메뉴 건너뛰기




Volumn 13, Issue 1, 2000, Pages 5-13

Native-like cyclic peptide models of a viral antigenic site: Finding a balance between rigidity and flexibility

Author keywords

Antigenic site A; Conformational stability; Cyclic disulfide peptide; Epitope mimics; Foot and mouth disease virus

Indexed keywords

ANTIGEN DETECTION; ANTIGEN SPECIFICITY; CIRCULAR DICHROISM SPECTROSCOPY; CRYSTALLOGRAPHY; CYCLIZATION; DISULFIDE BOND; ENVELOPE PROTEIN; FOOT AND MOUTH DISEASE VIRUS C; MONOCLONAL ANTIBODY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PROTEIN CONFORMATION; PROTEIN STABILITY; VIRUS ANTIGEN;

EID: 0034013532     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1352(200001/02)13:1<5::AID-JMR480>3.0.CO;2-L     Document Type: Article
Times cited : (28)

References (51)
  • 1
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution
    • Acharya R, Fry E, Stuart D, Fox G, Rowlands DJ, Brown F. 1989. The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution. Nature 337: 709-716.
    • (1989) Nature , vol.337 , pp. 709-716
    • Acharya, R.1    Fry, E.2    Stuart, D.3    Fox, G.4    Rowlands, D.J.5    Brown, F.6
  • 2
    • 0029039463 scopus 로고
    • Boc-S-methylbenzyl-(S)-2-amino-6-mercaptohexanoic acid: Preparation and application to the synthesis of a large cyclic disulfide peptide
    • Adeva A, Camarero JA, Giralt E, Andreu D. 1995. Boc-S-methylbenzyl-(S)-2-amino-6-mercaptohexanoic acid: preparation and application to the synthesis of a large cyclic disulfide peptide. Tetrahedron Lett. 36: 3885-3888.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 3885-3888
    • Adeva, A.1    Camarero, J.A.2    Giralt, E.3    Andreu, D.4
  • 5
    • 0014373538 scopus 로고
    • Foot-and-mouth disease
    • Bachrach, HL. 1968. Foot-and-mouth disease. A. Rev. Microbiol. 22: 201-244.
    • (1968) A. Rev. Microbiol. , vol.22 , pp. 201-244
    • Bachrach, H.L.1
  • 6
    • 0016817235 scopus 로고
    • Immune and antibody responses to an isolated capsid protein of foot-and-mouth disease virus
    • Bachrach HL, Moore DM, McKercher PD, Polatnik J. 1975. Immune and antibody responses to an isolated capsid protein of foot-and-mouth disease virus. J. Immunol. 115: 1636-1641.
    • (1975) J. Immunol. , vol.115 , pp. 1636-1641
    • Bachrach, H.L.1    Moore, D.M.2    McKercher, P.D.3    Polatnik, J.4
  • 7
    • 0001926444 scopus 로고
    • Solid phase peptide synthesis
    • (ed. E Gross and J Meienhofer), Academic Press, New York
    • Barany G, Merrifield RB. 1979. Solid phase peptide synthesis. In The Peptides, vol. 2 (ed. E Gross and J Meienhofer), pp. 1-284. Academic Press, New York.
    • (1979) The Peptides , vol.2 , pp. 1-284
    • Barany, G.1    Merrifield, R.B.2
  • 10
    • 0001275595 scopus 로고
    • A comparison of acid-labile linkage agents for the synthesis of peptide C-terminal amides
    • Bernatowicz MS, Daniels SB, Köster H. 1989. A comparison of acid-labile linkage agents for the synthesis of peptide C-terminal amides. Tetrahedron Lett. 30: 4645-4648.
    • (1989) Tetrahedron Lett. , vol.30 , pp. 4645-4648
    • Bernatowicz, M.S.1    Daniels, S.B.2    Köster, H.3
  • 11
    • 0019959784 scopus 로고
    • Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence
    • Bittle JL, Houghten RA, Alexander H, Sutcliffe JG, Lerner RA, Rowlands DJ, Brown F. 1982. Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature 298: 30-33.
    • (1982) Nature , vol.298 , pp. 30-33
    • Bittle, J.L.1    Houghten, R.A.2    Alexander, H.3    Sutcliffe, J.G.4    Lerner, R.A.5    Rowlands, D.J.6    Brown, F.7
  • 12
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • Bothner-By AA, Stephens RL, Lee JM, Warren CD, Jeanloz RW. 1984. Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame. J. Am. Chem. Soc. 106: 811-813.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.M.3    Warren, C.D.4    Jeanloz, R.W.5
  • 13
    • 0026595375 scopus 로고
    • New approaches to vaccination against foot-and-mouth disease
    • Brown F. 1992. New approaches to vaccination against foot-and-mouth disease. Vaccine 10: 1022-1026.
