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United States Patent (19. 11 Patent Number: 5,633,451 Duman 45 Date of Patent: May 27, 1997

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United States Patent (19. 11 Patent Number: 5,633,451 Duman 45 Date of Patent: May 27, 1997 IIIIUS005633451A United States Patent (19. 11 Patent Number: 5,633,451 Duman 45 Date of Patent: May 27, 1997 54 TRANSGENIC PLANT'S HAVING ANUCLEIC J. G. Duman et al., "Adaptations of insects to subzero ACID SEQUENCE ENCODING A temperatures”, Quart. Rev. Biol. 66, (4) PP. 387-410 (1991). DENDRODESANT FREEZE PROTEN J. G. Duman et al., "Hemolymph Proteins involved in the 75) Inventor: John G. Duman, South Bend, Ind. cold tolerance of terrestrial arthropods: Antifreeze and Ice Nucleator Proteins”. In Water and Life, Springer-Verlag, 73 Assignee: University of Notre Dame du Lac, Chapters 17 & 18 pp. 282-315, (1992). Notre Dame, Ind. J. G. Duman et al., "Thermal hysteresis proteins", Advances in Low Temperature Biology, vol. 2, pp. 131-182, (1993). 21) Appl. No.: 569,594 D. Tursman et al., "Cryoprotective effects of Thermal Hys 22 Filed: Dec. 8, 1995 teresis Protein on Survivorship of Frozen Gut Cells from the Freeze Tolerant Centipede Lithobius forficatus”, Journal of Related U.S. Application Data Experimental Zoology, vol. 272, pp. 249-257 (1995). 62) Division of Ser. No. 485,359, Jun. 7, 1995. D. W. et al., "Activation of antifreeze proteins from larvae 151 Int. Cl. ................. A01B 1/00; A01 H 1/06; of the beetle Dendroides canadensis". Comp. Physiol. B, A01B 5/10; A01G 13/00; C12N 5/04; C12N 15/82 vol. 161, pp. 279-283 (1991). 52 U.S. Cl. ......................... 800/205; 800/250; 435/69.1; D. W. Wu et al., "Purification and characterization of anti 435/419; 536/23.5 freeze proteins from larvae of the beetle Dandroides (58) Field of Search ................................. 800/205, 250; canadensis”, Comp. Physiol. B., vol. 161, pp. 271-278 435/69.1, 240.4; 536/23.5 (1991). 56) References Cited Primary Examiner-David T. Fox U.S. PATENT DOCUMENTS Assistant Examiner Thomas Haas 5,118,792 6/1992 Wanten et al. .......................... 530/350 Attorney, Agent, or Firm-Barnes & Thornburg OTHER PUBLICATIONS 57 ABSTRACT Wu, D.W. (1991) "Struture-function relationships of insect The present invention is directed to transgenic plants having antifreeze proteins" Diss. Abstr; Intl. 52(04B);2014. nucleic acid sequences encoding Dendroides canadensis J. G. Duman et al., "Hemolymph proteins involved in insect thermal hysteresis proteins. The THPs of Dendroides have subzero temperature tolerance:Ice nucleators and antifreeze significantly greater thermal hysteresis activity than any proteins”. In Insects at Low Temperatures, Chapman and other known anti-freeze protein. The thermal hysteresis Hall, pp. 94-127 (1991). activity of the purified THPs can be further enhanced by D. W. Wu et al., “Enhancement of insect antifreeze protein combining the THPs with various "activating” compounds. activity by antibodies”, Biochem. Biophys. Acta 1076, 416–420 (1991). 1 Claim, 5 Drawing Sheets U.S. Patent May 27, 1997 Sheet 1 of 5 5,633,451 3. HysteresisThermal (oC) O 2O 4O 6O 8O Protein Concentration (mg/ml) O 4O 8O 2O 6O AFP (mg/ml) U.S. Patent May 27, 1997 Sheet 3 of 5 5,633,451 O 2, 2 as 2 2. Z as u/ C / Dr O H m Hum m H CO 9 U 9 U U U 9 U N C / CC WMA:)X! ATÅW NOILISOd ?5Z 0BHÅO50 0S81A ON.d.HW.1 0NITW1 ONH3W1 OX'ÄX\!1 0B\\-\|1 5X\!1 0d C CO 9 fa TVN?ISaqI.Ld3d NIWH31(£)Sn U.S. Patent May 27, 1997 Sheet 4 of 5 5,633,451 80 Percent 60 Survival 40 20 O - 30 - 25 - 2 O - 15 - 1 O - 5 O Temperature (C) A76, 52. 8O 60 Percent Survival 0 20 O - 30 - 25 - 20 - 15 - 1 O - 5 O Temperature (C) 7F/( 5Ab Y 80 Percent 60 Survival 40 20 - 30 - 25 - 20 - 15 - 1 O - 5 O Temperature (C) At 7 ( 5d. U.S. Patent May 27, 1997 Sheet 5 of 5 5,633,451 80 Percent 60 Survival 40 20 - 30 - 25 Temperature- 20 - 15 - 10(C) - 5 O Af/0, 547 80 Percent 60 Survival 40 20 - 3 O - 25 - 20 - 5 - 10 - 5 O Temperature (C) 5,633,451 1. 2 TRANSGENC PLANT'S HAVING ANUCLEC terized as having higher percentages of hydrophilic amino ACID SEQUENCE ENCODING A acids (i.e. Thr, Ser, ASX, Glx, Lys, Arg) than the fishTHPs, DENDRODESANT FREEZE PROTEIN with generally 40-50 mol% of the residues being capable of forming hydrogen bonds. This is a division of application Ser. No. 08/485,359, filed Jun. 7, 1995. TABLE 1. BACKGROUND OF THE INVENTION Amino acid compositions (mol%) of representative THPs. Species from a broad phylogenetic range of insects have been reported to produce thermal-hysteresis proteins 10 Amino 1. 