메뉴 건너뛰기




Volumn 29, Issue 11, 2013, Pages 1407-1417

Conference report: "Functional glycomics in HIV type 1 vaccine design" workshop report, Bethesda, Maryland, April 30-May 1, 2012

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; IMMUNOGLOBULIN G; THREONINE;

EID: 84886666326     PISSN: 08892229     EISSN: 19318405     Source Type: Journal    
DOI: 10.1089/aid.2013.0102     Document Type: Conference Paper
Times cited : (3)

References (96)
  • 1
    • 84874075704 scopus 로고    scopus 로고
    • Committee on Assessing the Importance and Impact of Glycomics and Glycosciences. The National Academies Press, Washington, DC
    • Committee on Assessing the Importance and Impact of Glycomics and Glycosciences: Transforming Glycoscience: A Roadmap for the Future. The National Academies Press, Washington, DC, 2012.
    • (2012) Transforming Glycoscience: A Roadmap for the Future
  • 2
    • 84863860723 scopus 로고    scopus 로고
    • Evolutionary forces shaping the Golgi glycosylation machinery: Why cell surface glycans are universal to living cells
    • Varki A: Evolutionary forces shaping the Golgi glycosylation machinery: Why cell surface glycans are universal to living cells. Cold Spring Harb Perspect Biol 2011; 3(6): a005462.
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , Issue.6
    • Varki, A.1
  • 3
    • 0004106191 scopus 로고    scopus 로고
    • 2nd ed,. 784. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Varki A, et al: Essentials of Glycobiology, 2nd ed, Vol. 784. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 2009.
    • (2009) Essentials of Glycobiology
    • Varki, A.1
  • 4
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal R, et al.: A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 2011; 334(6059): 1097-1103.
    • (2011) Science , vol.334 , Issue.6059 , pp. 1097-1103
    • Pejchal, R.1
  • 5
    • 78650870657 scopus 로고    scopus 로고
    • Shotgun glycomics: A microarray strategy for functional glycomics
    • Song X, et al.: Shotgun glycomics: A microarray strategy for functional glycomics. Nat Methods 2011; 8(1): 85-90.
    • (2011) Nat Methods , vol.8 , Issue.1 , pp. 85-90
    • Song, X.1
  • 6
    • 84867071344 scopus 로고    scopus 로고
    • Platelet biogenesis and functions require correct protein O-glycosylation
    • Wang Y, et al.: Platelet biogenesis and functions require correct protein O-glycosylation. Proc Natl Acad Sci USA 2012; 109(40): 16143-16148.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.40 , pp. 16143-16148
    • Wang, Y.1
  • 7
    • 33846666906 scopus 로고    scopus 로고
    • NMR structural characterization of substrates bound to N-acetylglucosaminyltransferase v
    • Macnaughtan MA, et al.: NMR structural characterization of substrates bound to N-acetylglucosaminyltransferase V. J Mol Biol 2007; 366(4): 1266-1281.
    • (2007) J Mol Biol , vol.366 , Issue.4 , pp. 1266-1281
    • Macnaughtan, M.A.1
  • 8
    • 84869035983 scopus 로고    scopus 로고
    • Antiviral immune responses by human Langerhans cells and dendritic cells in HIV-1 infection
    • Van Den Berg LM and Geijtenbeek TB: Antiviral immune responses by human Langerhans cells and dendritic cells in HIV-1 infection. Adv Exp Med Biol 2013; 762: 45-70.
    • (2013) Adv Exp Med Biol , vol.762 , pp. 45-70
    • Van Den1    Berg, L.M.2    Geijtenbeek, T.B.3
  • 9
    • 84861883015 scopus 로고    scopus 로고
    • NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation
    • Barb AW, et al.: NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation. Biochemistry 2012; 51(22): 4618-4626.
    • (2012) Biochemistry , vol.51 , Issue.22 , pp. 4618-4626
    • Barb, A.W.1
  • 10
    • 70349275888 scopus 로고    scopus 로고
    • Mass spectrometry in the analysis of Nlinked and O-linked glycans
    • North SJ, et al.: Mass spectrometry in the analysis of Nlinked and O-linked glycans. Curr Opin Struct Biol 2009; 19(5): 498-506.
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.5 , pp. 498-506
    • North, S.J.1
  • 11
    • 79961184231 scopus 로고    scopus 로고
    • Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry
    • Go EP, et al.: Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry. J Virol 2011; 85(16): 8270-8284.