    • (1992) Vaccine , vol.10 , pp. 1022-1026
    • Brown, F.1
  • 14
    • 0027216643 scopus 로고
    • Cyclic disulfide model of the major antigenic site of serotype C foot-and-mouth disease virus
    • Camarero JA, Andreu D, Cairó JJ, Mateu MG, Domingo E, Giralt E. 1993. Cyclic disulfide model of the major antigenic site of serotype C foot-and-mouth disease virus. FEBS Lett. 328: 159-164.
    • (1993) FEBS Lett. , vol.328 , pp. 159-164
    • Camarero, J.A.1    Andreu, D.2    Cairó, J.J.3    Mateu, M.G.4    Domingo, E.5    Giralt, E.6
  • 16
    • 0016169865 scopus 로고
    • Determination of the helix and form of proteins in aqueous solution by circular dichroism
    • Chen YH, Yang JT, Chan KH. 1974. Determination of the helix and form of proteins in aqueous solution by circular dichroism. Biochemistry 23: 3350-3359.
    • (1974) Biochemistry , vol.23 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chan, K.H.3
  • 17
    • 0022444429 scopus 로고
    • Protection of cattle agains foot-and-mouth disease by a synthetic peptide
    • Di Marchi R, Brooke G, Gale C, Cracknell V, Doel T, Mowat N. 1986. Protection of cattle agains foot-and-mouth disease by a synthetic peptide. Science 232: 639-641.
    • (1986) Science , vol.232 , pp. 639-641
    • Di Marchi, R.1    Brooke, G.2    Gale, C.3    Cracknell, V.4    Doel, T.5    Mowat, N.6
  • 18
    • 0015939993 scopus 로고
    • Acid stability of several benzylic protecting groups used in solid phase peptide synthesis. Rearrangement of O-benzyltyrosine to 3-benzyltyrosine
    • Erickson BW, Merrifield RB. 1973. Acid stability of several benzylic protecting groups used in solid phase peptide synthesis. Rearrangement of O-benzyltyrosine to 3-benzyltyrosine. J. Am. Chem. Soc. 95: 3750-3756.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 3750-3756
    • Erickson, B.W.1    Merrifield, R.B.2
  • 19
    • 0001791958 scopus 로고
    • Principles and practice of solid phase peptide synthesis
    • Grant GA (ed.). Freeman, New York
    • Fields GB, Tian Z, Barany G. 1992. Principles and practice of solid phase peptide synthesis. In Synthetic Peptides: a User's Guide, Grant GA (ed.). Freeman, New York; pp. 77-183.
    • (1992) Synthetic Peptides: A User's Guide , pp. 77-183
    • Fields, G.B.1    Tian, Z.2    Barany, G.3
  • 21
    • 0025824499 scopus 로고
    • Antheprot: An interactive graphic software for analyzing protein structures from sequences
    • Geourjon C, Deléage G, Roux B. 1991. Antheprot: an interactive graphic software for analyzing protein structures from sequences. J. Mol. Graph. 9: 188-190.
    • (1991) J. Mol. Graph. , vol.9 , pp. 188-190
    • Geourjon, C.1    Deléage, G.2    Roux, B.3
  • 22
    • 0030927912 scopus 로고    scopus 로고
    • A cyclic disulfide peptide reproduces in solution the main structural features of a native antigenic site of foot-and-mouth disease virus
    • Haack T, Camarero JA, Roig X, Mateu MG, Domingo E, Andreu D, Giralt E. 1997. A cyclic disulfide peptide reproduces in solution the main structural features of a native antigenic site of foot-and-mouth disease virus. Int. J. Biol. Macromol. 20: 209-219.
