Functional Display of Maackia amurensis Hemagglutinin (MAH) on Bacteriophage

박테리오파아지 표면 발현 시스템을 이용한 Maackia amurensis Hemagglutinin (MAH)의 기능적 발현

  • Published : 2003.06.01

Abstract

A library of unlimited number of novel lectins with diverse specificities has been previously generated by randomly mutating the carbohydrate-recognition domain of Maackia amurensis hemagglutinin (MAH). To establish the experimental environment capable of selecting high affinity mutant lectins in E. coli, phage display system was adapted. Carbohydrate binding capacity of two phagemid vectors, pComb3 and pComb8 displaying wild-type MAH lectin was assessed. Specific bindings of pComb3 and pComb8 phages expressing w.t. MAH to affinity-purified polyclonal anti-MAH antibody and to glycophorin was demonstrated. Both phages also showed strong hemagglutinating activity to intact but not sialidase-treated human erythrocytes, which is consistent to the specificity of native MAH. Taken together, two different phage display vectors successfully allowed the expression of active MAH as a fusion protein on the surface of bacteriophage, which will lead to preparation of unique plant lectins with high affinity toward a variety of carbohydrate chains.

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References

  1. Vox Sang v.78 Introduction to antibody engineering and phage display Watkins, N. A.;Ouwehand, W. H. https://doi.org/10.1046/j.1423-0410.2000.7820072.x
  2. J. Gerontol. A. Biol. Sci. Med. Sci. v.50 Variations in activity of the human natural anti-Gal antibody in young and elderly populations Wang, L.;Anaraki, F.;Henion, T. R.;Galili, U.
  3. Glycoconj. J. v.17 A journey to the world of glycobiology Kobata, A. https://doi.org/10.1023/A:1011006122704
  4. Proc. Natl. Acad. Sci. U.S.A. v.99 Glycosylation defining cancer malignancy : new wine in an old bottle Hakomori, S. https://doi.org/10.1073/pnas.172380699
  5. Proc. Natl. Acad. Sci. U.S.A. v.98 Mutated plant lectin library useful to identify different cells Yim, M.;Ono, T.;Irimura, T. https://doi.org/10.1073/pnas.041621998
  6. Proc. Natl. Acad. Sci. U.S.A. v.91 Lambda foo: a lambda phage vector for the expression of foreign proteins Maruyama, I. N.;Maruyama, H. I.;Brenner, S. https://doi.org/10.1073/pnas.91.17.8273
  7. Nat. Biotechnol. v.15 Efficient epitope mapping by bacteriophage lambda surface display Kuwabara, I.;Maruyama, H.;Mikawa, Y. G.;Zuberi, R. I.;Liu, F. T.;Maruyama, I. N. https://doi.org/10.1038/nbt0197-74
  8. Proc. Natl. Acad. Sci. U.S.A. v.88 Assembly of combinatorial antibody libraries on phage surfaces: the gene III site Barbas, C. F. 3rd;Kang, A. S.;Lerner, R. A.;Benkovic, S. J. https://doi.org/10.1073/pnas.88.18.7978
  9. Proc. Natl. Acad. Sci. U.S.A. v.88 Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries Kang, A. S.;Jones, T. M.;Burton, D. R. https://doi.org/10.1073/pnas.88.24.11120
  10. J. Immunol. v.149 Application of a filamentous phage pⅧ fusion protein system suitable for efficient produciton, screening, and mutagenesis of F(ab) antibody fragments Huse, W. D.;Stinchcombe, T. J.;Glaser, S. M.;Starr, L.;MacLean, M.;Hellstrom, K. E.;Hellstrom, I.;Yelton, D. E.
  11. Mol. Immunol. v.34 Cloning of anti-Gal Fabs from combinatorial phage display libraries: structural analysis and comparison of Fab expression in pComb3H and pComb8 phage Wang, L.;Radic, M. Z.;Siegel, D.;Chang, T.;Bracy, J.;Galili, U. https://doi.org/10.1016/S0161-5890(97)00082-5
  12. Biochemistry v.15 Elucidation of lectin receptors by quantitative inhibition of lectin binding to human erythrocytes and lymphocytes Kawaguchi, T.;Osawa, T. https://doi.org/10.1021/bi00666a006
  13. FEBS. Lett. v.342 of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A Konami, Y.;Yamamoto, K.;Osawa, T.;Irimura, T. https://doi.org/10.1016/0014-5793(94)80527-X
  14. J. Biochem.(Tokyo) v.115 A unique amino acid sequence involved in the putative carbohydrate-binding domain of a legume lectin specific for sialylated carbohydrate chains: primary sequence determination of Maackia amurensis hemagglutinin (MAH) Konami, Y.;Ishida, C.;Yamamoto, K.;Osawa, T.;Irimura, T. https://doi.org/10.1093/oxfordjournals.jbchem.a124408
  15. J. Biochem. (Tokyo) v.121 Sialic acid-binding motif of Maackia amurensis lectins Yamamoto, K.;Konami, Y.;Irimura, T. https://doi.org/10.1093/oxfordjournals.jbchem.a021650
  16. J. Biol. Chem. v.275 An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides Imberty, A.;Gautier, C.;Lescar, C.;Lescar, J.;Perez, S.;Wyns, L.;Loris, R. https://doi.org/10.1074/jbc.M000560200
  17. Glycobiology v.2 Diversity in the sialic acids Varki, A. https://doi.org/10.1093/glycob/2.1.25
  18. Glycobiology v.2 Polysialylation: from bacteria to brains Troy, F. A. 2nd. https://doi.org/10.1093/glycob/2.1.5