Polynucleotides, materials incorporating them, and methods...

Details Polynucleotides, materials incorporating them, and methods... Polynucleotides, materials incorporating them, and methods...

2000-08-08

2003-04-08

Brusca, John S. (Department: 1631)

Chemistry: molecular biology and microbiology

Micro-organism, per se ; compositions thereof; proces of...

Bacteria or actinomycetales; media therefor

C435S320100, C536S023700

Reexamination Certificate

active

06544772

ABSTRACT:

TECHNICAL FIELD OF THE INVENTION
This invention relates to polynucleotides isolated from lactic acid bacteria, including partial and extended sequences, as well as to probes and primers specific to the polynucleotides; DNA constructs comprising the polynucleotides; biological materials, including plants, microorganisms and multicellular organisms, incorporating the polynucleotides; polypeptides expressed by the polynucleotides; and methods for using the polynucleotides and polypeptides.
BACKGROUND OF THE INVENTION
The present invention relates to polynucleotides isolated from a specific strain of lactic acid bacteria, namely
Lactobacillus rhamnosus
HN001 (
L. rhamnosus
HN001). Lactic acid bacteria, and their enzymes, are the major determinants of flavor and fermentation characteristics in fermented dairy products, such as cheese and yogurt. Flavors are produced through the action of bacteria and their enzymes on proteins, carbohydrates and lipids.
Lactobacillus rhamnosus
strain HN001 are heterofermentative bacteria that are Gram positive, non-motile, non-spore forming, catalase negative, facultative anaerobic rods exhibiting an optimal growth temperature of 37±1° C. and an optimum pH of 6.0-6.5. Experimental studies demonstrated that dietary supplementation with
Lactobacillus rhamnosus
strain HN001 induced a sustained enhancement in several aspects of both natural and acquired immunity (See PCT International Publication No. WO 99/10476). In addition,
L. rhamnosus
HN001, and certain other Gram-positive bacteria can specifically and directly modulate human and animal health (See, for example, Tannock et al.,
Applied Environ. Microbiol.
66:2578-2588, 2000; Gill et al.,
Brit. J. Nutrition
83:167-176; Quan Shu et al.,
Food and Chem. Toxicol.
38:153-161, 2000; Quan Shu et al.,
Intl. J. Food Microbiol.
56:87-96, 2000; Quan Shu et al.,
Intl. Dairy J.
9:831-836, 1999; Prasad et al.,
Intl. Dairy J.
8:993-1002, 1998; Sanders and Huis in't Veld,
Antonie van Leeuwenhoek
76:293-315, 1999; Salminen et al., 1998. In: Lactic Acid Bacteria, Salminen S and von Wright A (eds)., Marcel Dekker Inc, New York, Basel, Hong Kong, pp. 211-253; Delcour et al.,
Antonie van Leeuwenhoek
76:159-184, 1999; Blum et al.,
Antonie van Leeuwenhoek
76:199-205, 1999; Yasui et al.,
Antonie van Leeuwenhoek
76:383-389, 1999; Hirayama and Rafter,
Antonie van Leeuwenhoek
76:391-394, 1999; Ouwehand, 1998. In: Lactic Acid Bacteria, Salminen S and von Wright A (eds)., Marcel Dekker Inc, New York, Basel, Hong Kong, pp. 139-159; Isolauri et al., S 1998. In: Lactic Acid Bacteria, Salminen S and von Wright A (eds)., Marcel Dekker Inc, New York, Basel, Hong Kong, pp. 255-268; Lichtenstein and Goldin, 1998. In: Lactic Acid Bacteria, Salminen S and von Wright A (eds)., Marcel Dekker Inc, New York, Basel, Hong Kong, pp. 269-277; El-Nezami and Ahokas, 1998. In: Lactic Acid Bacteria, Salminen S and von Wright A (eds)., Marcel Dekker Inc, New York, Basel, Hong Kong, pp. 359-367; Nousianen et al., 1998. In: Lactic Acid Bacteria, Salminen S and von Wright A (eds)., Marcel Dekkcer Inc, New York, Basel, Hong Kong, pp. 437-473; Meisel and Bockelmann,
Antonie van Leeuwenhoek
76:207-215, 1999; Christensen et al., Antonie van Leeuwenhoek 76:217-246, 1999; Dunne et al.,
Antonie van Leeuwenhoek
76:279-292, 1999). Beneficial health effects attributed to these bacteria include the following:
Increased resistance to enteric pathogens and anti-infection activity, including treatment of rotavirus infection and infantile diarrhea—due to increases in antibody production caused by an adjuvant effect, increased resistance to pathogen colonization; alteration of intestinal conditions, such as pH; and the presence of specific antibacterial substances, such as bacteriocins and organic acids.
