Co-expression of recombination proteins

Details Co-expression of recombination proteins Co-expression of recombination proteins

2006-03-21

2006-03-21

Housel, James C (Department: 1648)

Chemistry: molecular biology and microbiology

Vector, per se

C435S069100, C435S069300, C536S023100, C536S023200, C536S023700

Reexamination Certificate

active

07015033

ABSTRACT:
Expression vectors are described which permit the recombinant expression of proteins which essentially contain, in addition to nucleic acid encoding the recombinant protein, nucleic acid encoding a non-proteolytic analog ofHaemophilusHin47 protein, with or without leader sequence, or nucleic acid encoding high molecular weight proteins of non-typeableHaemophilus, which are hmwB, hmwC or hmwBC.

REFERENCES:
patent: 5474914 (1995-12-01), Spaete
patent: 5506139 (1996-04-01), Loosmore et al.
patent: 5656436 (1997-08-01), Loosmore et al.
patent: 5869302 (1999-02-01), Loosmore et al.
patent: 5876733 (1999-03-01), Barenkamp
patent: 5935573 (1999-08-01), Loosmore et al.
patent: 5939297 (1999-08-01), Loosmore et al.
patent: 5981503 (1999-11-01), Loosmore et al.
patent: 6025342 (2000-02-01), Loosmore et al.
patent: 6147057 (2000-11-01), Loosmore et al.
patent: 6335182 (2002-01-01), Loosmore et al.
patent: 6361969 (2002-03-01), Galeotti
patent: WO 96/03506 (1996-02-01), None
patent: WO 96/30519 (1996-10-01), None
patent: WO 99 10375 (1998-08-01), None
Bass et al., “Multicopy Suppressors of Pre MutantEscherichia coliInclude Two HtrA (DegP) Protease Homologs (HhoAB), DksA, and a Truncated RlpA,” J. Bacteriology, 178:1154-61 (1996).
Watson et al. REcombinat DNA, W.H> freeman and Co., New York, 1992.
Bowie et al., Deciphering the Message in Protein Sequences: Tolerance to Amino Acid Substitutions, Science, vol. 247(4948), pp. 1306-1310 (1990).
Spiess et la., Cell, vol. 97, pp. 339-347 (Apr. 1999).
Faccio et al., The Journal of Biological Chemistry, vol. 275 No. 4, pp. 2581-2588 (Jan. 2000).
Stedman's Online Medical Dictionary, 27thEdition, defintion of “analog”, www. stedmans.com.
Bluestone, C.D. (1982) Current concepts in otolaryngology. Otitis media in children: to treat or not to treat? N. Engl. J. Med. 30: 1399-1404.
Loosmore, S.M., Yang, Y-P., Oomen, R., Shortreed, J.M., Coleman, D.C., and Klein, M.H. (1998) TheHaemophilus influenzaeHtrA protein is a protective antigen. Immun. 66:899-906.
Pallen, M.J. and Wren, B.W. (1997) The HtrA family of serine proteases. Molec. Microbiol. 26:209-221.
Barenkamp, S.J. and Bodor, F.F. (1990) Development of serum batericidal activity following nontypableHaemophilus influenzaeacute otitis media. Pediatr. Infect. Dis. 9:333-339.
St. Geme, III, J.W., Kumar, V.V., Cutter, D., and Barenkamp, S.J. (1993) High-molecular-weight proteins of nontypeableHaemophilus influenzaemediate attachment to human epithelial cells. Proc. Natl. Acad. Sci. USA 90:2875-2879.
Barenkamp, S.J. (1996) Immunization with high-molecular-weight adhesion proteins of nontypeableHaemophilus influenzaemodifies experimental otitis media in chinchillas. Infect. Immun. 64:1246-1251.
St. Geme III, J.W. and Grass, S. (1998) Secretion of theHaemophilus influenzaeHMW1 and HMW2 adesins ainvokves a periplasmic intermediate and requires the HMWB and HMBC proteins. Molec. Microbiol. 27:617-630.
Barenkamp, S.J. and St. Geme III, J.W. (1996) Identification of a second family of high-molecular-weight adhesion proteins expressed by non-typableHaemophilus influenzae. Molec. Microbiol. 19:1215-1223.