    • (2011) J Virol , vol.85 , Issue.16 , pp. 8270-8284
    • Go, E.P.1
  • 12
    • 84874622598 scopus 로고    scopus 로고
    • Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins
    • Go EP, et al.: Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins. J Proteome Res 2013; 12(3): 1223-1234.
    • (2013) J Proteome Res , vol.12 , Issue.3 , pp. 1223-1234
    • Go, E.P.1
  • 13
    • 77954357410 scopus 로고    scopus 로고
    • Correlates of protection induced by vaccination
    • Plotkin SA: Correlates of protection induced by vaccination. Clin Vaccine Immunol 2010; 17(7): 1055-1065.
    • (2010) Clin Vaccine Immunol , vol.17 , Issue.7 , pp. 1055-1065
    • Plotkin, S.A.1
  • 14
    • 79952107221 scopus 로고    scopus 로고
    • Contributions of humoral and cellular immunity to vaccine-induced protection in humans
    • Amanna IJ and Slifka MK: Contributions of humoral and cellular immunity to vaccine-induced protection in humans. Virology 2011; 411(2): 206-215.
    • (2011) Virology , vol.411 , Issue.2 , pp. 206-215
    • Amanna, I.J.1    Slifka, M.K.2
  • 15
    • 0035162494 scopus 로고    scopus 로고
    • Evolutionary and immunological implications of contemporary HIV-1 variation
    • Korber B, et al.: Evolutionary and immunological implications of contemporary HIV-1 variation. Br Med Bull 2001; 58: 19-42.
    • (2001) Br Med Bull , vol.58 , pp. 19-42
    • Korber, B.1
  • 16
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid JF, et al.: Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 2011; 333(6049): 1633-1637.
    • (2011) Science , vol.333 , Issue.6049 , pp. 1633-1637
    • Scheid, J.F.1
  • 17
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu X, et al.: Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 2011; 333(6049): 1593-1602.
    • (2011) Science , vol.333 , Issue.6049 , pp. 1593-1602
    • Wu, X.1
  • 18
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, et al.: Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009; 326(5950): 285-289.
    • (2009) Science , vol.326 , Issue.5950 , pp. 285-289
    • Walker, L.M.1
  • 19
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, et al.: Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011; 477(7365): 466-470.
    • (2011) Nature , vol.477 , Issue.7365 , pp. 466-470
    • Walker, L.M.1
  • 20
    • 77649318846 scopus 로고    scopus 로고
    • Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals
    • Corti D, et al.: Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS One 2010; 5(1): e8805.
    • (2010) PLoS One , vol.5 , Issue.1
    • Corti, D.1
  • 21
    • 80052938385 scopus 로고    scopus 로고
    • Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors
    • Bonsignori M, et al.: Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors. J Virol 2011; 85(19): 9998-10009.
    • (2011) J Virol , vol.85 , Issue.19 , pp. 9998-10009
    • Bonsignori, M.1
  • 22
    • 84861374644 scopus 로고    scopus 로고
    • PGV04, an HIV-1 gp120 CD4 binding site antibody, is broad and potent in neutralization but does not induce conformational changes characteristic of CD4
    • Falkowska E, et al.: PGV04, an HIV-1 gp120 CD4 binding site antibody, is broad and potent in neutralization but does not induce conformational changes characteristic of CD4. J Virol 2012; 86(8): 4394-4403.
    • (2012) J Virol , vol.86 , Issue.8 , pp. 4394-4403
    • Falkowska, E.1
  • 23
    • 84866443327 scopus 로고    scopus 로고
    • Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein
    • Klein F, et al.: Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein. J Exp Med 2012; 209(8): 1469-1479.
    • (2012) J Exp Med , vol.209 , Issue.8 , pp. 1469-1479
    • Klein, F.1
  • 24
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T, et al.: Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010; 329(5993): 811-817.
    • (2010) Science , vol.329 , Issue.5993 , pp. 811-817
    • Zhou, T.1
  • 25
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang J, et al.: Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 2012; 491(7424): 406-412.
    • (2012) Nature , vol.491 , Issue.7424 , pp. 406-412
    • Huang, J.1
  • 26
    • 82955241840 scopus 로고    scopus 로고
    • Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1
    • Kwong PD, Mascola JR, and Nabel GJ: Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1. Cold Spring Harb Perspect Med 2011; 1(1): a007278.
    • (2011) Cold Spring Harb Perspect Med , vol.1 , Issue.1
    • Kwong, P.D.1    Mascola, J.R.2    Nabel, G.J.3
  • 27
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, et al.: Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 2011; 480(7377): 336-343.
