On the peptide-antipeptide interactions in interleukin-1 receptor system

• Autorzy: Kluczyk A. , Cebrat M. , Zbozien-Pacamaj R. , Lisowski M. , Stefanowicz P. , Wieczorek Z. , Siemion I.Z.
• Języki publikacji: EN

Abstrakty

EN

Interleukin-1 receptor antagonist (IL-1Ra) and vaccinia virus protein C10L share a VTXFYF motif, with X being Lys or Arg residue, respectively. Peptides of such se­quence compete successfully with IL-1 for the cellular receptor. A pair of complemen­tary peptides, based on the Siemion's hypothesis on the periodicity of the genetic code (QWLNIN and QWANIN), and another pair, in which, following the Root- Bernstein theory, Lys was used as complementary amino acid to Phe (QWLKIK and QWAKIK), were investigated for the peptide-antipeptide interactions using mass spectrometry (ESI-MS) and circular dichroism (CD) methods. The CD measurements indicated some conformational changes, more pronounced in the Siemion's pairs, however, no heterodimer formation was found by MS. In the region of IL-1 receptor situated close to the position of IL-1Ra in the IL-1Ra-receptor complex, a KQKL mo­tif is present, suggesting a possibility of complementary recognition of the Root-Bernstein type in the IL-1 receptor. The biological activity of the complemen­tary peptides is similar to that of the original ones. They efficiently compete with IL-1 and show moderate immunosuppressory activity in humoral and cellular immune re­sponse. The inhibition of the IL-1-IL-1 receptor interaction may result from the com­plementary peptides acting as mini-receptors with affinity for IL-1.

Słowa kluczowe

EN

interleukin 1; vaccinia virus protein; receptor system; peptide-antipeptide interaction; immunomodulation; receptor antagonist; complementary peptide

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 1
• Opis fizyczny: p.57-66,fig.,ref.

Twórcy

autor

Kluczyk A.

• University of Wroclaw, F.Joliot-Curie 14, 50-383 Wroclaw, Poland

autor

Cebrat M.

autor

Zbozien-Pacamaj R.

autor

Lisowski M.

autor

Stefanowicz P.

autor

Wieczorek Z.

autor

Siemion I.Z.