2 2 (THPs). THPs are believed to play an important role in many acid (H-1) T4 T3 3 4 plant and animal species' ability to Survive exposure to ASX 14.3 7.3 5.3 9.5 7.1 subzero temperatures. By definition, the equilibrium melting Thr 17.2 6.6 2.3 6.0 2.7 and freezing points of water are identical. However, the Ser 10.3 7.4 11. 13.0 30.5 15 Glx 5.2 8.9 12.4 110 12.3 presence of thermal-hysteresis proteins lowers the non Pro 2.6 5.9 0.0 5.0 0.0 equilibrium freezing point of water without lowering the Gly 6.6 8.3 11.4 150 200 melting point (equilibriumfreezing point). Thus when THPs Ala 8.4 14.3 5.0 8.0 6.8 are added to a solution they produce a difference between the %Cys 15.9 O.O 28.0 6.0 0.0 freezing and melting temperatures of the solution, and this Val 17 11.5 2.3 3.0 3.0 20 Met 0.2 48 0.0 0.0 0.0 difference has been termed "thermal-hysteresis”. le 1.5 7. 1.0 1.2 19 In the absence of THPs a small (about 0.25 mm diameter) Leu. 19 0.0 2.2 6.5 3.1 Lys 3.4 6.8 15.4 3.1 7.5 ice crystal that is about to melt at the melting point tem Arg 4.8 2.6 0.0 8.0 0.0 perature will normally grow noticeably if the temperature is Tyr 3.9 2.3 0.0 1.0 2.0 lowered by 0.01° to 0.02°C. However, if THPs are present, Phe 0.0 3.9 0.0 2.2 1.1 the temperature may be lowered as much as 5° to 6° C. 25 His 19 19 3.1 0.0 2.3 below the melting point (depending upon the specific activ 1 = Dendroides canadensis; ity and concentration of the proteins present) before notice 2 = Tenebrionolitor, able crystal growth occurs. Consequently, because of THPs 3 = Choristoneura famiferana; ability to lower the freezing point of aqueous solutions, they 4 = Oncopeltus fasciatus are commonly referred to as antifreeze proteins. THPS lower 30 the freezing point of aqueous solutions via a non-colligative Several of the insect THPs have significant amounts of mechanism that does not depress the vapor pressure or raise cysteine. In particular 16 mole % of the amino acid residues the osmotic pressure of water, as is the case with colligative of the THPs of D. canadensis are cysteine, approximately type antifreezes such as glycerol. half of which are involved in disulfide bridges. Treatment Anti-freeze proteins are believed to exert their effect by 35 with dithiothreitol, which reduces these disulfide bonds, or adsorbing onto the surface of potential seed crystals via alkylation of free sulfhydryls, results in complete loss of hydrogen bonding. When anti-freeze proteins adsorb onto thermal-hysteresis activity. the ice surface they interfere with the addition of water The thermal-hysteresis activity present in the hemolymph molecules and force growth of the crystal into many highly (the circulatory fluid of insects) of Dendroides canadensis curved fronts with high surface free energy. Consequently, 40 insects in mid-winter averages 3-6°C. with some individu growth of the crystal requires the temperature to be further als having as much as 8-9 C. This activity is significantly lowered to allow crystal growth to proceed. greater than that which is present in the blood of polar fish; the maximal activity achievable with very high concentra Thermal-hysteresis proteins were first discovered, and tions of the fishTHPs is about 1.7°C. FIG. 1 compares the have been best studied, in marine teleost fishes inhabiting 45 activities of purified THPs from two species of fish and two seas where subzero temperatures occur, at least seasonally. species of insects: 1=Dendroides canadensis THP, the most In these THP-producing Antarctic fish an ice crystal present active THP currently known (solid squares); 2=Tenebrio in the blood serum that melts at -1.1° C., will fail to grow molitorTHP (solid circles);3=activity of the most active fish in size until the temperature is lowered to -2.5°C. (thermal THP, i.e. Antarctic eelpout and THP of Antarctic nototheni hysteresis=1.4° C). Thus the fish is protected from freezing SO ids (open squares); 4=activity of the least active fish THP, in its ice-laden -1.86 C. seawater environment. from cod Gadus morhua (open circles). The maximal activ Over the last 15 years it has been demonstrated that many ity of the most active fish and Tmolitor THPs are similar, insects and other terrestrial arthropods (including certain however, the THPs of D. canadensis have a greater specific spiders, mites, and centipedes) also produce thermal activity and a much greater maximal activity than any other hysteresis proteins.
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