    • (2011) Nature , vol.480 , Issue.7377 , pp. 336-343
    • McLellan, J.S.1
  • 28
    • 79952579682 scopus 로고    scopus 로고
    • Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop
    • Moore PL, et al.: Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop. J Virol 2011; 85(7): 3128-3141.
    • (2011) J Virol , vol.85 , Issue.7 , pp. 3128-3141
    • Moore, P.L.1
  • 29
    • 77954100808 scopus 로고    scopus 로고
    • Structure-function relationships of HIV-1 envelope sequence-variable regions refocus vaccine design
    • Zolla-Pazner S and Cardozo T: Structure-function relationships of HIV-1 envelope sequence-variable regions refocus vaccine design. Nat Rev Immunol 2010; 10(7): 527-535.
    • (2010) Nat Rev Immunol , vol.10 , Issue.7 , pp. 527-535
    • Zolla-Pazner, S.1    Cardozo, T.2
  • 30
    • 82555170601 scopus 로고    scopus 로고
    • Human anti-V3 HIV-1 monoclonal antibodies encoded by the VH5-51/VL lambda genes define a conserved antigenic structure
    • Gorny MK, et al.: Human anti-V3 HIV-1 monoclonal antibodies encoded by the VH5-51/VL lambda genes define a conserved antigenic structure. PLoS One 2011; 6(12): e27780.
    • (2011) PLoS One , vol.6 , Issue.12
    • Gorny, M.K.1
  • 31
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition
    • Calarese DA, et al.: Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 2003; 300(5628): 2065-2071.
    • (2003) Science , vol.300 , Issue.5628 , pp. 2065-2071
    • Calarese, D.A.1
  • 32
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: Identification structures and B cell ontogenies
    • Kwong PD and Mascola JR: Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies. Immunity 2012; 37(3): 412-425.
    • (2012) Immunity , vol.37 , Issue.3 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 33
    • 84869155712 scopus 로고    scopus 로고
    • Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape
    • Moore PL, et al.: Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape. Nat Med 2012; 18(11): 1688-1692.
    • (2012) Nat Med , vol.18 , Issue.11 , pp. 1688-1692
    • Moore, P.L.1
  • 34
    • 84866061123 scopus 로고    scopus 로고
    • Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer
    • Mao Y, et al.: Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer. Nat Struct Mol Biol 2012; 19(9): 893-899.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.9 , pp. 893-899
    • Mao, Y.1
  • 35
    • 77954982131 scopus 로고    scopus 로고
    • Crystal structure of PG16 and chimeric dissection with somatically related PG9: Structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1
    • Pancera M, et al.: Crystal structure of PG16 and chimeric dissection with somatically related PG9: Structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1. J Virol 2010; 84(16): 8098-8110.
    • (2010) J Virol , vol.84 , Issue.16 , pp. 8098-8110
    • Pancera, M.1
  • 37
    • 84880149399 scopus 로고    scopus 로고
    • Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16
    • Pancera M, et al.: Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16. Nat Struct Mol Biol 2013; 20(7): 804-813.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.7 , pp. 804-813
    • Pancera, M.1
  • 38
    • 84876272159 scopus 로고    scopus 로고
    • Mining the antibodyome for HIV-1-neutralizing antibodies with next-generation sequencing and phylogenetic pairing of heavy/light chains
    • Zhu J, et al.: Mining the antibodyome for HIV-1-neutralizing antibodies with next-generation sequencing and phylogenetic pairing of heavy/light chains. Proc Natl Acad Sci USA 2013; 110(16): 6470-6475.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.16 , pp. 6470-6475
    • Zhu, J.1
  • 39
    • 84865191430 scopus 로고    scopus 로고
    • Glycoform and net charge heterogeneity in gp120 immunogens used in HIV vaccine trials
    • Yu B, et al.: Glycoform and net charge heterogeneity in gp120 immunogens used in HIV vaccine trials. PLoS One 2012; 7(8): e43903.
    • (2012) PLoS One , vol.7 , Issue.8
    • Yu, B.1
  • 40
    • 0026346608 scopus 로고
    • Structure and function in recombinant HIV- 1 gp120 and speculation about the disulfide bonding in the gp120 homologs of HIV-2 and SIV
    • Gregory T, et al.: Structure and function in recombinant HIV- 1 gp120 and speculation about the disulfide bonding in the gp120 homologs of HIV-2 and SIV. Adv Exp Med Biol 1991; 303: 1-14.
