Chimeric avidin mutants

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

Reexamination Certificate

active

11321685

ABSTRACT:
The present invention relates to new chimeric mutants of avidin protein with improved properties, e.g. thermostability, better stability against proteolysis, better charge properties (for example lower pl) compared to native avidin and avidin-related proteins, AVRs. The chimeric avidin mutants comprise mutants where a region or regions in avidin are substituted by a corresponding region or regions from an AVR protein.

REFERENCES:
patent: WO-2004/018509 (2004-03-01), None
Ahlroth et al., “Characterization and Chromosomal Localization of the Chicken Avidin Gene Family,”Animal Gen., 31:367-375 (2000).
Ahlroth et al., “Copy-Number Fluctuation by Unequal Crossing-Over in the Chicken Avidin Gene Family,”Biochem. and Biophy. Res. Comm., 288:400-406 (2001).
Backmann et al., “Thermodynamics and Kinetics of Unfolding of the Thermostable Trimeric Adenylate Kinase from the ArchaeonSulfolobus acidocaldarius,” J. Mol. Biol., 284:817-833 (1998).
Britton et al., “Structure Determination of the Glutamate Dehydrogenase from the HyperthermophileThermococcus litoralisand its Comparison with that fromPyrococcus furiosus,” J. Mol. Biol., 293:1121-1132 (1999).
Chilkoti et al., “Site-Directed Mutagenesis Studies of the High-Affinity Streptavidin-Biotin Complex: Contributions of Tryptophan Residues 79, 108, and 120,”Proc. Natl. Acad. Sci., 92:1754-1758 (1995).
Chu et al., “Thermodynamic and Structural Consequences of Flexible Loop Deletion by Circular Permutation in the Streptavidin-Biotin System,”Protein Sci., 7:848-859 (1998).
Clackson et al., “A Hot Spot of Binding Energy in a Hormone-Receptor Interface,”Science, 267:383-386 (1995).
Delano, “Unraveling Hot Spots in Binding Interfaces: Progress and Challenges,”Structural Bio., 12:14-20 (2002).
Eisenberg-Domovich et al., “High-Resolution Crystal Structure of an Avidin-Related Protein: Insight into High-Affinity Biotin Binding and Protein Stability,”Acta Cryst., 61:528-538 (2005).
Ellison et al., “Limited Proteolysis of Native Proteins: The Interaction Between Avidin and Proteinase K,”Protein Sci. 4:1337-1345 (1995).
Ferrin, et al., “The MIDAS Display System,”J. Mol. Graphics, 6:36-37 (1988). only figures.
González et al., “Extremely High Thermal Stability of Streptavidin and Avidin Upon Biotin Binding,”BioMolec. Eng., 16:67-72 (1999).
Green, “Avidin and Streptavidin,”Methods in Enzymology, 184:51-67 (1990).
Green, “Avidin,”Advances in Protein Chem., 29:85-133 (1975).
Hu et al., “Conservation of Polar Residues as Hot Spots at Protein Interfaces,”Proteins: Structure, Function, and Genetics, 39:331-342 (2000).
Hyre et al., “Ser45 Plays an Important Role in Managing Both the Equilibrium and Transition State Energetics of the Streptavidin-Biotin System,”Protein Sci., 9:878-885 (2000).
Hytönen et al., “Chicken Avidin-Related Protein 4/5 Shows Superior Thermal Stability when Compared with Avidin while Retaining High Affinity to Biotin,”J. Bio. Chem., 279:9337-9343 (2004).
Hytönen et al., “Design and Construction of Highly Stable, Protease-Resistant Chimeric Avidins,”J. Bio. Chem., 280:10228-10233 (2005).
Hytönen et al., “Efficient Production of Active Chicken Avidin Using a Bacterial Signal Peptide inEscherichia coli,” Biochem. J. 384:385-390 (2004).
Search Report for FI 20041705 dated Jun. 14, 2005.
