Genome coding phytolacca antiviral protein and a recombinant expression vector therefor

Patent 5723326 Issued on March 3, 1998. Estimated Expiration Date:

June 6, 2015. Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.

Abstract Claims Description Full Text

Inventors

Assignee

Jinro Limited

Application

No. 471564 filed on 06/06/1995

US Classes:

435/199, Ribonuclease (3.1.4)435/69.1, Recombinant DNA technique included in method of making a protein or polypeptide435/69.2, Enzyme inhibitors or activators435/320.1, VECTOR, PER SE (E.G., PLASMID, HYBRID PLASMID, COSMID, VIRAL VECTOR, BACTERIOPHAGE VECTOR, ETC.) BACTERIOPHAGE VECTOR, ETC.)530/370, Plant proteins, e.g., derived from legumes, algae or lichens, etc.530/379, Derived from leafy green plants, e.g., alfalfa pollen, etc.536/23.2, Encodes an enzyme536/23.6Encodes a plant polypeptide

Examiners

Primary: Wax, Robert A.
Assistant: Prouty, Rebecca E.

Attorney, Agent or Firm

Darby & Darby

International Classes

C12N 009/22
C07K 014/415

Foreign Application Priority Data

1993-08-28 KR

Abstract

The present inventors discovered a novel genome coding Phytolacca insularis antiviral protein(PIP) isolated from Phytolacca insularis Nakai; and developed a recombinant vector for said PIP genome expression and a microorganism transformed therewith. PIP genome of the present invention has nucleotide homology of about 82%, compared with the genome of Phytolacca americana antiviral protein isolated from Phytolacca americana L., which is closely related to the Phytolacca insularis Nakai. PIP cDNA is consist of 918 bp of one open reading frame and termination codon; and polyadenylation signal which is ubiquitous in mRNA of most plants and animals, appears to be located in the upstream of 33 bp from the polyadenylation site. Recombinant PIP of the invention was proved to inhibit the growth of E. coli HB101 transformed with said expression vector.

Other References

J.D. Irvin -- Purification and Partial Characterization of the Antiviral Protein from Phytolacca americana which inhibits Eukaryotic Protein Synthesis; Arch. Biochem. Biophys., 169, 522-528 (1975)
K.C. Halling et al. -- Genomic Cloning and Characterization of a Ricin Gene from Ricinus communis; Nucleic Acid Res., 13, 8019-8033 (1985)
J. Katoaka et al. -- DNA Sequence of Mirabilis Antiviral Protein (MAP), a Ribosome-inactivating Protein with an Antiviral Property, from Mirabilis jalapa L. and Its Expression in Escherichia coli; J. Biol. Chem., 266, 8426-8430 (1991)
X. Zhang et al. -- Homology of Trichosanthin and Ricin A Chain; Nature, 321, 477-478 (1986)
Y.Endo et al. -- The RNA N-Glycosidase Activity of Ricin A-Chain; J. Biol. Chem., 263, 8735-8739 (1988)
J.D. Irvin et al. -- Purification and Properties of a Second Antiviral Protein from Phytolacca americana Which inactivates Eukaryotic Ribosomes: Arch. Biochem. Biophys., 200, 418-425 (1980)
B. Jansen et al. -- Establishment of a Human t(4;11) Leukemia in Severe Combined Immunodeficient Mice and successful Treatment Using Anti-CD19 (B43)-Pokeweed Antiviral Protein Immunotoxin; Cancer Res., 52, 406-412 (1992)
Y.W. Kim et al. -- Immunoconjugates That Neutralize HIV Virions Kill T cells infected with Diverse Strains of HIV-1: J.Immunol., 144, 1257-1262 (1990)
D.E. Myers et al. -- Production of a Pokeweed Antiviral Protein(PAP)-containing Immunotoxin, B43-PAP, Directed Against the CD19 Human B Lineage Lymphoid Differentiation Antigen in Highly Purified Form for Human Clinical Trails; J. Immunol. Methods, 136, 221-238 (1991)
M.P. Ready et al. -- Extracellular Location of Pokeweed Antiviral Protein; Proc. Natl. Acad. Sci. USA, 83, 5053-5056 (1986)
Q. Lin et al. -- Isolation and characterization of a cDNA Clone Encoding the Anti-viral Protein from Phytolacca americana; Plant Mol. Biol., 17, 609-614 (1991