Recombinant production of biologically active peptides and prote

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

435 691, 4351723, C12P 2100

Patent

active

055893643

ABSTRACT:
The present invention relates to the recombinant production of amphiphilic peptides with biologically and therapeutically significant activities. In one embodiment, this invention relates to recombinantly producing an amphiphilic peptide by providing a protease-deficient microbial host transformed with an expression vector containing DNA that encodes the amphiphilic peptide under the control of a regulatory sequence operable in the microbial host and expressing the amphiphilic peptide in the transformed microbial host. In another embodiment, this invention relates to providing an E. coli protease-deficient K-12 cell transformed with a vector that expresses a cleavable fusion protein comprising at least part of a carbohydrate binding protein and the amphiphilic peptide in the cell, expressing the fusion protein in the cell, and cleaving the fusion protein to obtain the amphiphilic peptide substantially free of carbohydrate binding protein residues. The biologically active amphiphilic peptide so produced can be further treated chemically or enzymatically to obtain a chemically distinct amphiphilic peptide with improved biological and therapeutic properties.

REFERENCES:
patent: 5028530 (1991-07-01), Lai et al.
patent: 5104796 (1992-04-01), Keith et al.
patent: 5206154 (1993-04-01), Lai et al.
patent: 5264365 (1993-11-01), Georgiou et al.
Baneyx, F., et al. (1992) Ann. N. Y. Acad Sci. 665, 301-308.
K. Venema et al., "Mode of Action of LciA, the Lactococcin A Immunity Protein," Molecular Microbiology, 1994, pp. 521-532.
S. Taguchi et al., "Extracellular Production System of Heterologous Peptide Driven by a Secretory Protease Inhibitor of Streptomyces," Appl. Microbiol Biotechnol., 1992, pp. 749-753.
D. Alexander et al., "Isolation and Purification of a Biologically Active Human Platelet-Derived Growth Factor BB Expressed in Escherichia coli," Protein Expression and Purification, 1992, pp. 204-211.
N. Cardenas et al., "Expression and Characterization of Recombinant mts-1 Protein" (CA Abstract Only) from Bioorg. Khim. (1993) 19(4), pp. 420-426.
Ohta et al.; Mechanisms of Antibacterial Action of Tachyplesins and Polyphemusins, a Group of Antimicrobial Peptides Isolated from Horseshoe Crab Hemocytes; Antimicrobial Agents and Chemotherapy; vol. 36, No. 7; Jul. 1992; pp. 1460-1465.
Grodberg et al.; omp T Encodes the Escherichia coli Outer Membrane Protease That Cleaves T7 RNA Polymerase during Purification; Journal of Bacteriology; vol. 170, No. 3; Mar. 1988; pp. 1245-1253.
Hussain et al.; Expression of ricin B chain in Escherichia coli; FEBS Letters; vol. 244, No. 2; Feb. 1989; pp. 383-387.
Richardson et al.; The expression of functional ricin B-chain in Saccharomyces cerevisiae; Biochimica et Biophysica Acta. 950; 1988; pp. 385-394.
Handl et al; High Yield of Active STb Enterotoxin from a Fusion Protein (MBP-STb) Expressed in Escherichia coli; Protein Expression and Purification 4; 1993; pp. 275-281.
Bedouelle et al.; Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose; Eur. J. Biochem. 171; 1988; pp. 541-549.
Martineau et al.; Expression of heterologous peptides at two permissive sites of the Ma1E protein: antigenicity and immunogenicity of foreign B-cell and T-cell epitopes; Gene, 113; 1992; pp. 35-46.
Maina et al.; An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein; Gene, 74; 1988; pp. 365-373.
Clement et al.; Bacterial vectors to target and/or purify polypeptides; their use in immunological studies; Ann. Biol. Clin., 49; 1991; pp. 249-254.
Szmelcman et al.; Export and One-Step Purification from Escherichia coli of a Ma1E-CD4 Hybrid Protein That Neutralizes HIV In Vitro; Journal of Acquired Immune Deficiency Syndromes, 3; 1990; pp. 859-872.
