Nucleic acids, vectors, and host cells including mycobacterium d

Details Nucleic acids, vectors, and host cells including mycobacterium d Nucleic acids, vectors, and host cells including mycobacterium d

1993-10-04

1999-09-21

Caputa, Anthony C.

Chemistry: molecular biology and microbiology

Animal cell, per se ; composition thereof; process of...

435358, 435365, 4352523, 43525233, 43525411, 4353201, 435 693, 536 237, C12N 500, C12N 120, C12N 1500, C07H 2104

Patent

active

059553561

DESCRIPTION:

BRIEF SUMMARY
BACKGROUND OF THE INVENTION

1. Field of the Invention
The invention relates to polypeptides and peptides, particularly recombinant polypeptides and peptides, which can be used for the diagnosis of tuberculosis. The invention also relates to a process for preparing the above-said polypeptides and peptides, which are in a state of biological purity such that they can be used as part of the active principle in the preparation of vaccines against tuberculosis.
It also relates to nucleic acids coding for said polypeptides and peptides.
Furthermore, the invention relates to the in vitro diagnostic methods and kits using the above-said polypeptides and peptides and to the vaccines containing the above-said polypeptides and peptides as active principle against tuberculosis.
By "recombinant polypeptides or peptides" it is to be understood that it relates to any molecule having a polypeptidic chain liable to be produced by genetic engineering, through transcription and translation, of a corresponding DNA sequence under the control of appropriate regulation elements within an efficient cellular host. Consequently, the expression "recombinant polypeptides" such as is used herein does not exclude the possibility for the polypeptides to comprise other groups, such as glycosylated groups.
The term "recombinant" indeed involves the fact that the polypeptide has been produced by genetic engineering, particularly because it results from the expression in a cellular host of the corresponding nucleic acid sequences which have previously been introduced into the expression vector used in said host.
Nevertheless, it must be understood that this expression does not exclude the possibility for the polypeptide to be produced by a different process, for instance by classical chemical synthesis according to methods used in the protein synthesis or by proteolytic cleavage of larger molecules.
The expression "biologically pure" or "biological purity" means on the one hand a grade of purity such that the recombinant polypeptide can be used for the production of vaccinating compositions and on the other hand the absence of contaminants, more particularly of natural contaminants.
2. Description of the Prior Art
Tuberculosis remains a major disease in developing countries. The situation is dramatic in some countries, particularly where high incidence of tuberculosis among AIDS patients represents a new source of dissemination of the disease.
Tuberculosis is a chronic infectious disease in which cell-mediated immune mechanisms play an essential role both for protection against and control of the disease.
Despite BCG vaccination, and some effective drugs, tuberculosis remains a major global problem. Skin testing with tuberculin PPD (protein-purified derivative) largely used for screening of the disease is poorly specific, due to cross reactivity with other pathogenic or environmental saprophytic mycobacteria.
Moreover, tuberculin PPD when used in serological tests (ELISA) does not permit discrimination between patients who have been vaccinated by BCG, or those who have been primo-infected, from those who are developing evolutive tuberculosis and for whom an early and rapid diagnosis would be necessary.
A protein with a molecular weight of 32-kDa has already been purified from zinc deficient M. bovis BCG culture filtrate. This protein was identified as antigen 85A (De Bruyn J. et al., 1987, "Purification, partial characterization and identification of a 32-kDa protein antigen of Mycobacterium bovis BCG" Microb. Pathogen. 2:351). Its NH.sub.2 -terminal amino acid sequence (Phe-Ser-Arg-Pro-Gly-Leu) (SEQ ID NO:1) is identical to that reported for the .alpha.-antigen (antigen 85B) protein purified from M. bovis BCG (Wiker, H. G. et al., 1986, "MPB59, a widely cross-reacting protein of Mycobacterium bovis BCG" Int. Arch. Allergy Appl. Immunol. 81:307). The antigen 85-complex is present among different strains of mycobacteria (De Bruyn J. et al., 1989, "Effect of zinc deficiency of the appearance of two immunodominant protein antigens (32-kDa and

REFERENCES:
Parsons, J.A. (ed) "Peptide Hormones", published by University Park Press (Baltimore), see Chapter 1 by Rudinger, E.J., "Characteristics of the amino acids as components of a peptide hormone sequence", pp. 1-7, Jun. 1976.
Lazar et al. Mol. Cell. Biol. 8(3):1247-52 Mar. 1988.
Kumar et al. PNAS 87:1337-1341 1990.
Bowie et al. Science 247:1306-1310 1990.
Shinnick, "The 65-Kilodalton Antigen of Mycobacterium tuberculosis", Journal of Bacteriology, 169:1080-1088 (Mar. 1987).
Matsuo et al., "Cloning and Expression of the Gene for the Cross-Reactive .alpha.-Antigen of Mycobacterium kansasii ", Infection and Immunity, 58:550-556 (Feb. 1990).
Nagai et al., "Isolation and Partial Characterization of Major Protein Antigens in the Culture Fluid of Mycobacterium tuberculosis", Infection and Immunity, 59:372-382 (Jan. 1991).
Wiker et al., "Evidence for Three Separate Genes Encoding the Proteins of the Mycobacterial Antigen 85 Complex", Infection and Immunity, vol. 58, No. 1, pp. 272-274 (Jan. 1990).
Worsaae et al., "Allergenic and Blastogenic Reactivity of Three Antigens from Mycobacterium tuberculosis in Sensitized Guinea Pigs", Infection and Immunity, vol. 55, pp. 2922-2927 (Dec. 1987).

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