Aid in lactose digestion—due to lactose degradation by bacterial lactase enzymes (such as beta-galactosidase) that act in the small intestine.
Anti-cancer (in particular anti-colon cancer) and anti-mutagenesis activities—due to anti-mutagenic activity; alteration of procancerous enzymatic activity of colonic microbes; reduction of the carcinogenic enzymes azoreductase, beta-glucuronidase and nitroreductase in the gut and/or faeces; stimulation of immune function; positive influence on bile salt concentration; and antioxidant effects.
Liver cancer reduction—due to aflatoxin detoxification and inhibition of mould growth.
Reduction of small bowel bacterial overgrowth—due to antibacterial activity; and decrease in toxic metabolite production from overgrowth flora.
Immune system modulation and treatment of autoimmune disorders and allergies—due to enhancement of non-specific and antigen-specific defence against infection and tumors; enhanced mucosal immunity; adjuvant effect in antigen-specific immune responses; and regulation of Th1/Th2 cells and production of cytokines.
Treatment of allergic responses to foods—due to prevention of antigen translocation into blood stream and modulation of allergenic factors in food.
Reduction of blood lipids and prevention of heart disease—due to assimilation of cholesterol by bacteria; hydrolysis of bile salts; and antioxidative effects.
Antihypertensive effect—bacterial protease or peptidase action on milk peptides produces antihypertensive peptides. Cell wall components act as ACE inhibitors.
Prevention and treatment of urogenital infections—due to adhesion to urinary and vaginal tract cells resulting in competitive exclusion; and production of antibacterial substances (acids, hydrogen peroxide and biosurfactants).
Treatment of inflammatory bowel disorder and irritable bowel syndrome—due to immuno-modulation; increased resistance to pathogen colonization; alteration of intestinal conditions such as pH; production of specific antibacterial substances such as bacteriocins, organic acids and hydrogen peroxide and biosurfactants; and competitive exclusion.
Modulation of infective endocarditis—due to fibronectin receptor-mediated platelet aggregation associated with Lactobacillus sepsis.
Prevention and treatment of
Helicobacter pylon
infection—due to competitive colonization and antibacterial effect.
Prevention and treatment of hepatic encephalopathy—due to inhibition and/or exclusion of urease-producing gut flora.
Improved protein and carbohydrate utilisation and conversion—due to production of beneficial products by bacterial action on proteins and carbohydrates.
Other beneficial health effects associated with
L. rhamnosus
include: improved nutrition; regulation of colonocyte proliferation and differentiation; improved lignan and isoflavone metabolism; reduced mucosal permeability; detoxification of carcinogens and other harmful compounds; relief of constipation and diarrhea; and vitamin synthesis, in particular folate.
Peptidases are enzymes that break the peptide bonds linking the amino group of one amino acid with the carboxy group (acid group) of an adjacent amino acid in a peptide chain. The bonds are broken in a hydrolytic reaction. There is a large family of peptidase enzymes that are defined by their specificity for the particular peptides bonds that they cleave (Barrett A J, Rawlings N D and Woessner J F (Eds.) 1998.
Handbook of proteolytic enzymes
. Academic Press, London, UK). The two main families are exopeptidases and endopeptidases.
Exopeptidases cleave amino acids from the N- or C-terminus of a peptide chain, releasing free amino acids or short (di- and tripeptides). Different types of exopeptidases include:
Aminopeptidases—release a free amino acid from the N-terminus of a peptide chain;
dipeptidyl-peptidase (also known as dipeptidyl-aminopeptidases)—release a dipeptide from the N-terminus of a peptide chain;
tripeptidyl-peptidases (also known as tripeptidyl-aminopeptidases)—release a trifpeptide from the N-terminus of a peptide chain);
carboxypeptidases—release a free amino acid from the C-terminus of a peptide chain;
peptidyl-dipeptidase—release a dipeptide from the C-terminus of a peptide chain;
dipeptidases—release two free amino acids from a dipeptide; and
tripeptidas

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