    • (1997) Int. J. Biol. Macromol. , vol.20 , pp. 209-219
    • Haack, T.1    Camarero, J.A.2    Roig, X.3    Mateu, M.G.4    Domingo, E.5    Andreu, D.6    Giralt, E.7
  • 23
    • 0028231391 scopus 로고
    • Synthesis of enantiomerically pure N-Fmoc-S-Mob-S-α-amino-∈-mercaptohexanoic acid and its use in solid phase peptide synthesis
    • Heeb NB, Aberle A, Nambiar KP. 1994. Synthesis of enantiomerically pure N-Fmoc-S-Mob-(S-α-amino-∈-mercaptohexanoic acid and its use in solid phase peptide synthesis. Tetrahedron Lett. 35: 2287-2290.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 2287-2290
    • Heeb, N.B.1    Aberle, A.2    Nambiar, K.P.3
  • 24
    • 0027354351 scopus 로고
    • Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides
    • Joisson C, Kuster F, Plaué S, Van Regenmortel MHV. 1993. Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides. Arch. Virol. 128: 299-317.
    • (1993) Arch. Virol. , vol.128 , pp. 299-317
    • Joisson, C.1    Kuster, F.2    Plaué, S.3    Van Regenmortel, M.H.V.4
  • 25
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor-based analytical system
    • Karlsson R, Michaelsson A, Matsson LJ. 1991. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor-based analytical system. J. Immunol. Meth. 145: 229-240.
    • (1991) J. Immunol. Meth. , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Matsson, L.J.3
  • 28
    • 37049079283 scopus 로고
    • A novel hydrogen matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands
    • Löfås S, Johnsson B. 1990. A novel hydrogen matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands. J. Chem. Soc. Chem. Commun. 21: 1526-1528.
    • (1990) J. Chem. Soc. Chem. Commun. , vol.21 , pp. 1526-1528
    • Löfås, S.1    Johnsson, B.2
  • 30
    • 0029029433 scopus 로고
    • Antibodies raised in a natural host and monoclonal antibodies recognize similar antigenic features of foot-and-mouth disease virus
    • Mateu MG, Andreu D, Domingo E. 1995a. Antibodies raised in a natural host and monoclonal antibodies recognize similar antigenic features of foot-and-mouth disease virus. Virology 210: 120-127.
    • (1995) Virology , vol.210 , pp. 120-127
    • Mateu, M.G.1    Andreu, D.2    Domingo, E.3
  • 31
    • 0028870354 scopus 로고
    • Direct evaluation of the immunodominance of a major antigenic site of foot-and-mouth disease virus in a natural host
    • Mateu MG, Camarero JA, Andreu D, Giralt E, Domingo E. 1995b. Direct evaluation of the immunodominance of a major antigenic site of foot-and-mouth disease virus in a natural host. Virology 206: 298-306.
    • (1995) Virology , vol.206 , pp. 298-306
    • Mateu, M.G.1    Camarero, J.A.2    Andreu, D.3    Giralt, E.4    Domingo, E.5
  • 33
    • 0343160838 scopus 로고
    • Implications of a quasispecies genome structure: Effect of frequent naturally occurring amino acid substitutions on the antigenicity of foot-and-mouth disease virus
    • Mateu MG, Martínez MA, Rocha E, Andreu D, Parejo J, Giralt E, Sobrino F, Domingo E. 1989. Implications of a quasispecies genome structure: effect of frequent naturally occurring amino acid substitutions on the antigenicity of foot-and-mouth disease virus. Proc. Natl. Acad. Sci. USA 86: 5883-5887.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5883-5887
    • Mateu, M.G.1    Martínez, M.A.2    Rocha, E.3    Andreu, D.4    Parejo, J.5    Giralt, E.6    Sobrino, F.7    Domingo, E.8
  • 34
    • 0025325915 scopus 로고
    • A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus
    • Mateu MG, Martínez MA, Capucci L, Andreu D, Giralt E, Sobrino F, Brocchi E, Domingo E. 1990. A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus. J. Gen. Virol. 71: 629-637.
    • (1990) J. Gen. Virol. , vol.71 , pp. 629-637
    • Mateu, M.G.1    Martínez, M.A.2    Capucci, L.3    Andreu, D.4    Giralt, E.5    Sobrino, F.6    Brocchi, E.7    Domingo, E.8
  • 36
    • 0025029685 scopus 로고
    • Antigenic properties and protective capacity of a cyclic peptide corresponding to site A of influenza virus haemagglutinin
    • Muller S, Plaué S, Samama JP, Valette M, Briand JP, Van Regenmortel MHV. 1990. Antigenic properties and protective capacity of a cyclic peptide corresponding to site A of influenza virus haemagglutinin. Vaccine 8: 308-314.
