메뉴 건너뛰기




Volumn 24, Issue 8, 2016, Pages 1346-1357

Somatic Hypermutation-Induced Changes in the Structure and Dynamics of HIV-1 Broadly Neutralizing Antibodies

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; GLYCOPROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; IMMUNOGLOBULIN F(AB) FRAGMENT; NEUTRALIZING ANTIBODY; VIRUS ANTIBODY;

EID: 84979741951     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2016.06.012     Document Type: Article
Times cited : (29)

References (51)
  • 2
    • 84864540090 scopus 로고    scopus 로고
    • Protein dynamics and the diversity of an antibody response
    • Adhikary, R., Yu, W., Oda, M., Zimmermann, J., Romesberg, F.E., Protein dynamics and the diversity of an antibody response. J. Biol. Chem. 287 (2012), 27139–27147.
    • (2012) J. Biol. Chem. , vol.287 , pp. 27139-27147
    • Adhikary, R.1    Yu, W.2    Oda, M.3    Zimmermann, J.4    Romesberg, F.E.5
  • 3
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J.S., Mayne, L., Englander, S.W., Primary structure effects on peptide group hydrogen exchange. Proteins 17 (1993), 75–86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 6
    • 70349613463 scopus 로고    scopus 로고
    • Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS
    • Engen, J.R., Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS. Anal. Chem. 81 (2009), 7870–7875.
    • (2009) Anal. Chem. , vol.81 , pp. 7870-7875
    • Engen, J.R.1
  • 7
    • 84904361849 scopus 로고    scopus 로고
    • Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains
    • Fera, D., Schmidt, A.G., Haynes, B.F., Gao, F., Liao, H.-X., Kepler, T.B., Harrison, S.C., Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains. Proc. Natl. Acad. Sci. USA 111 (2014), 10275–10280.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 10275-10280
    • Fera, D.1    Schmidt, A.G.2    Haynes, B.F.3    Gao, F.4    Liao, H.-X.5    Kepler, T.B.6    Harrison, S.C.7
  • 9
    • 0027943261 scopus 로고
    • Conformational isomerism and the diversity of antibodies
    • Foote, J., Milstein, C., Conformational isomerism and the diversity of antibodies. Proc. Natl. Acad. Sci. USA 91 (1994), 10370–10374.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10370-10374
    • Foote, J.1    Milstein, C.2
  • 11
    • 84893352067 scopus 로고    scopus 로고
    • Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline
    • Georgiev, I.S., Rudicell, R.S., Saunders, K.O., Shi, W., Kirys, T., McKee, K., O'Dell, S., Chuang, G.-Y., Yang, Z.-Y., Ofek, G., et al. Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline. J. Immunol. 192 (2014), 1100–1106.
    • (2014) J. Immunol. , vol.192 , pp. 1100-1106
    • Georgiev, I.S.1    Rudicell, R.S.2    Saunders, K.O.3    Shi, W.4    Kirys, T.5    McKee, K.6    O'Dell, S.7    Chuang, G.-Y.8    Yang, Z.-Y.9    Ofek, G.10
  • 13
    • 84865066445 scopus 로고    scopus 로고
    • Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120
    • Guttman, M., Kahn, M., Garcia, N.K., Hu, S.-L., Lee, K.K., Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120. J. Virol. 86 (2012), 8750–8764.
    • (2012) J. Virol. , vol.86 , pp. 8750-8764
    • Guttman, M.1    Kahn, M.2    Garcia, N.K.3    Hu, S.-L.4    Lee, K.K.5
  • 14
    • 84890532160 scopus 로고    scopus 로고
    • Analysis of overlapped and noisy hydrogen/deuterium exchange mass spectra
    • Guttman, M., Weis, D.D., Engen, J.R., Lee, K.K., Analysis of overlapped and noisy hydrogen/deuterium exchange mass spectra. J. Am. Soc. Mass Spectrom. 24 (2013), 1906–1912.
    • (2013) J. Am. Soc. Mass Spectrom. , vol.24 , pp. 1906-1912
    • Guttman, M.1    Weis, D.D.2    Engen, J.R.3    Lee, K.K.4
  • 15
    • 77951882041 scopus 로고    scopus 로고
    • Toward an antibody-based HIV-1 vaccine
    • Hoxie, J.A., Toward an antibody-based HIV-1 vaccine. Annu. Rev. Med. 61 (2010), 135–152.
    • (2010) Annu. Rev. Med. , vol.61 , pp. 135-152
    • Hoxie, J.A.1
  • 16
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James, L.C., Roversi, P., Tawfik, D.S., Antibody multispecificity mediated by conformational diversity. Science 299 (2003), 1362–1367.
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 18
    • 1642321774 scopus 로고    scopus 로고
    • Protein dynamics and the immunological evolution of molecular recognition