Bibliografia

• Alcami A, Koszinowski UH. (2000) Viral mechanisms of immune evasion. Trends Microbiol.; 8: 410-8.
• Antoni G, Presentini R, Perin F, Tagliabue A, Ghiara P, Censini S, Volpini G, Villa L, Borashi D. (1986) A short synthetic peptide fragment of human interleukin 1 with immunostimulatory but not inflammatory activity. J Immunol.; 137: 3201-4.
• Arend WP, Malyak M, Guthridge CJ, Gabay C. (1998) Interleukin-1 receptor antagonist: role in biology. Annu Rev Immunol.; 16: 27-55.
• Blalock JE, Smith EM. (1984) Hydropathic anti-complementarity of amino acids based on the genetic code. Biochem Biophys Res Commun.; 121: 203-7.
• Boraschi D, Antoni G, Perin F, Villa L, Nencioni L, Ghiara P, Presentini R, Tagliabue A. (1990) Defining the structural requirements of a biologically active domain of human IL-1. Eur Cytokine Netw.; 1: 21-6.
• Casadio R, Frigimelica E, Bossu P, Neumann D, Martin MU, Tagliabue A, Boraschi D. (2001) Model of interaction of the IL-1 receptor accessory protein IL-1RAcP with the IL-1beta/IL-1R1 complex. FEBSLett.; 499: 65- 8.
• Davids JW, El-Bakri A, Heal J, Christie G, Roberts GW, Raynes JG, Miller AD. (1997) Design of antisense (complementary) peptides as selective inhibitors of cytokine interleukin-1. Angew Chem Int Ed.; 36: 962-7.
• Dinarello CA. (1996) Biological basis for interleukin-1 in disease. Blood.; 87: 2095-147.
• Goebel SJ, Johnson GP, Perkus ME, Davis SW, Winslow JP, Paoletti E. (1990) The complete DNA sequence of vaccinia virus. Virology.; 179: 247-66.
• Greenfeder SA, Nunes P, Kwee L, Labow M, Chizzonite RA, Ju G. (1995) Molecular cloning and characterization of a second subunit of the interleukin 1 receptor complex. J Biol Chem.; 270: 13757-65.
• Heal JR, Bino S, Roberts GW, Raynes JG, Miller AD. (2000) Mechanistic investigation into complementary (antisense) peptide mini-receptor inhibitors of cytokine interleukin-1. Chembiochem.; 3: 76-85.
• Holsworth DD, Kiely JS, Root-Bernstein RS, Overhiser RW. (1994) Antisense-designed peptides: a comparative study focusing on possible complements to angiotensin II. PeptRes.; 7: 185-93.
• Ju G, Labriola-Tompkins E, Campen CA, Benjamin WR, Karas J, Plocinski J, Biondi D, Kaffka KL, Kilian PL, Eisenberg SP, Evans RJ. (1991) Conversion of the interleukin 1 receptor antagonist into an agonist by site-specific mutagenesis. Proc Natl Acad Sci U S A.; 88: 2658-62.
• Kluczyk A, Siemion IZ, Szewczuk Z, Wieczorek Z. (2002) The immunosuppressive activity of peptide fragments of vaccinia virus C10L protein and a hypothesis on the role of this protein in the viral invasion. Peptides.; 23: 823-34.
• Korherr C, Hofmeister R, Wesche H, Falk W. (1997) A critical role for interleukin-1 receptor accessory protein in interleukin-1 signaling. Eur J Immunol.; 27: 262-7.
• Lagrange PH, Mackaness GB, Miller TE, Pardon P. (1974) Influence of dose and route of antigen injection on the immunological induction of T cells. J Exp Med.; 139: 528-42.
• Loo JA, Holsworth DD, Root-Bernstein RS. (1994) Use of electrospray ionization mass spectroscopy to probe antisense peptide interactions. Biol Mass Spectrom.; 23: 6-12.
• Madhusudanan KP, Katti SB, Haq W, Misra PK. (2000) Antisense peptide interactions studied by electrospray ionization mass spectrometry. J Mass Spectrom.; 35: 237-41.
• Mekler LB. (1969) On specific selective interaction between amino acid residues of polypeptide chains. Biofizika (Russ.); 14: 581-4.
• Mishell RI, Dutton RW. (1967) Immunization of dissociated spleen cell cultures from normal mice. J Exp Med.; 126: 423-42.
• Root-Bernstein RS. (1982) Amino acid pairing. J Theor Biol.; 94: 885-94.
• Root-Bernstein RS, Holsworth DD. (1998) Antisense peptides: a critical mini-review. J Theor Biol.; 190: 107-19.
• Rothwell N. (2003) Interleukin-1 and neuronal injury: mechanisms, modification, and therapeutic potential. Brain Behav Immun.; 17: 152-7.
• Schreuder H, Tardif C, Trump-Kallmeyer S, Soffientini A, Sarubbi E, Akeson A, Bowlin T, Yanofski S, Barret RW. (1997) A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist. Nature.; 386: 194-200.
• Siemion IZ. (1995) The regularities of the changes of amino acid physico-chemical properties within the genetic code. Amino Acids. ; 8: 1-13.
• Siemion IZ, Kluczyk A, Wieczorek Z. (1998) Anti-IL-1 activity of peptide fragments of IL-1 family proteins. Peptides.; 19: 373-82.
• Siemion IZ, Zbozien-Pacamaj R, Stefanowicz P. (2001) New hypothesis on amino acid complementarity and its evaluation on TGF-beta2-related peptides. JMolRecognit.; 14: 1-12.
• Sims JE. (2002) IL-1 and IL-18 receptors, and their extended family. Curr Opin Immunol.; 14: 117-22.
• Small RE, Wixted MA, Roberts WN. (2001) Anakinra. An interleukin-1 receptor antagonist for treatment of rheumatoid arthritis. Formulation.; 36: 191-203.
• Smith GL, Symons JA, Khanna A, Vanderplasschen A, Alcami A. (1997) Vaccinia virus immune evasion. Immunol Rev. ; 159: 137-54.
• Vigers GPA, Anderson LJ, Caffes P, Brandhuber BJ. (1997) Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1. Nature.; 386: 190-4.
• Wieczorek Z, Kluczyk A, Slon-Usakiewicz JJ, Siemion IZ. (1997) A hexapeptide VTKFYF from C-terminal part of interleukin-1 receptor antagonist, an inhibitor of IL-1-IL-1 receptor interaction. Pol J Pharmacol.; 49: 107-17.