    • (1990) Vaccine , vol.8 , pp. 308-314
    • Muller, S.1    Plaué, S.2    Samama, J.P.3    Valette, M.4    Briand, J.P.5    Van Regenmortel, M.H.V.6
  • 37
    • 0027293685 scopus 로고
    • Use of substituted and tandem-repeated peptides to probe the relevance of the highly conserved RGD tripeptide in the immune response against foot-and-mouth disease virus
    • Novella IS, Borrego B, Mateu MG, Domingo E, Giralt E, Andreu D. 1993. Use of substituted and tandem-repeated peptides to probe the relevance of the highly conserved RGD tripeptide in the immune response against foot-and-mouth disease virus. FEBS Lett. 330: 253-259.
    • (1993) FEBS Lett. , vol.330 , pp. 253-259
    • Novella, I.S.1    Borrego, B.2    Mateu, M.G.3    Domingo, E.4    Giralt, E.5    Andreu, D.6
  • 38
    • 0017584483 scopus 로고
    • Subtyping of foot-and-mouth disease virus
    • Mackowiak C and Regamey RH (eds). Karger, Basel
    • Pereira HG. 1977. Subtyping of foot-and-mouth disease virus. In: Developments in Biological Standardization, vol. 35. Mackowiak C and Regamey RH (eds). Karger, Basel; pp. 167-174.
    • (1977) Developments in Biological Standardization , vol.35 , pp. 167-174
    • Pereira, H.G.1
  • 39
    • 0003285096 scopus 로고
    • Foot-and-mouth disease
    • Gibbs EPJ (ed.). Academic Press, New York
    • Pereira HG. 1981. Foot-and-mouth disease. In Virus Diseases of Food Animals, vol. 2. Gibbs EPJ (ed.). Academic Press, New York; pp. 333-363.
    • (1981) Virus Diseases of Food Animals , vol.2 , pp. 333-363
    • Pereira, H.G.1
  • 40
    • 1042283148 scopus 로고
    • Antibodies against a preselected peptide recognize and neutralize foot-and-mouth disease virus
    • Pfaff E, Mussgay M, Böhm HO, Schultz GE, Schaller H. 1982. Antibodies against a preselected peptide recognize and neutralize foot-and-mouth disease virus. EMBO J. 1: 869-874.
    • (1982) EMBO J. , vol.1 , pp. 869-874
    • Pfaff, E.1    Mussgay, M.2    Böhm, H.O.3    Schultz, G.E.4    Schaller, H.5
  • 41
    • 0028135460 scopus 로고
    • Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technique and ELISA
    • Richalet-Secordel PM, Zeder-Lutz G, Plaué S, Sommermeyer-Leroux G, Van Regenmortel MHV. 1994a. Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technique and ELISA. J. Immunol. Meth. 176: 221-234.
    • (1994) J. Immunol. Meth. , vol.176 , pp. 221-234
    • Richalet-Secordel, P.M.1    Zeder-Lutz, G.2    Plaué, S.3    Sommermeyer-Leroux, G.4    Van Regenmortel, M.H.V.5
  • 42
    • 0028168419 scopus 로고
    • Cross-reactive potential of rabbit antibodies raised against a cyclic peptide representing a chimeric V3 loop of HIV-1 gp120 studied by biosensor technique and ELISA
    • Richalet-Secordel PM, Deslandres A, Plaué S, You B, Barré-Sinoussi, Van Regenmortel MHV. 1994b. Cross-reactive potential of rabbit antibodies raised against a cyclic peptide representing a chimeric V3 loop of HIV-1 gp120 studied by biosensor technique and ELISA. FEMS Immunol. Med. Microbiol. 9: 77-88.
    • (1994) FEMS Immunol. Med. Microbiol. , vol.9 , pp. 77-88
    • Richalet-Secordel, P.M.1    Deslandres, A.2    Plaué, S.3    You, B.4    Van Regenmortel, M.H.V.5
  • 43
    • 0030571002 scopus 로고    scopus 로고
    • Analysis of mass transport-limited binding kinetics in evanescent wave biosensors
    • Schuck P, Minton AP. 1996. Analysis of mass transport-limited binding kinetics in evanescent wave biosensors. Anal. Biochem. 240: 262-272.