    • Jimenez, R., Salazar, G., Yin, J., Joo, T., Romesberg, F.E., Protein dynamics and the immunological evolution of molecular recognition. Proc. Natl. Acad. Sci. USA 101 (2004), 3803–3808.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3803-3808
    • Jimenez, R.1    Salazar, G.2    Yin, J.3    Joo, T.4    Romesberg, F.E.5
  • 20
    • 84875759341 scopus 로고    scopus 로고
    • Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization
    • Klein, F., Diskin, R., Scheid, J.F., Gaebler, C., Mouquet, H., Georgiev, I.S., Pancera, M., Zhou, T., Incesu, R.-B., Fu, B.Z., et al. Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell 153 (2013), 126–138.
    • (2013) Cell , vol.153 , pp. 126-138
    • Klein, F.1    Diskin, R.2    Scheid, J.F.3    Gaebler, C.4    Mouquet, H.5    Georgiev, I.S.6    Pancera, M.7    Zhou, T.8    Incesu, R.-B.9    Fu, B.Z.10
  • 22
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies
    • Kwong, P.D., Mascola, J.R., Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies. Immunity 37 (2012), 412–425.
    • (2012) Immunity , vol.37 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 23
    • 0038103565 scopus 로고    scopus 로고
    • X-ray snapshots of the maturation of an antibody response to a protein antigen
    • Li, Y., Li, H., Yang, F., Smith-Gill, S.J., Mariuzza, R.A., X-ray snapshots of the maturation of an antibody response to a protein antigen. Nat. Struct. Biol. 10 (2003), 482–488.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 482-488
    • Li, Y.1    Li, H.2    Yang, F.3    Smith-Gill, S.J.4    Mariuzza, R.A.5
  • 24
    • 0041333138 scopus 로고    scopus 로고
    • Enhancing protein crystallization through precipitant synergy
    • Majeed, S., Ofek, G., Belachew, A., Huang, C.-C., Zhou, T., Kwong, P.D., Enhancing protein crystallization through precipitant synergy. Structure 11 (2003), 1061–1070.
    • (2003) Structure , vol.11 , pp. 1061-1070
    • Majeed, S.1    Ofek, G.2    Belachew, A.3    Huang, C.-C.4    Zhou, T.5    Kwong, P.D.6
  • 25
    • 0033634681 scopus 로고    scopus 로고
    • Maturation of an antibody response is governed by modulations in flexibility of the antigen-combining site
    • Manivel, V., Sahoo, N.C., Salunke, D.M., Rao, K.V., Maturation of an antibody response is governed by modulations in flexibility of the antigen-combining site. Immunity 13 (2000), 611–620.
    • (2000) Immunity , vol.13 , pp. 611-620
    • Manivel, V.1    Sahoo, N.C.2    Salunke, D.M.3    Rao, K.V.4
  • 26
    • 0037100251 scopus 로고    scopus 로고
    • The primary antibody repertoire represents a linked network of degenerate antigen specificities
    • Manivel, V., Bayiroglu, F., Siddiqui, Z., Salunke, D.M., Rao, K.V.S., The primary antibody repertoire represents a linked network of degenerate antigen specificities. J. Immunol. 169 (2002), 888–897.
    • (2002) J. Immunol. , vol.169 , pp. 888-897
    • Manivel, V.1    Bayiroglu, F.2    Siddiqui, Z.3    Salunke, D.M.4    Rao, K.V.S.5
  • 27
    • 77952311370 scopus 로고    scopus 로고
    • The role of antibodies in HIV Vaccines
    • Mascola, J.R., Montefiori, D.C., The role of antibodies in HIV Vaccines. Annu. Rev. Immunol. 28 (2010), 413–444.
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 413-444
    • Mascola, J.R.1    Montefiori, D.C.2
  • 30
    • 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, P.L., Gray, E.S., Sheward, D., Madiga, M., Ranchobe, N., Lai, Z., Honnen, W.J., Nonyane, M., Tumba, N., Hermanus, T., 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. 85 (2011), 3128–3141.
    • (2011) J. Virol. , vol.85 , pp. 3128-3141
    • Moore, P.L.1    Gray, E.S.2    Sheward, D.3    Madiga, M.4    Ranchobe, N.5    Lai, Z.6    Honnen, W.J.7    Nonyane, M.8    Tumba, N.9    Hermanus, T.10
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • [20] Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., Minor, W., [20] Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997), 307–326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 84884678235 scopus 로고    scopus 로고
    • A Next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies
    • Sanders, R.W., Derking, R., Cupo, A., Julien, J.-P., Yasmeen, A., de Val, N., Kim, H.J., Blattner, C., de la Peña, A.T., et al. A Next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog., 9, 2013, e1003618.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003618
