Model-based development of an assay for the rapid detection of biotin-blocked binding sites of streptavidin

Engineering in Life Sciences

Volumn 15, Issue 6, 2015, Pages 627-639

  Müller, Jakob M ^a   Risse, Joe M ^a   Friehs, Karl ^a   Flaschel, Erwin ^a  

^a BIELEFELD UNIVERSITY   (Germany)

Author keywords

Assay; Detection of biotin blocked binding sites; Fermentation monitoring; Kinetic modeling; Streptavidin

Indexed keywords

ASSAYS; BINS; COENZYMES; DISSOCIATION; FERMENTATION; KINETIC THEORY; PROTEINS; QUENCHING;

DISSOCIATION CONSTANT; FERMENTATION MONITORING; FERMENTATION PROCESS; FLUORESCENCE QUENCHING; KINETIC MODELING; MODEL BASED DEVELOPMENT; PROTEIN STREPTAVIDIN; STREPTAVIDIN;

BINDING SITES;

BIOTIN; STREPTAVIDIN;

ASSAY; CHEMICAL BINDING; DETECTION METHOD; FERMENTATION; FLUORESCENCE; KINETICS; MODEL TEST; MOLECULAR ANALYSIS; PROTEIN; VITAMIN;

ARTICLE; BINDING SITE; BIOASSAY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DISSOCIATION CONSTANT; ESCHERICHIA COLI; FERMENTATION MONITORING; MEASUREMENT ACCURACY; MODEL; SCREENING; SUPERNATANT; THERMOSTABILITY;

EID: 84941190883     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.201400227     Document Type: Article

References (35)