    • (1996) Anal. Biochem. , vol.240 , pp. 262-272
    • Schuck, P.1    Minton, A.P.2
  • 44
    • 0022454040 scopus 로고
    • Immunogenicity of loop-structured short synthetic peptides mimicking the antigenic site A of influenza virus haemagglutinin
    • Schulze-Gahmen U, Klenk HD, Beyreuther K. 1986. Immunogenicity of loop-structured short synthetic peptides mimicking the antigenic site A of influenza virus haemagglutinin. Eur. J. Biochem. 159: 283-289.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 283-289
    • Schulze-Gahmen, U.1    Klenk, H.D.2    Beyreuther, K.3
  • 45
    • 0019990849 scopus 로고
    • Location and characterization of the antigenic portion of the FMDV immunizing protein
    • Strohmaier K, Franze R, Adam KH. 1982. Location and characterization of the antigenic portion of the FMDV immunizing protein. J. Gen. Virol. 59: 295-306.
    • (1982) J. Gen. Virol. , vol.59 , pp. 295-306
    • Strohmaier, K.1    Franze, R.2    Adam, K.H.3
  • 46
    • 0020661774 scopus 로고
    • Antibodies that react with predeterminated sites on proteins
    • Sutcliffe JG, Shinnick TM, Green N, Lerner R. 1983. Antibodies that react with predeterminated sites on proteins. Science 219: 660-666.
    • (1983) Science , vol.219 , pp. 660-666
    • Sutcliffe, J.G.1    Shinnick, T.M.2    Green, N.3    Lerner, R.4
  • 47
    • 0342644832 scopus 로고    scopus 로고
    • A comparative study of cyclization strategies applied to the synthesis of head-to-tail cyclic analogs of a viral epitope
    • Valero M-L, Giralt E, Andreu D. 1999. A comparative study of cyclization strategies applied to the synthesis of head-to-tail cyclic analogs of a viral epitope. J. Pept. Res. 53: 56-67.
    • (1999) J. Pept. Res. , vol.53 , pp. 56-67
    • Valero, M.-L.1    Giralt, E.2    Andreu, D.3
  • 48
    • 0028575730 scopus 로고
    • Ability of linear and cyclic peptides of neutralization antigenic site 1 of poliovirus type 1 to induce virus cross-reactive and neutralizing antibodies
    • Van der Werf S, Briand JP, Plaué S, Burckard J, Girard M, Van Regenmortel MHV. 1994. Ability of linear and cyclic peptides of neutralization antigenic site 1 of poliovirus type 1 to induce virus cross-reactive and neutralizing antibodies. Res. Virol. 145: 349-359.
    • (1994) Res. Virol. , vol.145 , pp. 349-359
    • Van Der Werf, S.1    Briand, J.P.2    Plaué, S.3    Burckard, J.4    Girard, M.5    Van Regenmortel, M.H.V.6
  • 49
    • 0029019739 scopus 로고
    • Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: Direct involvement of the Arg-Gly-Asp motif in the interaction
    • Verdaguer N, Mateu MG, Andreu D, Giralt E, Domingo E, Fita I, 1995. Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: Direct involvement of the Arg-Gly-Asp motif in the interaction. EMBO J. 14: 1690-1696.
    • (1995) EMBO J. , vol.14 , pp. 1690-1696
    • Verdaguer, N.1    Mateu, M.G.2    Andreu, D.3    Giralt, E.4    Domingo, E.5    Fita, I.6
  • 50
    • 0031963629 scopus 로고    scopus 로고
    • A similar pattern of interaction for different antibodies with a major antigenic site of foot-and-mouth disease virus: Implications for intratypic antigenic variation
    • Verdaguer N, Sevilla N, Valero ML, Stuart D, Brocchi E, Andreu D, Giralt E, Domingo E, Mateu MG, Fita I. 1998. A similar pattern of interaction for different antibodies with a major antigenic site of foot-and-mouth disease virus: implications for intratypic antigenic variation. J. Virol. 72: 739-748.
    • (1998) J. Virol. , vol.72 , pp. 739-748
    • Verdaguer, N.1    Sevilla, N.2    Valero, M.L.3    Stuart, D.4    Brocchi, E.5    Andreu, D.6    Giralt, E.7    Domingo, E.8    Mateu, M.G.9    Fita, I.10
  • 51
    • 0025729547 scopus 로고
    • Design of bioactive peptides based on antibody hypervariable region structures. Development of conformationally constrained and dimeric peptides with enhanced affinity
    • Williams WV, Kieber-Emmons T, Von Feldt J, Greene MI, Weiner DB. 1991. Design of bioactive peptides based on antibody hypervariable region structures. Development of conformationally constrained and dimeric peptides with enhanced affinity. J. Biol. Chem. 266: 5182-5190.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5182-5190
    • Williams, W.V.1    Kieber-Emmons, T.2    Von Feldt, J.3    Greene, M.I.4    Weiner, D.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.