    • (1991) Adv Exp Med Biol , vol.303 , pp. 1-14
    • Gregory, T.1
  • 41
    • 77956385205 scopus 로고    scopus 로고
    • Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens
    • Doores KJ, et al.: Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens. Proc Natl Acad Sci USA 2010; 107(31): 13800-13805.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.31 , pp. 13800-13805
    • Doores, K.J.1
  • 42
    • 80051677678 scopus 로고    scopus 로고
    • The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade
    • Bonomelli C, et al.: The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLoS One 2011; 6(8): e23521.
    • (2011) PLoS One , vol.6 , Issue.8
    • Bonomelli, C.1
  • 43
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • Crooks ET, et al.: Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. J Virol 2011; 85(12): 5825-5839.
    • (2011) J Virol , vol.85 , Issue.12 , pp. 5825-5839
    • Crooks, E.T.1
  • 44
    • 22944491144 scopus 로고    scopus 로고
    • Glycomics and mass spectrometry
    • Morelle W and Michalski JC: Glycomics and mass spectrometry. Curr Pharm Des 2005; 11(20): 2615-2645.
    • (2005) Curr Pharm des , vol.11 , Issue.20 , pp. 2615-2645
    • Morelle, W.1    Michalski, J.C.2
  • 45
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of posttranslational modifications
    • Mann M and Jensen ON: Proteomic analysis of posttranslational modifications. Nat Biotechnol 2003; 21(3): 255-261.
    • (2003) Nat Biotechnol , vol.21 , Issue.3 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 46
    • 9044241681 scopus 로고    scopus 로고
    • Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
    • Trkola A, et al.: Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J Virol 1996; 70(2): 1100-1108.
    • (1996) J Virol , vol.70 , Issue.2 , pp. 1100-1108
    • Trkola, A.1
  • 47
    • 26444450696 scopus 로고    scopus 로고
    • Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12
    • Calarese DA, et al.: Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12. Proc Natl Acad Sci USA 2005; 102(38): 13372-13377.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.38 , pp. 13372-13377
    • Calarese, D.A.1
  • 48
    • 45749138808 scopus 로고    scopus 로고
    • A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120
    • Astronomo RD, et al.: A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120. J Virol 2008; 82(13): 6359-6368.
    • (2008) J Virol , vol.82 , Issue.13 , pp. 6359-6368
    • Astronomo, R.D.1
  • 49
    • 41649109652 scopus 로고    scopus 로고
    • Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN
    • Wang SK, et al.: Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN. Proc Natl Acad Sci USA 2008; 105(10): 3690-3695.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.10 , pp. 3690-3695
    • Wang, S.K.1
  • 50
    • 65349132918 scopus 로고    scopus 로고
    • A yeast glycoprotein shows high-affinity binding to the broadly neutralizing human immunodeficiency virus antibody 2G12 and inhibits gp120 interactions with 2G12 and DC-SIGN
    • Luallen RJ, et al.: A yeast glycoprotein shows high-affinity binding to the broadly neutralizing human immunodeficiency virus antibody 2G12 and inhibits gp120 interactions with 2G12 and DC-SIGN. J Virol 2009; 83(10): 4861-4870.
    • (2009) J Virol , vol.83 , Issue.10 , pp. 4861-4870
    • Luallen, R.J.1
  • 51
    • 77949907643 scopus 로고    scopus 로고
    • Antibodies against Manalpha1 2- Manalpha1 2-Man oligosaccharide structures recognize envelope glycoproteins from HIV-1 and SIV strains
    • Luallen RJ, et al.: Antibodies against Manalpha1, 2- Manalpha1, 2-Man oligosaccharide structures recognize envelope glycoproteins from HIV-1 and SIV strains. Glycobiology 2010; 20(3): 280-286.
    • (2010) Glycobiology , vol.20 , Issue.3 , pp. 280-286
    • Luallen, R.J.1
  • 52
    • 77951073160 scopus 로고    scopus 로고
    • Defining criteria for oligomannose immunogens for HIV using icosahedral virus capsid scaffolds
    • Astronomo RD, et al.: Defining criteria for oligomannose immunogens for HIV using icosahedral virus capsid scaffolds. Chem Biol 2010; 17(4): 357-370.
    • (2010) Chem Biol , vol.17 , Issue.4 , pp. 357-370
    • Astronomo, R.D.1
  • 53
    • 77956366187 scopus 로고    scopus 로고
    • Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody 2G12 induces enhanced antibody responses to self oligomannose glycans
    • Dunlop DC, et al.: Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody, 2G12, induces enhanced antibody responses to self oligomannose glycans. Glycobiology 2010; 20(7): 812-823.
