Stabilisation of the FC fragment of human IgG1 by engineered intradomain disulfide bonds

PLoS ONE

Volumn 7, Issue 1, 2012, Pages

  Wozniak Knopp, Gordana ^a   Stadlmann, Johannes ^a   Rüker, Florian ^a  

^a UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; FC RECEPTOR; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G1; DISULFIDE; IMMUNOGLOBULIN G;

AMINO TERMINAL SEQUENCE; ANTIGEN BINDING; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DISULFIDE BOND; HUMAN; MELTING POINT; PROTEIN DOMAIN; THERMOSTABILITY; WILD TYPE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; GENETICS; MASS SPECTROMETRY; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; MUTATION; PROTEIN BINDING; PROTEIN ENGINEERING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTEIN UNFOLDING; TEMPERATURE; TRANSITION TEMPERATURE;

AMINO ACID SEQUENCE; BINDING SITES; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; DISULFIDES; HUMANS; IMMUNOGLOBULIN FC FRAGMENTS; IMMUNOGLOBULIN G; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN ENGINEERING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; RECEPTOR, ERBB-2; TEMPERATURE; TRANSITION TEMPERATURE;

EID: 84855857695     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030083     Document Type: Article

References (32)

1. Huber R, Deisenhofer J, Colman PM, Matsushima M, Palm W, (1976) Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature 264: 415-420.
2. Wozniak-Knopp G, Bartl S, Bauer A, Mostageer M, Woisetschlager M, et al. (2010) Introducing antigen-binding sites in structural loops of immunoglobulin constant domains: Fc fragments with engineered HER2/neu-binding sites and antibody properties. Protein Eng Des Sel 23: 289-297.
3. Tischenko VM, Abramov VM, Zav'yalov VP, (1998) Investigation of the cooperative structure of Fc fragments from myeloma immunoglobulin G. Biochemistry 37: 5576-5581.
4. Ghirlando R, Lund J, Goodall M, Jefferis R, (1999) Glycosylation of human IgG-Fc: influences on structure revealed by differential scanning micro-calorimetry. Immunol Lett 68: 47-52.
5. Demarest SJ, Rogers J, Hansen G, (2004) Optimization of the antibody C(H)3 domain by residue frequency analysis of IgG sequences. J Mol Biol 335: 41-48.
6. Gong R, Vu BK, Feng Y, Prieto DA, Dyba MA, et al. (2009) Engineered human antibody constant domains with increased stability. J Biol Chem 284: 14203-14210.
7. Hagihara Y, Mine S, Uegaki K, (2007) Stabilization of an immunoglobulin fold domain by an engineered disulfide bond at the buried hydrophobic region. J Biol Chem 282: 36489-36495.
8. Jefferis R, Lund J, Pound JD, (1998) IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation. Immunol Rev 163: 59-76.
9. Burmeister WP, Gastinel LN, Simister NE, Blum ML, Bjorkman PJ, (1994) Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor. Nature 372: 336-343.
10. Burmeister WP, Huber AH, Bjorkman PJ, (1994) Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 372: 379-383.
11. Mimura Y, Church S, Ghirlando R, Ashton PR, Dong S, et al. (2000) The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms. Mol Immunol 37: 697-706.
12. Vaughn DE, Bjorkman PJ, (1997) High-affinity binding of the neonatal Fc receptor to its IgG ligand requires receptor immobilization. Biochemistry 36: 9374-9380.
13. Vaughn DE, Milburn CM, Penny DM, Martin WL, Johnson JL, et al. (1997) Identification of critical IgG binding epitopes on the neonatal Fc receptor. J Mol Biol 274: 597-607.
14. Kabat EA, Wu TT, Perry HM, Gottesman KS, Foeller C, (1991) Sequences of Proteins of Immunological Interest 5th edn (US Department of Health and Human Services). NIH Publication No 91-3242.
15. Hider RC, Kupryszewski G, Rekowski P, Lammek B, (1988) Origin of the positive 225-230 nm circular dichroism band in proteins. Its application to conformational analysis. Biophys Chem 31: 45-51.
16. Kotzia GA, Labrou NE, (2009) Engineering thermal stability of L-asparaginase by in vitro directed evolution. FEBS J 276: 1750-1761.
17. Dahiyat BI, (1999) In silico design for protein stabilization. Curr Opin Biotechnol 10: 387-390.
18. Gershenson A, Arnold FH, (2000) Enzyme stabilization by directed evolution. Genet Eng (N Y) 22: 55-76.
19. Steipe B, Schiller B, Pluckthun A, Steinbacher S, (1994) Sequence statistics reliably predict stabilizing mutations in a protein domain. J Mol Biol 240: 188-192.
20. Betz SF, (1993) Disulfide bonds and the stability of globular proteins. Protein Sci 2: 1551-1558.
21. Saerens D, Conrath K, Govaert J, Muyldermans S, (2008) Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains. J Mol Biol 377: 478-488.
22. Arbabi-Ghahroudi M, To R, Gaudette N, Hirama T, Ding W, et al. (2009) Aggregation-resistant VHs selected by in vitro evolution tend to have disulfide-bonded loops and acidic isoelectric points. Protein Eng Des Sel 22: 59-66.
23. Deisenhofer J, (1981) Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. Biochemistry 20: 2361-2370.
24. Powers DB, Amersdorfer P, Poul M, Nielsen UB, Shalaby MR, et al. (2001) Expression of single-chain Fv-Fc fusions in Pichia pastoris. J Immunol Methods 251: 123-135.
25. Bretthauer RK, Castellino FJ, (1999) Glycosylation of Pichia pastoris-derived proteins. Biotechnol Appl Biochem 30 (Pt 3): 193-200.
26. Schellman JA, (1955) The stability of hydrogen-bonded peptide structures in aqueous solution. C R Trav Lab Carlsberg Chim 29: 230-259.
27. Pace CN, Grimsley GR, Thomson JA, Barnett BJ, (1988) Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J Biol Chem 263: 11820-11825.
28. McAuley A, Jacob J, Kolvenbach CG, Westland K, Lee HJ, et al. (2008) Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain. Protein Sci 17: 95-106.
29. Azuma H, Hayashi T, Dent JA, Ruggeri ZM, Ware J, (1993) Disulfide bond requirements for assembly of the platelet glycoprotein Ib-binding domain of von Willebrand factor. J Biol Chem 268: 2821-2827.
30. Furukawa Y, Torres AS, O'Halloran TV, (2004) Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. EMBO J 23: 2872-2881.
31. Sowdhamini R, Srinivasan N, Shoichet B, Santi DV, Ramakrishnan C, et al. (1989) Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. Protein Eng 3: 95-103.
32. Ruiz M, Lefranc MP, (2002) IMGT gene identification and Colliers de Perles of human immunoglobulins with known 3D structures. Immunogenetics 53: 857-883.