    • Sanders, R.W.1    Derking, R.2    Cupo, A.3    Julien, J.-P.4    Yasmeen, A.5    de Val, N.6    Kim, H.J.7    Blattner, C.8    de la Peña, A.T.9
  • 38
    • 53549108576 scopus 로고    scopus 로고
    • Germline V-genes sculpt the binding site of a family of antibodies neutralizing human cytomegalovirus
    • Thomson, C.A., Bryson, S., McLean, G.R., Creagh, A.L., Pai, E.F., Schrader, J.W., Germline V-genes sculpt the binding site of a family of antibodies neutralizing human cytomegalovirus. EMBO J. 27 (2008), 2592–2602.
    • (2008) EMBO J. , vol.27 , pp. 2592-2602
    • Thomson, C.A.1    Bryson, S.2    McLean, G.R.3    Creagh, A.L.4    Pai, E.F.5    Schrader, J.W.6
  • 40
    • 84971224753 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry of related proteins with divergent sequences: a comparative study of HIV-1 Nef allelic variants
    • Wales, T.E., Poe, J.A., Emert-Sedlak, L., Morgan, C.R., Smithgall, T.E., Engen, J.R., Hydrogen exchange mass spectrometry of related proteins with divergent sequences: a comparative study of HIV-1 Nef allelic variants. J. Am. Soc. Mass Spectrom. 27 (2016), 1048–1061.
    • (2016) J. Am. Soc. Mass Spectrom. , vol.27 , pp. 1048-1061
    • Wales, T.E.1    Poe, J.A.2    Emert-Sedlak, L.3    Morgan, C.R.4    Smithgall, T.E.5    Engen, J.R.6
  • 42
    • 0030821164 scopus 로고    scopus 로고
    • Structural insights into the evolution of an antibody combining site
    • Wedemayer, G.J., Patten, P.A., Wang, L.H., Schultz, P.G., Stevens, R.C., Structural insights into the evolution of an antibody combining site. Science 276 (1997), 1665–1669.
    • (1997) Science , vol.276 , pp. 1665-1669
    • Wedemayer, G.J.1    Patten, P.A.2    Wang, L.H.3    Schultz, P.G.4    Stevens, R.C.5
  • 43
    • 84859455527 scopus 로고    scopus 로고
    • Structure-based model of allostery predicts coupling between distant sites
    • Weinkam, P., Pons, J., Sali, A., Structure-based model of allostery predicts coupling between distant sites. Proc. Natl. Acad. Sci. USA 109 (2012), 4875–4880.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 4875-4880
    • Weinkam, P.1    Pons, J.2    Sali, A.3
  • 44
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing of hydrogen exchange mass spectra using HX-Express
    • Weis, D.D., Engen, J.R., Kass, I.J., Semi-automated data processing of hydrogen exchange mass spectra using HX-Express. J. Am. Soc. Mass Spectrom. 17 (2006), 1700–1703.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 45
    • 84864363185 scopus 로고    scopus 로고
    • Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120
    • West, A.P., Diskin, R., Nussenzweig, M.C., Bjorkman, P.J., Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120. Proc. Natl. Acad. Sci. USA 109 (2012), E2083–E2090.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. E2083-E2090
    • West, A.P.1    Diskin, R.2    Nussenzweig, M.C.3    Bjorkman, P.J.4
  • 47
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu, X., Zhou, T., Zhu, J., Zhang, B., Georgiev, I., Wang, C., Chen, X., Longo, N.S., Louder, M., McKee, K., et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 333 (2011), 1593–1602.
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1    Zhou, T.2    Zhu, J.3    Zhang, B.4    Georgiev, I.5    Wang, C.6    Chen, X.7    Longo, N.S.8    Louder, M.9    McKee, K.10
  • 48
    • 0042744723 scopus 로고    scopus 로고
    • Structural plasticity and the evolution of antibody affinity and specificity
    • Yin, J., Beuscher, A.E., Andryski, S.E., Stevens, R.C., Schultz, P.G., Structural plasticity and the evolution of antibody affinity and specificity. J. Mol. Biol. 330 (2003), 651–656.
    • (2003) J. Mol. Biol. , vol.330 , pp. 651-656
    • Yin, J.1    Beuscher, A.E.2    Andryski, S.E.3    Stevens, R.C.4    Schultz, P.G.5
  • 50
    • 84882589754 scopus 로고    scopus 로고
    • Multidonor Analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies
    • Zhou, T., Zhu, J., Wu, X., Moquin, S., Zhang, B., Acharya, P., Multidonor Analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity 39 (2013), 245–258.
    • (2013) Immunity , vol.39 , pp. 245-258
    • Zhou, T.1    Zhu, J.2    Wu, X.3    Moquin, S.4    Zhang, B.5    Acharya, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.