    • (2010) Glycobiology , vol.20 , Issue.7 , pp. 812-823
    • Dunlop, D.C.1
  • 54
    • 77957201600 scopus 로고    scopus 로고
    • Very few substitutions in a germ line antibody are required to initiate significant domain exchange
    • Huber M, et al.: Very few substitutions in a germ line antibody are required to initiate significant domain exchange. J Virol 2010; 84(20): 10700-10707.
    • (2010) J Virol , vol.84 , Issue.20 , pp. 10700-10707
    • Huber, M.1
  • 55
    • 77957189612 scopus 로고    scopus 로고
    • Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged
    • Doores KJ, et al.: Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged. J Virol 2010; 84(20): 10690-10699.
    • (2010) J Virol , vol.84 , Issue.20 , pp. 10690-10699
    • Doores, K.J.1
  • 56
    • 78049424266 scopus 로고    scopus 로고
    • Computational glycoscience: Characterizing the spatial and temporal properties of glycans and glycan-protein complexes
    • Woods RJ and Tessier MB: Computational glycoscience: Characterizing the spatial and temporal properties of glycans and glycan-protein complexes. Curr Opin Struct Biol 2010; 20(5): 575-583.
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.5 , pp. 575-583
    • Woods, R.J.1    Tessier, M.B.2
  • 57
    • 68249116079 scopus 로고    scopus 로고
    • From carbohydrate leads to glycomimetic drugs
    • Ernst B and Magnani JL: From carbohydrate leads to glycomimetic drugs. Nat Rev Drug Discov 2009; 8(8): 661-677.
    • (2009) Nat Rev Drug Discov , vol.8 , Issue.8 , pp. 661-677
    • Ernst, B.1    Magnani, J.L.2
  • 58
    • 37849026069 scopus 로고    scopus 로고
    • Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses
    • Li Y, et al.: Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses. J Virol 2008; 82(2): 638-651.
    • (2008) J Virol , vol.82 , Issue.2 , pp. 638-651
    • Li, Y.1
  • 59
    • 78751608551 scopus 로고    scopus 로고
    • The role of differential IgG glycosylation in the interaction of antibodies with FcgammaRs in vivo
    • Anthony RM and Nimmerjahn F: The role of differential IgG glycosylation in the interaction of antibodies with FcgammaRs in vivo. Curr Opin Organ Transplant 2011; 16(1): 7-14.
    • (2011) Curr Opin Organ Transplant , vol.16 , Issue.1 , pp. 7-14
    • Anthony, R.M.1    Nimmerjahn, F.2
  • 60
    • 80053578013 scopus 로고    scopus 로고
    • Impact of differential glycosylation on IgG activity
    • Lux A and Nimmerjahn F: Impact of differential glycosylation on IgG activity. Adv Exp Med Biol 2011; 780: 113-124.
    • (2011) Adv Exp Med Biol , vol.780 , pp. 113-124
    • Lux, A.1    Nimmerjahn, F.2
  • 61
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields RL, et al.: Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem 2002; 277(30): 26733-26740.
    • (2002) J Biol Chem , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1
  • 62
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa T, et al.: The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J Biol Chem 2003; 278(5): 3466-3473.
    • (2003) J Biol Chem , vol.278 , Issue.5 , pp. 3466-3473
    • Shinkawa, T.1
  • 63
    • 12144289636 scopus 로고    scopus 로고
    • Defucosylated chimeric anti-CC chemokine receptor 4 IgG1 with enhanced antibody-dependent cellular cytotoxicity shows potent therapeutic activity to T-cell leukemia and lymphoma
    • Niwa R, et al.: Defucosylated chimeric anti-CC chemokine receptor 4 IgG1 with enhanced antibody-dependent cellular cytotoxicity shows potent therapeutic activity to T-cell leukemia and lymphoma. Cancer Res 2004; 64(6): 2127-2133.
    • (2004) Cancer Res , vol.64 , Issue.6 , pp. 2127-2133
    • Niwa, R.1
  • 64
    • 28444495153 scopus 로고    scopus 로고
    • IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides
    • Niwa R, et al.: IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides. J Immunol Methods 2005; 306(1-2): 151-160.
    • (2005) J Immunol Methods , vol.306 , Issue.1-2 , pp. 151-160
    • Niwa, R.1
  • 65
    • 84863579036 scopus 로고    scopus 로고
    • A nonfucosylated variant of the anti-HIV-1 monoclonal antibody b12 has enhanced FcgammaRIIIamediated antiviral activity in vitro but does not improve protection against mucosal SHIV challenge in macaques
    • Moldt B, et al.: A nonfucosylated variant of the anti-HIV-1 monoclonal antibody b12 has enhanced FcgammaRIIIamediated antiviral activity in vitro but does not improve protection against mucosal SHIV challenge in macaques. J Virol 2012; 86(11): 6189-6196.
