Chemistry: molecular biology and microbiology – Micro-organism – per se ; compositions thereof; proces of... – Bacteria or actinomycetales; media therefor
Reexamination Certificate
2006-05-09
2006-05-09
Brusca, John S. (Department: 1631)
Chemistry: molecular biology and microbiology
Micro-organism, per se ; compositions thereof; proces of...
Bacteria or actinomycetales; media therefor
C435S320100, C536S023400, C536S023700, C536S024300
Reexamination Certificate
active
07041490
ABSTRACT:
The subject of the invention is the genomic sequence and the nucleotide sequences encoding polypeptides ofChlamydia trachomatis, such as cellular envelope polypeptides, which are secreted or specific, or which are involved in metabolism, in the replication process or in virulence, polypeptides encoded by such sequences, as well as vectors including the said sequences and cells or animals transformed with these vectors. The invention also relates to transcriptional gene products of theChlamydia trachomatisgenome, such as, for example, antisense and ribozyme molecules, which can be used to control growth of the microorganism. The invention also relates to methods of detecting these nucleic acids or polypeptides and kits for diagnosingChlamydia trachomatisinfection. The invention also relates to a method of selecting compounds capable of modulating bacterial infection and a method for the biosynthesis or biodegradation of molecules of interest using the said nucleotide sequences or the said polypeptides. The invention finally comprises, pharmaceutical, in particular vaccine, compositions for the prevention and/or treatment of bacterial, in particularChlamydia trachomatis, infections.
REFERENCES:
patent: 5436327 (1995-07-01), Southern et al.
patent: 5700637 (1997-12-01), Southern
patent: 6207647 (2001-03-01), Black et al.
patent: WO 89/10977 (1989-11-01), None
Genbank Accession No. X68033 (May 2, 1994).
Genbank Accession No. M 74221 (Feb. 16, 1995).
Genbank Accession No. Z11839 (Dec. 6, 1996).
Genbank Accession No. T67502 (Jul. 9, 1997).
Genbank Accession No. Q54841 (Jul. 15, 1994).
Genbank Accession No. X63515 (Feb. 17, 1997).
Genbank Accession No. U76536 (Feb. 1, 1997).
Genbank Accession No. L35530 (Dec. 20, 1994).
Genbank Accession No. X 59601 (Dec. 19, 1996).
Genbank Accession No. N70920 (May 7, 1991).
Sigma Catalog[Published by the Sigma Chemical Company, P.O. Box 14508, Saint Louis, Missouri 63178], pp. 776-778, 1990.
Cousineau et al., Gene, vol. 120, No. 1, pp. 33-41 (1992).
Beunis CJ et al., “Inhibition of lipopolysaccharide biosynthesis and cell growth following inactivation of the kdtA gene inEscherichia coli”, J Biol Chem. Nov. 17, 1995;270(46):27646-52.
Brade H et al., “Chemical and serological investigations on the genus-specific lipopolysaccharide epitope ofChlamydia”, Proc Natl Acad Sci U S A. Apr. 1987;84(8):2508-12.
Caldwell HD et al., “Monoclonal antibody against a genus-specific antigen ofChlamydiaspecies: location of the eptiope onChlamydiallipopolysaccharide”, Infect Immun. May 1984;44(2):306-14.
Fu Y et al., “A synthetic glycoconjugate representing the genus-specific epitope ofChlamydiallipopolysaccharide exhibits the same specificity as its natural counterpart”, Infect Immun. Apr. 1992;60(4):1314-21.
Girjes AA et al., “Lipopolysaccharide biosynthesis genes in koala type I Chamydia: cloning and characterization”, Res Microbiol. Jun. 1997;148(5):413-25.
Holst O et al., “Structure, serological specificity, and synthesis of artificial glycoconjugates representing the genus-specific lipopolysaccharide epitope ofChlamydiaspp”, J. Bacteriol. Mar. 1991;173(6):1862-6.
Mamat U et al., “The genus-specific lipopolysaccharide epitope ofChlamydiais assembled inC. psittaciandC. trachomatisby glycosyltransferases of low homology”, Mol Microbiol. Dec. 1993;10(5):935-41.
Nao FE et al., “Expression of theChlamydialgenus-specific lipopolysaccharide epitope inEscherichia coli”, Science. May 1985 10:228(4700):742-4.
Altschul, S.F. et al., 1990, “Basic local alignment search tool”, J. Mol. Biol. 215:403-410.
Altschul et al., 1997, “Gapped BLAST and PSI-BLAST: a new generation of protein database search programs”, Nucl. Acids Res. 25:3389-3402.
