Streptavidin mutants

Sano, Takeshi; Cantor, Charles R; Vajda, Sandor; Reznik, Gabriel O; Smith, Cassandra L; Pandori, Mark W

Title: Streptavidin mutants

Patent · Sat Jan 01 00:00:00 EST 2000

OSTI ID:872848

Sano, Takeshi ^[1]; Cantor, Charles R ^[2]; Vajda, Sandor ^[3]; Reznik, Gabriel O ^[4]; Smith, Cassandra L ^[2]; Pandori, Mark W ^[5]

1 Longfellow Pl. #2715, Boston, MA 02114
11 Bay State Rd. #6, Boston, MA 02215
8 Hillcrest Rd., Medfield, MA 02050
270 Babcock St., #7F, Boston, MA 02215
9605 Genesee Ave., #E2, San Diego, CA 92121

The present invention relates to streptavidin proteins and peptides having a altered physical properties such as an increased stability or increased or decreased affinity for binding biotin. The invention also relates to methods for the detection, identification, separation and isolation of targets using streptavidin proteins or peptides. Streptavidin with increased or reduced affinity allows for the use of the streptavidin-biotin coupling systems for detection and isolation systems wherein it is necessary to remove of one or the other of the binding partners. Such systems are useful for the purification of functional proteins and viable cells. The invention also relates to nucleic acids which encode these streptavidin proteins and peptides and to recombinant cells such as bacteria, yeast and mammalian cells which contain these nucleic acids.

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Research Organization:: Boston University

DOE Contract Number:: FG02-93ER61656

Assignee:: Sano, Takeshi (1 Longfellow Pl. #2715, Boston, MA 02114);Cantor, Charles R. (11 Bay State Rd. #6, Boston, MA 02215);Vajda, Sandor (8 Hillcrest Rd., Medfield, MA 02050);Reznik, Gabriel O. (270 Babcock St., #7F, Boston, MA 02215);Smith, Cassandra L. (11 Bay State Rd. #6, Boston, MA 02215);Pandori, Mark W. (9605 Genesee Ave., #E2, San Diego, CA 92121)

Patent Number(s):: US 6022951

OSTI ID:: 872848

Country of Publication:: United States

Language:: English

References (14)

A streptavidin-metallothionein chimera that allows specific labeling of biological materials with many different heavy metal ions. Sano, T.; Glazer, A. N.; Cantor, C. R. Proceedings of the National Academy of Sciences, Vol. 89, Issue 5 https://doi.org/10.1073/pnas.89.5.1534	journal	March 1992
[2] Introduction to avidin-biotin technology Wilchek, Meir; Bayer, Edward A. Avidin-Biotin Technology https://doi.org/10.1016/0076-6879(90)84256-G	book	January 1990
Oligonucleotide Arrays: New Concepts and Possibilities Chetverin, Alexander B.; Kramer, Fred Russell Bio/Technology, Vol. 12, Issue 11 https://doi.org/10.1038/nbt1194-1093	journal	November 1994
Molecular cloning and nucleotide sequence of the streptavidin gene Argarana, Carlos E.; Kuntz, Irwin D.; Birken, Steven Nucleic Acids Research, Vol. 14, Issue 4 https://doi.org/10.1093/nar/14.4.1871	journal	January 1986
Isolation of specific lymphocyte receptors by high-performance immunoaffinity chromatography Phillips, T. M.; Frantz, S. C. Journal of Chromatography A, Vol. 444 https://doi.org/10.1016/S0021-9673(01)94004-X	journal	July 1988
Expression vectors for streptavidin-containing chimeric proteins Sano, Takeshi; Cantor, Charles R. Biochemical and Biophysical Research Communications, Vol. 176, Issue 2, p. 571-577 https://doi.org/10.1016/S0006-291X(05)80222-0	journal	April 1991
Recombinant Core Streptavidins Sano, Takeshi; Pandori, Mark W.; Chen, Xiaomin Journal of Biological Chemistry, Vol. 270, Issue 47 https://doi.org/10.1074/jbc.270.47.28204	journal	November 1995
Expression of a cloned streptavidin gene in Escherichia coli. Sano, T.; Cantor, C. R. Proceedings of the National Academy of Sciences, Vol. 87, Issue 1 https://doi.org/10.1073/pnas.87.1.142	journal	January 1990
Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120. Chilkoti, A.; Tan, P. H.; Stayton, P. S. Proceedings of the National Academy of Sciences, Vol. 92, Issue 5 https://doi.org/10.1073/pnas.92.5.1754	journal	February 1995
Characterization and crystallization of core streptavidin. Pähler, A.; Hendrickson, W. A.; Kolks, M. A. Journal of Biological Chemistry, Vol. 262, Issue 29 https://doi.org/10.1016/S0021-9258(18)47884-2	journal	October 1987
Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors Zoller, Mark J.; Smith, Michael Recombinant DNA Part B, p. 468-500 https://doi.org/10.1016/0076-6879(83)00074-9	book	January 1983
Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site Gitlin, G.; Bayer, E. A.; Wilchek, M. Biochemical Journal, Vol. 256, Issue 1 https://doi.org/10.1042/bj2560279	journal	November 1988
A Streptavidin Mutant Containing a Cysteine Stretch That Facilitates Production of a Variety of Specific Streptavidin Conjugates Sano, Takeshi; Smith, Cassandra L.; Cantor, Charles R. Nature Biotechnology, Vol. 11, Issue 2 https://doi.org/10.1038/nbt0293-201	journal	February 1993
Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin. Sano, T.; Cantor, C. R. Proceedings of the National Academy of Sciences, Vol. 92, Issue 8 https://doi.org/10.1073/pnas.92.8.3180	journal	April 1995

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Title: Streptavidin mutants

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References (14)

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