    • (2012) J Virol , vol.86 , Issue.11 , pp. 6189-6196
    • Moldt, B.1
  • 66
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y, Nimmerjahn F, and Ravetch JV: Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006; 313(5787): 670-673.
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 67
    • 34248168722 scopus 로고    scopus 로고
    • Recombinant gp120 vaccine-induced antibodies inhibit clinical strains of HIV-1 in the presence of Fc receptor-bearing effector cells and correlate inversely with HIV infection rate
    • Forthal DN, et al.: Recombinant gp120 vaccine-induced antibodies inhibit clinical strains of HIV-1 in the presence of Fc receptor-bearing effector cells and correlate inversely with HIV infection rate. J Immunol 2007; 178(10): 6596-6603.
    • (2007) J Immunol , vol.178 , Issue.10 , pp. 6596-6603
    • Forthal, D.N.1
  • 68
    • 69549103041 scopus 로고    scopus 로고
    • Fc receptor-mediated antiviral antibodies
    • Forthal DN and Moog C: Fc receptor-mediated antiviral antibodies. Curr Opin HIV AIDS 2009; 4(5): 388-393.
    • (2009) Curr Opin HIV AIDS , vol.4 , Issue.5 , pp. 388-393
    • Forthal, D.N.1    Moog, C.2
  • 69
    • 81155162632 scopus 로고    scopus 로고
    • IgG2 inhibits HIV-1 internalization by monocytes and IgG subclass binding is affected by gp120 glycosylation
    • Forthal DN, et al.: IgG2 inhibits HIV-1 internalization by monocytes, and IgG subclass binding is affected by gp120 glycosylation. AIDS 2011; 25(17): 2099-2104.
    • (2011) AIDS , vol.25 , Issue.17 , pp. 2099-2104
    • Forthal, D.N.1
  • 70
    • 84855970041 scopus 로고    scopus 로고
    • Emerging concepts on the role of innate immunity in the prevention and control of HIV infection
    • Ackerman ME, Dugast AS, and Alter G: Emerging concepts on the role of innate immunity in the prevention and control of HIV infection. Annu Rev Med 2012; 63: 113-130.
    • (2012) Annu Rev Med , vol.63 , pp. 113-130
    • Ackerman, M.E.1    Dugast, A.S.2    Alter, G.3
  • 71
    • 57449101496 scopus 로고    scopus 로고
    • NK cells in HIV-1 infection: Evidence for their role in the control of HIV-1 infection
    • Alter G and Altfeld M: NK cells in HIV-1 infection: Evidence for their role in the control of HIV-1 infection. J Intern Med 2009; 265(1): 29-42.
    • (2009) J Intern Med , vol.265 , Issue.1 , pp. 29-42
    • Alter, G.1    Altfeld, M.2
  • 72
    • 84871434642 scopus 로고    scopus 로고
    • Antibody-dependent cellular cytotoxicity and NK cell-driven immune escape in HIV infection: Implications for HIV vaccine development
    • Isitman G, Stratov I, and Kent SJ: Antibody-dependent cellular cytotoxicity and NK cell-driven immune escape in HIV infection: Implications for HIV vaccine development. Adv Virol 2012; 2012: 637208.
    • (2012) Adv Virol , vol.2012 , pp. 637208
    • Isitman, G.1    Stratov, I.2    Kent, S.J.3
  • 73
    • 84877152391 scopus 로고    scopus 로고
    • Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity
    • Ackerman ME, et al.: Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity. J Clin Invest 2013; 123(5): 2183-2192.
    • (2013) J Clin Invest , vol.123 , Issue.5 , pp. 2183-2192
    • Ackerman, M.E.1
  • 74
    • 12144289425 scopus 로고    scopus 로고
    • Envelope-constrained neutralizationsensitive HIV-1 after heterosexual transmission
    • Derdeyn CA, et al.: Envelope-constrained neutralizationsensitive HIV-1 after heterosexual transmission. Science 2004; 303(5666): 2019-2022.
    • (2004) Science , vol.303 , Issue.5666 , pp. 2019-2022
    • Derdeyn, C.A.1
  • 75
    • 23244453195 scopus 로고    scopus 로고
    • Evidence for frequent reinfection with human immunodeficiency virus type 1 of a different subtype
    • Chohan B, et al.: Evidence for frequent reinfection with human immunodeficiency virus type 1 of a different subtype. J Virol 2005; 79(16): 10701-10708.
