. Virol. , vol.75 , Issue.1 , pp. 226-233
    • Saraiva, M.1    Alcami, A.2
  • 73
    • 0345598122 scopus 로고    scopus 로고
    • Analysis of an orf virus chemokine-binding protein: Shifting ligand specificities among a family of poxvirus viroceptors
    • Seet B.T., McCaughan C.A., Handel T.M., Mercer A., Brunetti C., McFadden G., Fleming S.B. Analysis of an orf virus chemokine-binding protein: Shifting ligand specificities among a family of poxvirus viroceptors. Proc. Natl. Acad. Sci. U.S.A. 2003, 100(25):15137-15142.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , Issue.25 , pp. 15137-15142
    • Seet, B.T.1    McCaughan, C.A.2    Handel, T.M.3    Mercer, A.4    Brunetti, C.5    McFadden, G.6    Fleming, S.B.7
  • 75
    • 0030248239 scopus 로고    scopus 로고
    • Cowpox virus genome encodes a second soluble homologue of cellular TNF receptors, distinct from CrmB, that binds TNF but not LT alpha
    • Smith C.A., Hu F.Q., Smith T.D., Richards C.L., Smolak P., Goodwin R.G., Pickup D.J. Cowpox virus genome encodes a second soluble homologue of cellular TNF receptors, distinct from CrmB, that binds TNF but not LT alpha. Virology 1996, 223(1):132-147.
    • (1996) Virology , vol.223 , Issue.1 , pp. 132-147
    • Smith, C.A.1    Hu, F.Q.2    Smith, T.D.3    Richards, C.L.4    Smolak, P.5    Goodwin, R.G.6    Pickup, D.J.7
  • 76
  • 77
    • 0036635507 scopus 로고    scopus 로고
    • Smallpox: anything to declare?
    • Smith G.L., McFadden G. Smallpox: anything to declare?. Nat. Rev. Immunol. 2002, 2(7):521-527.
    • (2002) Nat. Rev. Immunol. , vol.2 , Issue.7 , pp. 521-527
    • Smith, G.L.1    McFadden, G.2
  • 79
    • 0023201475 scopus 로고
    • Replication and virulence of pseudorabies virus mutants lacking glycoprotein gX
    • Thomsen D.R., Marchioli C.C., Yancey R.J., Post L.E. Replication and virulence of pseudorabies virus mutants lacking glycoprotein gX. J. Virol. 1987, 61(1):229-232.
    • (1987) J. Virol. , vol.61 , Issue.1 , pp. 229-232
    • Thomsen, D.R.1    Marchioli, C.C.2    Yancey, R.J.3    Post, L.E.4
  • 80
    • 0025880218 scopus 로고
    • Myxoma virus expresses a secreted protein with homology to the tumor necrosis factor receptor gene family that contributes to viral virulence
    • Upton C., Macen J.L., Schreiber M., McFadden G. Myxoma virus expresses a secreted protein with homology to the tumor necrosis factor receptor gene family that contributes to viral virulence. Virology 1991, 184(1):370-382.
    • (1991) Virology , vol.184 , Issue.1 , pp. 370-382
    • Upton, C.1    Macen, J.L.2    Schreiber, M.3    McFadden, G.4
  • 81
    • 0026621761 scopus 로고
    • Encoding of a homolog of the IFN-gamma receptor by myxoma virus
    • Upton C., Mossman K., McFadden G. Encoding of a homolog of the IFN-gamma receptor by myxoma virus. Science 1992, 258(5086):1369-1372.
    • (1992) Science , vol.258 , Issue.5086 , pp. 1369-1372
    • Upton, C.1    Mossman, K.2    McFadden, G.3
  • 83
    • 0036218112 scopus 로고    scopus 로고
    • Critical role for a high-affinity chemokine-binding protein in gamma-herpesvirus-induced lethal meningitis
    • van Berkel V., Levine B., Kapadia S.B., Goldman J.E., Speck S.H., Virgin H.W. Critical role for a high-affinity chemokine-binding protein in gamma-herpesvirus-induced lethal meningitis. J. Clin. Invest. 2002, 109(7):905-914.
    • (2002) J. Clin. Invest. , vol.109 , Issue.7 , pp. 905-914
    • van Berkel, V.1    Levine, B.2    Kapadia, S.B.3    Goldman, J.E.4    Speck, S.H.5    Virgin, H.W.6
  • 84
    • 65549105105 scopus 로고    scopus 로고
    • Analysis of the herpesvirus chemokine-binding glycoprotein G residues essential for chemokine binding and biological activity
    • Van de Walle G.R., Kaufer B.B., Chbab N., Osterrieder N. Analysis of the herpesvirus chemokine-binding glycoprotein G residues essential for chemokine binding and biological activity. J. Biol. Chem. 2009, 284(9):5968-5976.
    • (2009) J. Biol. Chem. , vol.284 , Issue.9 , pp. 5968-5976
    • Van de Walle, G.R.1    Kaufer, B.B.2    Chbab, N.3    Osterrieder, N.4
  • 85
    • 35748953120 scopus 로고    scopus 로고
    • Herpesvirus chemokine-binding glycoprotein G (gG) efficiently inhibits neutrophil chemotaxis in vitro and in vivo
    • Van de Walle G.R., May M.L., Sukhumavasi W., von Einem J., Osterrieder N. Herpesvirus chemokine-binding glycoprotein G (gG) efficiently inhibits neutrophil chemotaxis in vitro and in vivo. J. Immunol. 2007, 179(6):4161-4169.