Johnson et al., “Alignment and Searching for Common Protein Folds Using a Data Bank of Structural Templates,”J. Mol. Biol., 231:735-752 (1993).
Kannan et al., “Aromatic Clusters: a Determinant of Thermal Stability of Thermophilic Proteins,”Protein Eng., 13:753-761 (2000).
Klumb et al., “Energetic Roles of Hydrogen Bonds at the Ureido Oxygen Binding Pocket in the Streptavidin-Biotin Complex,”Biochemistry, 37:7657-7663 (1998).
Knapp et al., “Crystal Structure of Glutamate Dehydrogenase from the Hyperthermophilic EubacteriumThermotoga maritimaat 3.0 Å Resolution,”J. Mol. Biol., 267:916-932 (1997).
Laitinen et al., “Biotin Induces Tetramerization of a Recombinant Monomeric Avidin,”J. Bio. Chem., 276:8219-8224 (2001).
Laitinen et al., “Chicken Avidin-Related Proteins Show Altered Biotin-Binding and Physico-Chemical Properties as Compared with Avidin,”Biochem. J., 383:609-617 (2002).
Laitinen et al., “Mutation of a Critical Tryptophan to Lysine in Avidin or Streptavidin May Explain Why Sea Urchin Fibropellin Adopts an Avidin-Like Domain,”FEBS Letters, 461:52-58 (1999).
Livnah et al., “Three-Dimensional Structures of Avidin and the Avidin-Biotin Complex,”Proc. Natl. Acad. Sci., 90:5076-5080 (1993).
Marttila et al., “Engineering of Chicken Avidin: A Progressive Series of Reduced Charge Mutants,”FEBS Letters, 441:313-317 (1998).
Nardone et al., “Biochemical Characterization and Crystal Structure of a Recombinant Hen Avidin and its Acidic Mutant Expressed inEscherichia coli,” Eur. J. Biochem., 256:453-460 (1998).
Nordlund et al., “Enhancing the Thermal Stability of Avidin,”J. Bio. Chem., 278:2479-2483 (2003).
Sarkar et al., “The “Megaprimer” Method of Site-Directed Mutagenesis,” www.pubmed.gov, Biotechniques, 8 (1990).
Serrano et al., “Aromatic-Aromatic Interactions and Protein Stability,”J. Mol. Biol. 218:465-475 (1991).
Szilágyi et al., “Structural Differences Between Mesophilic, Moderately Thermophilic and Extremely Thermophilic Protein Subunits: Results of a Comprehensive Survey,”Structure, 8:493-504 (2000).
Thompson et al., “Transproteomic Evidence of a Loop-Deletion Mechanism for Enhancing Protein Thermostability,”J. Mol. Biol. 290:595-604 (1999).
Tuohimaa et al., “Development of Progestin-Specific Response in the Chicken Oviduct,”Int. J. Dev. Biol., 33:125-134 (1989).
Vetriani et al., “Protein Thermostability Above 100° C: A Key Role for Ionic Interactions,”Proc. Natl. Acad. Sci., 95:12300-12305 (1998).
Villeret et al., “The Crystal Structure ofPyrococcus furiosusOrnithine Carbamoyltransferase Reveals a Key Role for Oligomerization in Enzyme Stability at Extremely High Temperatures,”Proc. Natl. Acad. Sci., 95:2801-2806 (1998).
Wang et al., “Influence of the Carbohydrate Moiety on the Stability of Glycoproteins,”Am. Chem. Soc., 35:7299-7307 (1996).
Weber et al., “Structural Origins of High-Affinity Biotin Binding to Streptavidin,”Science, 243:85-88 (1989).
Wilchek et al., “Foreword and Introduction to the Book (Strept)Avidin-Biotin System,”Elsevier Sci., 16:1-4 (1999).
Wilchek et al., “Introduction to Avidin-Biotin Technology,”Methods in Enzymology, 184:5-13 (1990).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Chimeric avidin mutants does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Chimeric avidin mutants, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Chimeric avidin mutants will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3739618

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.