    • (2005) J Virol , vol.79 , Issue.16 , pp. 10701-10708
    • Chohan, B.1
  • 76
    • 44649102135 scopus 로고    scopus 로고
    • Identification and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection
    • Keele BF, et al.: Identification and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection. Proc Natl Acad Sci USA 2008; 105(21): 7552-7557.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.21 , pp. 7552-7557
    • Keele, B.F.1
  • 77
    • 9744280420 scopus 로고    scopus 로고
    • Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin
    • Zhang M, et al.: Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin. Glycobiology 2004; 14(12): 1229-1246.
    • (2004) Glycobiology , vol.14 , Issue.12 , pp. 1229-1246
    • Zhang, M.1
  • 78
    • 29444442970 scopus 로고    scopus 로고
    • Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection
    • Frost SD, et al.: Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection. Proc Natl Acad Sci USA 2005; 102(51): 18514-18519.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.51 , pp. 18514-18519
    • Frost, S.D.1
  • 79
    • 34648816125 scopus 로고    scopus 로고
    • N-linked glycan modifications in gp120 of human immunodeficiency virus type 1 subtype C render partial sensitivity to 2G12 antibody neutralization
    • Gray ES, et al.: N-linked glycan modifications in gp120 of human immunodeficiency virus type 1 subtype C render partial sensitivity to 2G12 antibody neutralization. J Virol 2007; 81(19): 10769-10776.
    • (2007) J Virol , vol.81 , Issue.19 , pp. 10769-10776
    • Gray, E.S.1
  • 80
    • 80051832232 scopus 로고    scopus 로고
    • A signature in HIV-1 envelope leader peptide associated with transition from acute to chronic infection impacts envelope processing and infectivity
    • Asmal M, et al.: A signature in HIV-1 envelope leader peptide associated with transition from acute to chronic infection impacts envelope processing and infectivity. PLoS One 2011; 6(8): e23673.
    • (2011) PLoS One , vol.6 , Issue.8
    • Asmal, M.1
  • 81
    • 18744394633 scopus 로고    scopus 로고
    • The C108g epitope in the V2 domain of gp120 functions as a potent neutralization target when introduced into envelope proteins derived from human immunodeficiency virus type 1 primary isolates
    • Pinter A, et al.: The C108g epitope in the V2 domain of gp120 functions as a potent neutralization target when introduced into envelope proteins derived from human immunodeficiency virus type 1 primary isolates. J Virol 2005; 79(11): 6909-6917.
    • (2005) J Virol , vol.79 , Issue.11 , pp. 6909-6917
    • Pinter, A.1
  • 82
    • 80054988972 scopus 로고    scopus 로고
    • Characterization of structural features and diversity of variable-region determinants of related quaternary epitopes recognized by human and rhesus macaque monoclonal antibodies possessing unusually potent neutralizing activities
    • Krachmarov C, et al.: Characterization of structural features and diversity of variable-region determinants of related quaternary epitopes recognized by human and rhesus macaque monoclonal antibodies possessing unusually potent neutralizing activities. J Virol 2011; 85(20): 10730-10740.
    • (2011) J Virol , vol.85 , Issue.20 , pp. 10730-10740
    • Krachmarov, C.1
  • 83
    • 84861324362 scopus 로고    scopus 로고
    • HIV-1 virus-like particles bearing pure env trimers expose neutralizing epitopes but occlude nonneutralizing epitopes
    • Tong T, et al.: HIV-1 virus-like particles bearing pure env trimers expose neutralizing epitopes but occlude nonneutralizing epitopes. J Virol 2012; 86(7): 3574-3587.
    • (2012) J Virol , vol.86 , Issue.7 , pp. 3574-3587
    • Tong, T.1
  • 84
    • 84863220988 scopus 로고    scopus 로고
    • Infection inflammation and host carbohydrates: A glyco-evasion hypothesis
    • Kreisman LS and Cobb BA: Infection, inflammation and host carbohydrates: A glyco-evasion hypothesis. Glycobiology 2012; 22(8): 1019-1030.
    • (2012) Glycobiology , vol.22 , Issue.8 , pp. 1019-1030
    • Kreisman, L.S.1    Cobb, B.A.2
  • 85
    • 44049095632 scopus 로고    scopus 로고
    • Protein-glycan interactions in the control of innate and adaptive immune responses
    • van Kooyk Y and Rabinovich GA: Protein-glycan interactions in the control of innate and adaptive immune responses. Nat Immunol 2008; 9(6): 593-601.