St. Geme III, J,W,, Cutter, D., and Barenkamp., S.J. (1996) Characterization of the genetic locus encodingHaemophilus influenzaetype b surface fibrils. J. Bact. 178:6281-6287.
Laemmil, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
St. Geme III (2001) The Pathogenesis of nontypableHaemophilus influenzaeotitis media, Vaccine 19, S41-S50.
Andrew Hayhurst and William . Harris (1999),Escherichia coliSkp Chaperone Coexpression Improves Solubility and Phage Display of Single-Chain antibody Fragments, Protein Expression and Purification 15, 336-343.
Ellis, J. (1987) Proteins as molecular chaperones. Nature 328:378-379.
Barenkamp, S.J. and St. Geme III, J,W, (1994) Genes encoding high-molecular-weight adhesion proteins of nontypeableHaemophilus influenzaeare part of gene clusters. Infect. Immun. 62:3320-3328.
Talkington, D.F., Brown, B.G., Tharpe, J.A., Koenig, A., and Russell, H. (1996) Protection of mice against fatal pneumococcal challenge by immunization with pneumococcal surface adhesin A (PsaA). Microb. Pathog. 21:17-22.
Caspers, P., Stieger, M., and Burn, P. (1994) Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases inEscherichia coli. Cell Mol Biol (Noisy-le-grand) 40(5):635-44.
Nishihara, K., Kanemori, M., Kitagawa, M., Tanagi, H., and Yura, T. (1998) Chaperone coexpression plasmids: differential and synergistic roles of DnaK-Dna-GrpEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, inEscherichia coli. Appl. Environ Microbiol 64(5):1694-9.
Crowl, R. et al., (1985) Versatile expression vectors for high-level synthesis of cloned gene products inEscherichia coli, Gene, 38:31-38.
Lobigs M, Chelvanayagam G, Müllbacher, A, “Proteolytic processing of peptides in the lumen of the endoplasmic reticulum for antigen presentation by major histocompatibility class I”, Eur. J. Immunol., vol. 30, pp. 1496-1506 (May 2000).
Bernstein HD, “The biogenesis and assembly of bacterial membrane proteins”, Current Opin. Microbiol., vol. 3, No. 2, pp. 203-209 (Apr. 2000).
Poquet I, Saint V, Seznec E, Simoes N, Bolotin A, Gruss A, “HtrA is the unique surface housekeeping protease inLactococcus lactisand is required for natural protein processing”, Mol. Microbiol., vol. 35, No. 5, pp. 1042-1051 (Mar. 2000).
Noone D, Howell A, Devine KM, “Expression of ykdA, encoding aBacillus subtilishomologue of HtrA, is heat shock inducible and negatively autoregulated”, J. Bacteriol., vol. 182, No. 6, pp. 1592-1599 (Mar. 2000).
Fakruddin JM, Biswas S, Sharma YD, “Metalloprotease activity in a small heat shock protein of the human malaria parasite Plasmodium vivax”, Infection and Immunity, vol. 68, No. 3, pp. 1202-1206 (Mar. 2000).
Kim KI, Park SC, Kang SH, Cheong GW, Chung CH, “Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein inEscherichia coli”, J. Mol. Biol., vol. 294, pp. 1363-1374 (Dec. 1999).
Forsdyke DR, “Heat shock proteins as mediators of aggregation-induced ‘danger’ signals: implications of the slow evolutionary fine-tuning of sequences for the antigenicity of cancer cells”, Cell Stress & Chaperones, vol. 4, No. 4, pp. 205-210 (Dec. 1999).

Affiliated with

Also associated with

Rating

Co-expression of recombination proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Co-expression of recombination proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Co-expression of recombination proteins will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3561186