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Download File US005633451A ‘ United States Patent 1191 [11] Patent Number: 5,633,451 Duman [45] Date of Patent: May 27, 1997 [54] TRANSGENIC PLANTS HAVING A NUCLEIC J. G. Duman et al., “Adaptations of insects to subzero ACID SEQUENCE ENCODING A temperatures”, Quart. Rev. Biol. 66, (4) PP. 387-410 (1991). DENDROlDES ANTIFREEZE PROTEIN 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 for?catus”, Journal of Related US. 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 of the beetle Dendroides canadensis”, Comp. Physiol. B, [51] Int. Cl.6 ............................. .. A01H 1/00; A01H 1/06; vol. 161, pp. 279-283 (1991). A01H 5/10; A01G 13/00; C12N 5/04; C12N 15/82 [52] US. Cl. ....................... .. 800/205; 800/250; 435/69.1; D. W. Wu et al., “Puri?cation and characterization of anti 435/419; 536/235 freeze proteins from larvae of the beetle Dandroides [58] Field of Search ................................... .. 800/205, 250; canadensis”, Comp. Physiol. B, vol. 161, pp. 271-278 435/691, 2404; 536/235 (1991). [56] References Cited Primary Examiner-David T. Fox U.S. PATENT DOCUlVIENTS Assistant Examiner—Thomas Haas 5,ll8,7% 6/1992 Warren et a1. ........................ .. 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 anti?eeze proteins” Diss. Abstr. Intl. 52(04-B):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 signi?cantly 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 puri?ed 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 US. Patent May 27, 1997 Sheet 1 of 5 5,633,451 3 l 2 HysTeresisThermal . I". ' 3 2 (0C) '- _.....- "'bt/0o~.¢. 1- Mr". O I I l | I 0 2o_ 40 so so Pro’rem Concentration (mg/ml) TH (°C) 0 4O 80 I20 I60 AFP (mg/ml) US. Patent May 27, 1997 Sheet 4 of 5 5,633,451 80' Percent 60~ Survival 40: 20‘ 0- | | I.1 1 I ~30 -25 -2O -15 -10 -5 0 Temperature (C) F142 5m 80: P t 60" ercen ' Survival 40: 20“ l l 0 . ~30 ~25 -20 --15 ,-1O -5 0 Temperature (Cl FIG 5% 80“ Percent 60? Survival 40-_ 20“ -30 -25 -20 -15 -10 -5 0 Temnerature (Ci F1651‘ US. Patent May 27, 1997 Sheet 5 0f 5 5,633,451 Percent - Survival 40 -30 -25 -20 715 -10 -5 0 Temperature (C) F16. 5d Percent - - Survival 40'. -30 -25 -20 -15 -10 -5 0 Temperature (C) FIG 5a? 5 ,633,451 1 2 TRANSGENIC PLANTS HAVING A NUCLEIC terized as having higher percentages of hydrophilic amino ACID SEQUENCE ENCODING A acids (i.e. Thr, Ser, Asx. Glx. Lys, Arg) than the ?sh THPs, DENDROIDES ANTIFREEZE 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, ?led 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 (l-I-l) T-4 T-3 3 4 plant and animal species’ ability to survive exposure to A5): 14.3 7.3 5.3 9.5 7.1 subzero temperatures. By de?nition. the equilibrium melting 'Ilrr 17.2 6.6 2.3 6.0 2.7 and freezing points of water are identical. However, the Ser 10.3 7.4 11.1 13.0 30.5 presence of thermal-hysteresis proteins lowers the non Glx 5.2 8.9 12.4 11.0 12.3 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 15.0 20.0 melting point (equilibrium freezing point). Thus when THPs Ala 8.4 14.3 5.0 8.0 6.8 are added to a solution they produce a di?’erence between the VzCys 15.9 0.0 28.0 6.0 0.0 freezing and melting temperatures of the solution, and this Val 1.7 11.5 2.3 3.0 3.0 Met 0.2 4.8 0.0 0.0 0.0 20 diiference has been termed “thermal-hysteresis”. He 1.5 7.1 1.0 1.2 1.9 In the absence of THPs a small (about 0.25 mm diameter) Len 1.9 0.0 2.2 6.5 3.1 ice crystal that is about to melt at the melting point tem Lys 3.4 6.8 15.4 3.1 7.5 Arg 4.8 2.6 0.0 8.0 0.0 perature will normally grow noticeably if the temperature is 'Iyr 3.9 2.3 0.0 1.0 2.0 lowered by 001° to 002° 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 1.9 1.9 3.1 0.0 2.3 below the melting .point (depending upon the speci?c activ l = Dendroides canadensis; ity and concentration of the proteins present) before notice 2 = Tenebn'a molizar, able crystal growth occurs. Consequently, because of THPs 3 = Chon'staneura ?lmzferana; ability to lower the freezing point of aqueous solutions. they 4 = Oncapelrusfasciatu: 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 signi?cant amounts of mechanism ?rat 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 disul?de bridges. Treatment Anti-freeze proteins are believed to exert their etfect by 35 with dithiothreitol, which reduces these disul?de bonds, or adsorbing onto the surface of potential seed crystals via alkylation of free sulthydryls, 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 ?uid of insects) of Dendroides canadensis curved fronts with high surface free energy. Consequently, 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 signi?cantly lowered to allow crystal growth to proceed. greater than that which is present in the blood of polar ?sh; Thermal-hysteresis proteins were ?rst discovered, and the maximal activity achievable with very high concentra have been best studied, in marine teleost ?shes inhabiting tions of the ?sh THPs is about 1.7° C. FIG. 1 compares the 45 activities of puri?ed THPs from two species of ?sh and two seas where subzero temperatures occur. at least seasonally. In these THP-producing Antarctic ?sh an ice crystal present species of insects: l=Dendroides canadensis THP, the most in the blood serum that melts at —1.1° C., will fail to grow active THP currently known (solid squares); 2=Tenebri0 in size until the temperature is lowered to —2.5° C. (thermal molitor THP (solid circles); 3=activity of the most active ?sh hysteresis=1.4° C.). Thus the ?sh is protected from freezing THP, i.e. Antarctic eelpout and THP of Antarctic nototheni in its ice-laden —1.86° C. seawater environment. ids (open squares); 4=activity of the least active ?sh THP, 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 ?sh and T molitor THPs are similar. insects and other terrestrial arthropods (including certain however, the THPs of D. canadensis have a greater speci?c spiders, mites, and centipedes) also produce thermal activity and a much greater maximal activity than any other hysteresis proteins. Low levels of thermal hysteresis activity 55 known THP. In addition as will be described later, the are also quite common in overwintering plants and are Dendroides canadensis TI-[Ps can be activated by the pres present in certain fungi and bacteria.
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