Bai, M. et al., 1993, “Mutations that alter an Arg-Gly-Asp (RGD) sequence in the adenovirus type 2 penton base protein abolish its cell-rounding activity and delay virus reproduction in flat cells”,. Virol. 67:5198-5205.
Fox, G. et al., 1989, “The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (Arginine-Glycine-Aspartic Acid)”, J. Gen. Virol. 70:625-637.
Gish et al., 1993, “Identification of protein coding regions by database similarity search”, Nature Genetics 3:266-272.
Gonnet et al., 1992, “Exhaustive matching of the entire protein sequence database”, Science 256:1443-1445.
Hackstadt, T. 1996, “Origins and functions of the chlamydial inclusion”, Trends in Microbiol. 5:288-293.
Hayashi, S. & Wu, H.C., 1992, “Identification and characterization of lipid-modified proteins in bacteria”, in N.M. Hooper and A.J. Turner (ed.),Lipid Modification of Proteins: A Practical Approach, Oxford University Press, New York, pp. 261-285.
Heinkoff & Heinkoff, 1993, “Performance evaluation of amino acid substitution matrices”, Proteins 17:49-61.
Higgins et al., 1996, “Using CLUSTAL for multiple sequence alignments”, Meth. Enzymol. 266:383-402.
Hueck, C.J., 1998, “Type III protein secretion systems in bacterial pathogens of animals and plants”, Molec. Biology Rev. 62:379-433.
Huovinen, P. et al., 1989, “Pharyngitis in adults: the presence and coexistence of viruses and bacterial organisms”, Ann. Intern. Med. 110:612-616.
Karlin & Altschul, 1990, “Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes”, PNAS USA 87:2264-2268.
Lee, C.A., 1997, “Type III secretion systems: machines to deliver bacterial proteins into eukaryotic cells?”, Trends Microbiol. 5:148-156.
Leininger, E. et al., 1991, “Pertactin, and Arg-Gly-Asp-containingBordetella pertussissurface protein that promotes adherence of mammalian cells”, PNAS USA 88:345-349.
Longbottom et al., 1998, “Molecular cloning and characterization of the genes coding for the highly immunogenic cluster of 90-kilodalton envelope proteins from theChlamydia psittacisubtype that causes abortion in sheep”, Infect. Immunol. 66:1317-1324.
Lukacova, M. et al., 1994, “Lipopolysaccharaide smooth-rough phase variation in bacteria of the genusChlamydia”, Infect. Immunol. 62(6):2270-2276.
Morrison, R.P. et al., 1995, “Gene knockout mice establish a primary protective role for major histocompatability complex class II-restricted responses inChlamydia trachomatis”, Infect. Immun. 63:4661-4668.
Nakai, K. & Kanehisa, M., 1991, “Expert system for predicting protein localization sites in gram-negative bacteria”, Proteins 11:95-110.
Nielsen, H. et al., 1997, “Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites”, Protein Engin. 10:1-6.
Pearson & Lipman, 1988, “Improved tools for biological sequence comparison”, PNAS USA 85(8):2444-2448.
Peterson et al., 1988, “Protective role of magnesium in the neutralization by antibodies ofChlamydia trachomatisinfectivity”, Infect. Immun. 56(4):885-891.
Pierschbacher & Ruoslahti, 1987, “Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion”, J. Biol. Chem. 262:17294-17298.
Pugsley, A.P., 1993, “The complete general secretory pathway in gram-negative bacteria”, (abstract) Microbiol. Rev. 57:50-108.
Rank, R.G. et al., 1988, “Susceptibility to reinfection after a primary chlamydial genital infection”, Infect. Immun. 56:2243-2249.
Raulston, J.E., 1995, “Chlamydial envelope components and pathogen—host cell interactions”, Mol. Microbiol. 15:607-616.
Reeves, P.R. et al., 1996, inBacterial Polysaccharide Synthesis and Gene Nomenclature, Elsevier Science Ltd., pp. 10071-10078, from Trends in Microbiology, 1996, 4(12):495-503.
Relman,D. et al., 1990, “Recognition of a bacterial adhesin by an integrin: macro
Fletcher Leah Diane
Griffais Rémy
Hoiseth Susan K.
Metcalf Benjamin J.
Peek Joel A.
Brusca John S.
Saliwanchik Lloyd & Saliwanchik
Serono Genetics Institute S.A.
LandOfFree
Chlamydia trachomatis polynucleotides and vectors,... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Chlamydia trachomatis polynucleotides and vectors,..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Chlamydia trachomatis polynucleotides and vectors,... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3528404