Interaction of epitope-related and -unrelated peptides with anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab fragment

Journal of Molecular Recognition

Volumn 16, Issue 1, 2003, Pages 54-62

  Welfle, Karin ^a   Misselwitz, Rolf ^a   Höhne, Wolfgang ^b   Welfle, Heinz ^a  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

Binding constant; Binding specificity; Circular dichroism; Isothermal titration calorimetry

Indexed keywords

ANIMALS; ANTIBODIES, MONOCLONAL; CALORIMETRY; EPITOPES; HIV CORE PROTEIN P24; HUMANS; IMMUNOGLOBULIN FAB FRAGMENTS; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

EID: 0037263711     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/jmr.607     Document Type: Article

References (27)

1. Baker BM, Murphy KP. 1998. Prediction of binding energetics from structure using empirical parameterization. Meth. Enzymol. 295: 294-315.
2. Berthet-Colominas C, Monaco S, Novelli A, Sibai G, Mallet F, Cusack S. 1999. Head-to-tail dimers and interdomain flexibility revealed by the crystal structure of HIV-1 capsid protein (p24) complexed with a monoclonal antibody Fab. EMBO J. 18: 1124-1136.
3. Buck M. 1998. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 31: 297-355.
4. Freire E. 1999. The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme. Proc. Natl Acad. Sci. USA 96: 10118-10122.
5. Fukada H, Takahashi K. 1998. Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride. Proteins: Struct. Funct. Genet. 33: 159-166.
6. Gamble TR, Yoo S, Vajdos FF, von Schwedler UK, Worthylake DK, Wang H, McCutcheon JP, Sundquist WI, Hill CP. 1997. Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science 278: 849-853.
7. Gitti R, Lee BM, Walker J, Summers MF, Yoo S, Sundquist WI. 1996. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science 273: 231-235.
8. Grunow R, Giese R, Porstmann T, Doepel H, Haensel K, von Baehr R. 1990. Development and biological testing of human and murine antibodies against HIV antigens. Z. Klin. Med. 45: 367-369.
9. Höhne W, Küttner G, Kießig S, Hausdorf G, Grunow R, Winkler K, Wessner H, Gießmann E, Stigler R, Schneider-Mergener J, von Baehr R, Schomburg D. 1993. Structural base of the interaction of a monoclonal antibody against p24 of HIV-1 with its peptide epitope. Mol. Immunol. 30: 1213-1221.
10. Keitel T, Kramer A, Wessner H, Scholz C, Schneider-Mergener J, Höhne W. 1997. Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity. Cell 91: 811-820.
11. Kramer A, Keitel T, Winkler K, Stöcklein W, Höhne W, Schneider-Mergener J. 1997. Molecular basis for the binding promiscuity of an anti-p24 (HIV-1) monoclonal antibody. Cell 91: 799-809.
12. Lavigne P, Bagu JR, Boyko R, Willard L, Holmes CFB, Sykes BD. 2000. Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcytin-LR docked complexes. Protein Sci. 9: 252-264.
13. Lo Conte L, Chothia C, Janin J. 1999. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285: 2177-2198.
14. Luque I, Freire E. 1998. Structure-based prediction of binding affinities and molecular design of peptide ligands. Meth. Enzymol. 295: 295-315.
15. Mariuzza RA, Poljak RJ. 1993. The basics of binding: mechanisms of antigen recognition and mimicry by antibodies. Curr. Opin. Immunol. 5: 50-55.
16. Momany CL, Kovari CL, Prongay AJ, Keller W, Gitti RK, Lee BM, Gorbalenya AE, Tong L, McClure J, Ehrlich LS, Summers MF, Carter C, Rossman MG. 1996. Crystal structure of dimeric HIV-1 capsid protein. Nat. Struct. Biol. 3: 763-770.
17. Muñoz V, Serrano L. 1997. Development of the multiple sequence approximation within the Agadir model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 41: 495-509.
18. Murphy KP, Freire E. 1992. Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv. Protein Chem. 43: 323-361.
19. Murphy KP, Gill SJ. 1991. Solid model compounds and the thermodynamics of protein unfolding. J. Mol. Biol. 222: 699-709.
20. Murphy KP, Bhakuni V, Xie D, Freire E. 1992. The molecular basis of cooperativity in protein folding III: Identification of cooperative folding units and folding intermediates. J. Mol. Biol. 227: 293-306.
21. Murphy KP, Freire E, Paterson Y. 1995. Configurational effects in antibody-antigen interactions studied by microcalorimetry. Proteins: Struct. Funct. Genet. 21: 83-90.
22. Scholtz JM, Quian H, York EJ, Stewart JM, Baldwin RL. 1991. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers 31: 1463-1470.
23. Spolar RS, Record Jr MT. 1994. Coupling of local folding to sitespecific binding of proteins to DNA. Science 263: 777-784.
24. Stanfield RL, Wilson IA. 1995. Protein-peptide interactions. Curr. Opin. Struct. Biol. 5:103-113.
25. Welfle K, Misselwitz R, Hausdorf G, Höhne W, Welfle H. 1999. Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments. Biochim. Biophys. Acta 1431: 120-131.
26. Wilson IA, Stanfield RL. 1994. Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4: 857-867.
27. Wiseman T, Williston S, Brandts JF, Lin LN. 1989. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179: 131-137.