Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Amino acid sequence disclosed in whole or in part; or...
Reexamination Certificate
1998-05-01
2004-01-27
Nolan, Patrick J. (Department: 1644)
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Amino acid sequence disclosed in whole or in part; or...
C530S379000
Reexamination Certificate
active
06682738
ABSTRACT:
FIELD OF THE INVENTION
The present invention relates to proteins belonging to a novel class of proteins designated as &bgr;-expansins, a composition comprising such proteins, isolated polynucleotides encoding &bgr;-expansins, methods for using the polynucleotides and proteins of the invention and methods for identifying, isolating and purifying expansins, including &agr; and &bgr;-expansins.
BACKGROUND OF THE INVENTION
Many grasses, such as rye grass, Kentucky bluegrass and orchard grass, release prodigious quantities of wind-dispersed pollen that trigger hayfever, seasonal asthma and related immune reactions in humans. Up to 25% of adults suffer these allergic responses as a result of inhaling pollen-laden air. (Knox, B. et al., (1996)
Trends in Plant Science
1:156-164.) The major and most wide-spread allergenic component of grass pollen are the group I allergens. (Griffith, I., et al, (1991)
FEBS Lett
. 279:210-215; Perez, M., et al., (1990)
J. Biol. Chem
. 265:16210-16215; Esch, R. E. et al., (1989)
Mol. Immunol
. 26:557-561.) These are glycoproteins of about 30 kD that are quickly and profusely released by grass pollen upon hydration; in humans they bind to IgE antibodies to initiate the allergic response. Pollen from grasses contain one or more forms of these allergens, which are named after the source species, e.g. Lol pI is from
Lolium perenne
(rye grass), Ory sI is from
Oryza sativa
(rice), etc. Although the immunological aspects of these allergens, especially Lol pI, have been extensively studied, their biological function in the plant is unknown. Nevertheless, high sequence conservation among homologs in divergent grass species implies that they serve a vital biological function. (Xu, H. L., et al., (1995)
Gene
164:255-259; Broadwater, A. H., et al., (1993)
Gene
131:227-230.)
Recently, Shcherban et al. (Shcherban, T. Y., et al., (1995)
Proc. Natl. Acad. Sci. USA
, 92:9245-9249) noted that group I pollen allergens have a distant sequence similarity to expansins. Expansins are extracellular proteins that promote plant cell wall enlargement, evidently by disrupting noncovalent bonding between cellulose microfibrils and matrix polymers. (McQueen-Mason, S., et al. (1994)
Proc. Natl Acad. Sci. USA
91:6574-6578; McQueen-Mason, S. et al., (1992)
Plant Cell
4:1425-1433.) These previously described expansins are referred to in this specification as alpha-expansins. Applicant has now surprisingly discovered that the group I pollen allergens are structurally and functionally related to expansins and that they comprise a second family of expansins, &bgr;-expansins.
SUMMARY OF THE INVENTION
The present invention relates to &bgr;-expansins, including vegetative homologs of &bgr;-expansins, compositions thereof and isolated polynucleotides encoding the &bgr;-expansins of the invention. Beta-expansins, and polynucleotides encoding -expansins, of the invention may be of natural origin, isolated and purified or recombinatly produced. For purposes of the present invention, a “vegetative homolog” is defined as a &bgr;-expansin which is originally found in any plant part but pollen.
In one aspect, the invention relates to a polypeptide belonging to a class of &bgr;-expansins such as, for example, a group I grass pollen allergen and a vegetative &bgr;-expansin and compositions thereof.
In another aspect, the invention relates to a polynucleotide encoding the &bgr;-expansin of the invention, and a vector, a host cell and a transgenic plant comprising said polynucleotide.
In yet another aspect, the invention relates to a method of altering physical properties of the plant cell wall or any cell wall products derived from plant material, for example paper or textile.
In a further aspect, the invention relates to a method of identifying, isolating and purifying an expansin protein (including both &agr; and &bgr;-expansins) or a polynucleotide encoding such protein.