    • (2008) Nat Immunol , vol.9 , Issue.6 , pp. 593-601
    • Van Kooyk, Y.1    Rabinovich, G.A.2
  • 86
    • 75749084864 scopus 로고    scopus 로고
    • Regulation of intracellular signaling by extracellular glycan remodeling
    • Parker RB and Kohler JJ: Regulation of intracellular signaling by extracellular glycan remodeling. ACS Chem Biol 2010; 5(1): 35-46.
    • (2010) ACS Chem Biol , vol.5 , Issue.1 , pp. 35-46
    • Parker, R.B.1    Kohler, J.J.2
  • 88
    • 84859877617 scopus 로고    scopus 로고
    • Changes in antigen-specific IgG1 Fc Nglycosylation upon influenza and tetanus vaccination
    • Selman MH, et al.: Changes in antigen-specific IgG1 Fc Nglycosylation upon influenza and tetanus vaccination. Mol Cell Proteomics 2012; 11(4): M111 014563.
    • (2012) Mol Cell Proteomics , vol.11 , Issue.4
    • Selman, M.H.1
  • 89
    • 11844287660 scopus 로고    scopus 로고
    • Repeated immunization induces the increase in fucose content on antigen-specific IgG N-linked oligosaccharides
    • Guo N, et al.: Repeated immunization induces the increase in fucose content on antigen-specific IgG N-linked oligosaccharides. Clin Biochem 2005; 38(2): 149-153.
    • (2005) Clin Biochem , vol.38 , Issue.2 , pp. 149-153
    • Guo, N.1
  • 90
    • 0032462161 scopus 로고    scopus 로고
    • Changes in the galactose content of IgG during humoral immune responses
    • Lastra GC, et al.: Changes in the galactose content of IgG during humoral immune responses. Autoimmunity 1998; 28(1): 25-30.
    • (1998) Autoimmunity , vol.28 , Issue.1 , pp. 25-30
    • Lastra, G.C.1
  • 91
    • 78650656127 scopus 로고    scopus 로고
    • Fc-glycosylation influences Fcgamma receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12
    • Forthal DN, et al.: Fc-glycosylation influences Fcgamma receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12. J Immunol 2010; 185(11): 6876-6882.
    • (2010) J Immunol , vol.185 , Issue.11 , pp. 6876-6882
    • Forthal, D.N.1
  • 92
    • 0036852231 scopus 로고    scopus 로고
    • Viral interference with antigen presentation
    • Yewdell JW and Hill AB: Viral interference with antigen presentation. Nat Immunol 2002; 3(11): 1019-1025.
    • (2002) Nat Immunol , vol.3 , Issue.11 , pp. 1019-1025
    • Yewdell, J.W.1    Hill, A.B.2
  • 93
    • 26244439658 scopus 로고    scopus 로고
    • Viral modulation of antigen presentation: Manipulation of cellular targets in the ER and beyond
    • Lilley BN and Ploegh HL: Viral modulation of antigen presentation: Manipulation of cellular targets in the ER and beyond. Immunol Rev 2005; 207: 126-144.
    • (2005) Immunol Rev , vol.207 , pp. 126-144
    • Lilley, B.N.1    Ploegh, H.L.2
  • 94
    • 67649842408 scopus 로고    scopus 로고
    • MHC class i antigen presentation: Learning from viral evasion strategies
    • Hansen TH and Bouvier M: MHC class I antigen presentation: Learning from viral evasion strategies. Nat Rev Immunol 2009: 9(7): 503-513.
    • (2009) Nat Rev Immunol , vol.9 , Issue.7 , pp. 503-513
    • Hansen, T.H.1    Bouvier, M.2
  • 95
    • 70449534963 scopus 로고    scopus 로고
    • Proximal glycans outside of the epitopes regulate the presentation of HIV-1 envelope gp120 helper epitopes
    • Li H, et al.: Proximal glycans outside of the epitopes regulate the presentation of HIV-1 envelope gp120 helper epitopes. J Immunol 2009; 182(10): 6369-6378.
    • (2009) J Immunol , vol.182 , Issue.10 , pp. 6369-6378
    • Li, H.1
  • 96
    • 84865533313 scopus 로고    scopus 로고
    • Host glycans and antigen presentation
    • Ryan SO and Cobb BA: Host glycans and antigen presentation. Microbes Infect 2012; 14(11): 894-903. Diseases
    • (2012) Microbes Infect , vol.14 , Issue.11 , pp. 894-903
    • Ryan, S.O.1    Cobb, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.