1. Chaiet, L., Wolf, F. J., The properties of streptavidin, a biotin-binding protein produced by streptomycetes. Arch. Biochem. Biophys. 1964, 106, 1-5.
2. Stapley, E. O., Mata, J. M., Miller, I. M., Demny, T. C. et al., Antibiotic MSD-235. I. Production by Streptomyces avidinii and Streptomyces lavendulae. Antimicrob. Agents Chemother. (Bethesda) 1963, 161, 20-27.
3. Sano, T., Vajda, S., Reznik, G. O., Smith, C. L. et al., Molecular engineering of streptavidin. Ann. N Y Acad. Sci. 1996, 799, 383-390.
4. Katz, B. A., Binding of biotin to streptavidin stabilizes intersubunit salt bridges between Asp61 and His87 at low pH. J. Mol. Biol. 1997, 274, 776-800.
5. González, M., Argarana, C. E., Fidelio, G. D., Extremely high thermal stability of streptavidin and avidin upon biotin binding. Biomol. Eng. 1999, 16, 67-72.
6. Skerra, A., Schmidt, T. G. M., Applications of a peptide ligand for streptavidin: The strep-tag. Biomol. Eng. 1999, 16, 79-86.
7. Szafranski, P., Mello, C. M., Sano, T., Smith, C. L. et al., A new approach for containment of microorganisms: Dual control of streptavidin expression by antisense RNA and the T7 transcription system. Proc. Natl. Acad. Sci. U S A 1997, 94, 1059-1063.
8. Kalofonos, H. P., Rusckowski, M., Siebecker, D. A., Sivolapenko, G. B. et al., Imaging of tumor in patients with indium-111-labeled biotin and streptavidin-conjugated antibodies: Preliminary communication. J. Nucl. Med. 1990, 31, 1791-1796.
9. Nguyen, V. A. T., Huynh, H. A., Hoang, T. V., Ninh, N. T. et al., Killed Bacillus subtilis spores expressing streptavidin: A novel carrier of drugs to target cancer cells. J. Drug Target. 2013, 21, 528-541.
10. Bayer, E. A., Kulik, T., Adar, R., Wilchek, M., Close similarity among streptavidin-like, biotin-binding proteins from Streptomyces. Biochim. Biophys. Acta 1995, 1263, 60-66.
11. Nordlund, H. R., Hytönen, V. P., Laitinen, O. H., Kulomaa, M. S., Novel avidin-like protein from a root nodule symbiotic bacterium Bradyrhizobium japonicum. J. Biol. Chem. 2005, 280, 13250-13255.
12. Helppolainen, S. H., Nurminen, K. P., Määttä, J. A. E., Halling, K. K. et al., Rhizavidin from Rhizobium etli: The first natural dimer in the avidin protein family. Biochem. J. 2007, 405, 397-405.
13. Pähler, A., Hendrickson, W. A., Kolks, M. A., Argarana, C. E. et al., Characterization and crystallization of core streptavidin. J. Biol. Chem. 1987, 262, 13933-13937.
14. Bayer, E. A., Ben-Hur, H., Hiller, Y., Wilchek, M., Postsecretory modifications of streptavidin. Biochem. J. 1989, 259, 369-376.
15. Sano, T., Pandori, M. W., Chen, X., Smith, C. L. et al., Recombinant core streptavidins. A minimum-sized core streptavidin has enhanced structural stability and higher accessibility to biotinylated macromolecules. J. Biol. Chem. 1995, 270, 28204-28209.
16. Hofmann, K., Wood, S. W., Brinton, C. C., Montibeller, J. A. et al., Iminobiotin affinity columns and their application to retrieval of streptavidin. Proc. Natl. Acad. Sci. U S A 1980, 77, 4666-4668.
17. Wu, S.-C., Wong, S.-L., Engineering of a Bacillus subtilis strain with adjustable levels of intracellular biotin for secretory production of functional streptavidin. Appl. Environ. Microbiol. 2002, 68, 1102-1108.
18. Wu, S.-C., Qureshi, M. H., Wong, S.-L., Secretory production and purification of functional full-length streptavidin from Bacillus subtilis. Protein Expr. Purif. 2002, 24, 348-356.
19. Nogueira, E. S., Schleier, T., Dürrenberger, M., Ballmer-Hofer, K. et al., High-level secretion of recombinant full-length streptavidin in Pichia pastoris and its application to enantioselective catalysis. Protein Expr. Purif. 2014, 93, 54-62.
20. Sano, T., Cantor, C. R., Expression of a cloned streptavidin gene in Escherichia coli. Proc. Natl. Acad. Sci. U S A 1990, 87, 142-146.
21. Kada, G., Falk, H., Gruber, H. J., Accurate measurement of avidin and streptavidin in crude biofluids with a new, optimized biotin-fluorescein conjugate. Biochim. Biophys. Acta 1999, 1417, 33-43.
22. Kada, G., Kaiser, K., Falk, H., Gruber, H. J., Rapid estimation of avidin and streptavidin by fluorescence quenching or fluorescence polarization. Biochim. Biophys. Acta 1999, 1427, 44-48.
23. Holmberg, A., Blomstergren, A., Nord, O., Lukacs, M. et al., The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures. Electrophoresis 2005, 26, 501-510.
24. Buranda, T., Jones, G. M., Nolan, J. P., Keij, J. et al., Ligand receptor dynamics at streptavidin-coated particle surfaces:A flow cytometric and spectrofluorimetric study. J. Phys. Chem. B 1999, 103, 3399-3410.
25. Chivers, C. E., Crozat, E., Chu, C., Moy, V. T. et al., A streptavidin variant with slower dissociation and increased mechanostability. Nat. Methods 2010, 7, 391-393.
26. Deng, L., Kitova, E. N., Klassen, J. S., Dissociation kinetics of the streptavidin-biotin Interaction measured during direct electrospray ionization mass spectrometry analysis. J. Am. Soc. Mass Spectrom. 2013, 24, 49-56.
27. Müller, J. M., Risse, J. M., Jussen, D., Flaschel, E., Development of fed-batch strategies for the production of streptavidin by Streptomyces avidinii based on power input and oxygen supply studies. J. Biotechnol. 2013, 163, 325-332.
28. Higgins, D. R., Cregg, J. M. (Eds.), Methods in Molecular Biology: Pichia protocols, Vol. 103, Humana Press, New York City 1998.
29. Hoops, S., Sahle, S., Gauges, R., Lee, C. et al., COPASI: A COmplex PAthway SImulator. Bioinformatics 2006, 22, 3067-3074.
30. Funahashi, A., Tanimura, N., Morohashi, M., Kitano, H., CellDesigner:A process diagram editor for gene-regulatory and biochemical networks. BIOSILICO 2003, 1, 159-162.
31. Scilab Enterprises, Scilab: Free and open source software for numerical computation (OS, Version 5.5.0), 2012.
32. Hunter, J. D., Matplotlib: A 2 D graphics environment. Comput. Sci. Eng. 2007, 9, 90-95.
33. Arrhenius, S., On the reaction rate of the inversion of non-refined sugar upon souring. Z. Phys. Chem. 1889, 4, 226-248.
34. Waner, M. J., Navrotskaya, I., Bain, A., Oldham, E. D. et al., Thermal and sodium dodecylsulfate induced transitions of streptavidin. Biophys. J. 2004, 87, 2701-2713.
35. Aslan, F. M., Yu, Y., Mohr, S. C., Cantor, C. R., Engineered single-chain dimeric streptavidins with an unexpected strong preference for biotin-4-fluorescein. Proc. Natl. Acad. Sci. U S A 2005, 102, 8507-8512.