REFERENCES:
Skolnick et al. TISTECH, vol. 18, pp. 34-39, 2000.*
Brenner et al. PNAS vol. 95 pp 6073-6078 May 1998.*
Cosgrove, D.J. et al. Group I allergens of grass pollen as cell wall-loosening agents. Proc. Natl. Acad. Sci. U.S.A. 94:6559-6564, Jun. 1997*
Roitt, I.M. Encyclopedia of Immunology. Immunoglobulin Fold, E.A. Padlan, pp827-828. Immunoglobulin Gene Superfamily. P.J. Delves & I.M.Roitt. pp831-833. Academic Press, London, 1992.*
Shcherban, T.Y. Molecular cloning and sequence analysis of expansins—a highly conserved, multigene family of proteins that mediate cell wall extension in plants. Proc. Natl. Acad. Sci. U.S.A. 92:9245-9249, Sep. 1995.*
Perez, M. et al. cDNA cloning and immunological characterization of the rye grass allergen Lol P I. J. Biol. Chem. 265:16,210-16,215, Sep. 25, 1990.*
Merriam-Webster's Collegiate Dictionary. pp. 1027 and 1236, Springfield, MA, 1966.*
Sinnott, E.W. Botany: Principles and Problems. 2nd. Edition. McGraw-Hill, New York, 1929.*
Cosgrove, D.J. Characterization of long-term extension of isolated cell walls from growing cucumber hypocotyls. Planta 177:121-130, Feb. 28, 1989.*
Crowell, D.N. Cytokinin regulation of a soybean pollen allergen gene. Plant Mol. Biol. 25:829-835, Aug. 1994.*
McQueen-Mason, “Two Endogenous Proteins That Induce Cell Wall Extension in Plants,” The Plant Cell, American Society of Plant Physiologists, p. 1425-1433, (May 24, 1992).
Broadwater, “Zea ml, The Maize Homolog of the Allergen-Encoding Lol pl Gene of Rye Grass,” Gene, Slsevier Science Publishers, p. 227-230, (May 24, 1993).
Perez, “cDNA Cloning and Immunological Characterization of the Rye Grass Allergen Lol pl,” The J. of Biological Chemistry, the American Society for Biochemistry and Molecular Biology, Inc., vol. 265 (No. 27), p. 16210-15, (May 24, 1990).
Griffith, “Cloning and Sequencing of Lol pl, The Major Allergenic Protein of Rye-Grass Pollen,” Federation of European Biochemical Societies, Elsevier Science Publishers, vol. 279 (No. 2), p. 210-21, (May 24, 1991).
Staff, “Cellular Localization of Water Soluble, Allergenic Proteins in Rye-Grass (Lolium Perenne) Pollen Using Monoclonal and Specific IgE Antibodies with Immunogold Probes.” Histochemical Journal, Chapman and Hall Ltd., p. 276-290, (May 24, 1990).
Esch, “Identification and Localization of Allergenic Determinants On Grass Group I Antigens Using Monoclonal Antibodies,” The J. of Immunology, The American Association of Immunologists, vol. 142 (No. 1), p. 179-184, (May 24, 1989).
McQueen-Mason, “Expansin Mode of Action On Cell Walls,” Plant Physiology, p. 87-100, (May 24, 1995).
Knox, “Pollen Allergens: Development and Function,” Sex Plant Reproduction, Springer-Verlag, p. 318-323, (May 24, 1996).
Knox, “Environmental and Molecular Biology of Pollen Allergens,” Trends in Plant Science, Elsevier Science Ltd., vol. 1 (No. 5), p. 156-164, (May 24, 1996).
Heslop-Harrison, “The Pollen-Stigma Interaction In the Grasses,” Acta Botany Neerl., vol. 33 (No. 1), p. 81-99, (May 24, 1984).
Smith, “Molecular Characterization of Group I Allergens of Grass Pollen,” Pollen Biotechnology, p. 125-143.
Heslop-Harrison, “The Pollen-Stigma Interaction In the Grasses,” Acta Bot. Neel., p. 193-211, (May 24, 1985).
Wu, “Growth Maintenance Of the Maize Primary Root At Low Water Potentials Involves Increase In Cell-Wall Extension Properties, Expansin Activity, and Wall Susceptibility to Expansins,” Plant Physiology, p. 765-772, (May 24, 1996).
Cosgrove, “Role of Expansin In Cell Enlargement of Oat Coleoptiles,” Plant Physiology, p. 1321-1328, (May 24, 1993).
Shcherban, “Molecular Cloning and Sequence Analysis of Expansins—A Highly Conserved, Multigene Family of Proteins That Mediate Cell Wall Extension In Plants,” Plant Biology, Proc. Natl. Acad. Sci., p. 9245-9249, (May 24, 1995).
McKee Voorhees & Sease, P.L.C.
Nolan Patrick J.
The Penn State Research Foundation
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