    • (2007) J. Immunol. , vol.179 , Issue.6 , pp. 4161-4169
    • Van de Walle, G.R.1    May, M.L.2    Sukhumavasi, W.3    von Einem, J.4    Osterrieder, N.5
  • 88
    • 73149110358 scopus 로고    scopus 로고
    • Glycoprotein G from pseudorabies virus binds to chemokines with high affinity and inhibits their function
    • Viejo-Borbolla A., Munoz A., Tabares E., Alcami A. Glycoprotein G from pseudorabies virus binds to chemokines with high affinity and inhibits their function. J. Gen. Virol. 2010, 91(Pt 1):23-31.
    • (2010) J. Gen. Virol. , vol.91 , pp. 23-31
    • Viejo-Borbolla, A.1    Munoz, A.2    Tabares, E.3    Alcami, A.4
  • 89
    • 34247218607 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of equine herpesvirus type 1 (EHV-1) mutants devoid of the viral chemokine-binding glycoprotein G (gG)
    • von Einem J., Smith P.M., Van de Walle G.R., O'Callaghan D.J., Osterrieder N. In vitro and in vivo characterization of equine herpesvirus type 1 (EHV-1) mutants devoid of the viral chemokine-binding glycoprotein G (gG). Virology 2007, 362(1):151-162.
    • (2007) Virology , vol.362 , Issue.1 , pp. 151-162
    • von Einem, J.1    Smith, P.M.2    Van de Walle, G.R.3    O'Callaghan, D.J.4    Osterrieder, N.5
  • 90
    • 9344236534 scopus 로고    scopus 로고
    • Human cytomegalovirus encodes a highly specific RANTES decoy receptor
    • Wang D., Bresnahan W., Shenk T. Human cytomegalovirus encodes a highly specific RANTES decoy receptor. Proc. Natl. Acad. Sci. U.S.A. 2004, 101(47):16642-16647.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.47 , pp. 16642-16647
    • Wang, D.1    Bresnahan, W.2    Shenk, T.3
  • 91
    • 0038446974 scopus 로고    scopus 로고
    • The gammaherpesvirus chemokine binding protein binds to the N terminus of CXCL8
    • Webb L.M., Clark-Lewis I., Alcami A. The gammaherpesvirus chemokine binding protein binds to the N terminus of CXCL8. J. Virol. 2003, 77(15):8588-8592.
    • (2003) J. Virol. , vol.77 , Issue.15 , pp. 8588-8592
    • Webb, L.M.1    Clark-Lewis, I.2    Alcami, A.3
  • 92
    • 2442636810 scopus 로고    scopus 로고
    • The gammaherpesvirus chemokine binding protein can inhibit the interaction of chemokines with glycosaminoglycans
    • Webb L.M., Smith V.P., Alcami A. The gammaherpesvirus chemokine binding protein can inhibit the interaction of chemokines with glycosaminoglycans. FASEB J. 2004, 18(3):571-573.
    • (2004) FASEB J. , vol.18 , Issue.3 , pp. 571-573
    • Webb, L.M.1    Smith, V.P.2    Alcami, A.3
  • 93
    • 0023188784 scopus 로고
    • Rapid identification of nonessential genes of herpes simplex virus type 1 by Tn5 mutagenesis
    • Weber P.C., Levine M., Glorioso J.C. Rapid identification of nonessential genes of herpes simplex virus type 1 by Tn5 mutagenesis. Science 1987, 236(4801):576-579.
    • (1987) Science , vol.236 , Issue.4801 , pp. 576-579
    • Weber, P.C.1    Levine, M.2    Glorioso, J.C.3
  • 94
    • 79960244085 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the CC chemokine binding protein 35K-Fc reveals residues essential for activity and mutations that increase the potency of CC chemokine blockade
    • White G.E., McNeill E., Christou I., Channon K.M., Greaves D.R. Site-directed mutagenesis of the CC chemokine binding protein 35K-Fc reveals residues essential for activity and mutations that increase the potency of CC chemokine blockade. Mol. Pharmacol. 2011, 80(2):328-336.
    • (2011) Mol. Pharmacol. , vol.80 , Issue.2 , pp. 328-336
    • White, G.E.1    McNeill, E.2    Christou, I.3    Channon, K.M.4    Greaves, D.R.5
  • 95
    • 79960963198 scopus 로고    scopus 로고
    • Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor
    • Xue X., Lu Q., Wei H., Wang D., Chen D., He G., Huang L., Wang H., Wang X. Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor. PLoS Pathog. 2011, 7(7):e1002162.
    • (2011) PLoS Pathog. , vol.7 , Issue.7 , pp. e1002162
    • Xue, X.1    Lu, Q.2    Wei, H.3    Wang, D.4    Chen, D.5    He, G.6    Huang, L.7    Wang, H.8    Wang, X.9
  • 97
    • 0034144269 scopus 로고    scopus 로고
    • Chemokines: a new classification system and their role in immunity
    • Zlotnik A., Yoshie O. Chemokines: a new classification system and their role in immunity. Immunity 2000, 12(2):121-127.
    • (2000) Immunity , vol.12 , Issue.2 , pp. 121-127
    • Zlotnik, A.1    Yoshie, O.2
  • 98
    • 34249707951 scopus 로고    scopus 로고
    • The chemokine and chemokine receptor superfamilies and their molecular evolution
    • Zlotnik A., Yoshie O., Nomiyama H. The chemokine and chemokine receptor superfamilies and their molecular evolution. Genome Biol. 2006, 7(12):243.
    • (2006) Genome Biol. , vol.7 , Issue.12 , pp. 243
    • Zlotnik, A.1    Yoshie, O.2    Nomiyama, H.3


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