di Guan et al.; Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein; Gene, 67; 1988; pp. 21-30.
Blondel et al.; Export and purifiction of a cytoplasmic dimeric protein by fusion to the maltose-binding protein of Escherichia coli; Eur. J. Biochem. 193; 1990; pp. 325-330.
Protein Fusion & Purification System Instruction Manual; New England BioLabs; Version 3.01; Revised Feb. 1993, pp. 1-37.
Casteels-Josson et al.; Apidaecin multipeptide precursor structure: a putative mechanism for amplication of the insect antibacterial response; The EMBO Journal, vol. 12, No. 4; 1993; pp. 1569-1578.
Elish et al.; Biochemical Analysis of Spontaneous fepA Mutants of Escherichia coli; Journal of General Microbiology, vol. 134; 1988; pp. 1355-1364.
Iwanaga; Primitive Coagulation Systems and their Message to Modern Biology; Thrombosis and Haemostasis; 70(1); 1993; pp. 48-55.
Kokryakov et al.; Protegrins: leukocyte antimicrobial peptides that combine features of cortiscostatic defensins and tachyplesins; FEBS Letters; vol. 327, No. 2; Jul. 1993; pp. 231-136.
Lama et al.; Expression of Poliovirus Nonstructural Proteins in Escherichia coli Cells; The Journal of Biological Chemistry; vol. 267, No. 22; Aug. 5, 1992; pp. 15932-15937.
Hellers et al., Expression and post-translational processing of preprocecropin A using a baculovirus vector; European Journal of Biochemistry; vol. 199; 1991; pp. 435-439.
Gunne et al.; Structure of preproattacin and its processing in insect cells infected with a recombinant baculovirus; European Journal of Biochemistry; vol. 187; 1990; pp. 699-703.
Lama et al.; Inducible expression of a toxic poliovirus membrane protein in Escherichia coli: Comparative studies using different expression systems based on T7 promoters; Biochemical and Biophysical Research Communications; vol. 188, No. 3; 1992; pp. 972-981.
Yee et al.; Recombinant protein expression in high cell density fed-batch cultures of Escherichia coli; Biotechnology, vol. 10; Dec. 1992; pp. 1550-1556.
Yee et al.; Recombinant Trypsin Production in High Cell Density Fed-Batch Cultures in Escherichia coli; Biotechnology and Bioengineering, vol. 41; 1993; pp. 781-790.
Wales et al.; Mutational Analysis of the Galactose Binding Ability of Recombinant Ricin B Chain; The Journal of Biological Chemistry, vol. 266, No. 29; Oct. 15, 1991; pp. 19172-19279.
Qoronfleh et al.; A Modified pET Vector that Augments Heterologous Protein Expression; Biotechnology Letters, vol. 15, No. 4; Apr. 1993; pp. 337-340.
Piers et al.; Recombinant DNA procedures for producing small anti-microbial cationic peptides in bacteria; Gene, vol. 134; 1993; pp. 7-13.
Bibi et al.; Functional expression of mouse mdr1 in Escherichia coli; Proc. Natl. Acad. Sci., vol. 90; Oct. 1993; pp. 9209-9213.
Sugimura et al.; Purification, Characterization, and Primary Structure of Escherichia coli Protease VII with Specificity for Paired Basic Residues: Identity of Protease VII and OmpT; Journal of Bacteriology, vol. 170, No. 12; Dec. 1988; pp. 5625-5632.
McIntosh et al.; Genetic and Physiological Studies on the Relationship Between Colicin B Resistance and Ferrienterochelin Uptake in Escherichia coli K-12; Journal of Bacteriology, vol. 137, No. 1; Jan. 1979; pp. 653-657.
Schein; Production of Soluble Recombinant Proteins in Bacteria; Biotechnology, vol. 7; Nov. 1989; pp. 1141-1149.

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

Recombinant production of biologically active peptides and prote does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Recombinant production of biologically active peptides and prote, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Recombinant production of biologically active peptides and prote will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-1141436

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