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United States Department of Agriculture

Agricultural Research Service

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Each year, approximately 60 new patents are issued by the U.S. Patent Office for USDA inventions. The Office of Technology Transfer (OTT) transfers these inventions through licenses to the private sector for commercialization. Below are links to technologies that are available for licensing. 

 

Subject Matter

Docket

Title

Description

Animal Health

154.1

REAGENTS TO DETECT GIARDIA LAMBLIA TROPHOZOITES AND CYSTS

Antisera were prepared in rabbits using recombinant proteins expressed in Escherichia coli.  While antisera provides a high titer reagent to detect G. lamblia cysts and trophozoites, monoclonal antibodies could also be prepared that recognize these giardin proteins. These could provide an unlimited supply of detection reagent without the need to repeatedly immunize animals to obtain antisera.

Animal Health

51.11

USE OF VITAMIN D IN DAIRY MASTITIS TREATMENT

The hydroxylated derivates of vitamins D3 or D2 are administered to the mammary gland of a female animal in an amount effective to inhibit or significantly reduce the growth of bacteria in the animal's mammary gland.

Animal Health

128.10

NEW METHOD AND DEVICE FOR SCRUBBING AMMONIA FROM AIR EXHAUSTED FROM ANIMAL REARING FACILITIES USING POTASSIUM BISULFATE AS THE ACID SOURCE

The containment facility ventilation system comprises a two stage scrubber configuration.  Exhaust air flows out of an animal containment facility and into a particulate scrubber, which removes particulates, reduces the dust and alkalinity of the exhaust air.  The air then flows into a chemical scrubber which removes ammonia from the exhaust air.  The chemical scrubber comprises a potassium bisulfate scrubber solution.  The bioproducts create a potential fertilizer.

Animal Health

69.08

HIGH ENERGY ELECTRON-BEAM IRRADIATION FOR THE PRODUCTION OF IMMUNOMODULATORS IN POULTRY

Invention to produce effective vaccines utilizing High Energy (10 MeV) Electron-Beam (E-beam) Irradiation offers unique and effective methodologies to produce large volumes of vaccines including viruses, bacteria, and protozoal candidates.  The stated invention relies on using high energy ionizing radiation to "kill" the target microorganism without destroying their immunogenicity (i.e., capacity to elicit an immune response).

Animal Health

105.10

INACTIVATED VIBRIO VULNIFICUS VACCINE

Vibrio vulnificus is a Gram-negative halophilic bacterium common to estuarine and marine environments.  The bacterium receives much attention due to the ability to produce disease in humans (usually immunocompromised people) either by consumption of raw oysters and/or contact with the bacterium in the marine environment.  The USDA isolated and characterized V. vulnificus from the sick fish. Biochemical analyses demonstrated that the isolate is a biotype 1 isolate and molecular characterization of the 16S rRNA demonstrated the isolate was 16S rRNA type B.  This rRNA type is usually associated with clinical human cases.  Following isolation and characterization, ARS developed an inactivated vaccine that is effective in preventing the disease in tilapia grown in low saline water (1.5 ppt). 

Animal Health

161.03

IMMUNOPOTENTIATING EFFECT OF A FOMITELLA FRAXINEA DERIVED LECTIN OF CHICKEN IMMUNITY AND RESISTANCE TO COCCIDIOSIS

This invention reports a novel immunopotentiating effect of a lectin (FFrL) extracted from the mushroom Fomitella fraxinea on poultry intestinal immunity and poultry coccidiosis.  The treatment regimen could involve oral feeding, intramuscular injection or intravenous injection.

Animal Health

8.08

MODIFIED ASPERGILLUS NIGER PHYTASE

The invention relates to the modification of Aspergillus niger phytase PhyA to produce an enzyme with superior heat tolerance.  For swine and poultry.

Animal Health

28.08 + 12.11 + 217.13

HYBRIDOMAS PRODUCING HIGHLY SPECIFIC MONOCLONAL ANTIBODIES TO DETECT MYCOBACTERIUM AVIUM SUBSPECIES PARATUBERCULOSIS

Hybridoma cell lines which produce and secrete monoclonal antibodies which selectively bind to Mycobacterium avium subspecies paratuberculosis have been produced.  Cells of M. avium subspecies paratuberculosis in biological samples may be detected and d quantified by contacting the sample with the antibodies to form a M. avium subspecies paratuberculosis/antibody immunocomplex when M. avium subspecies paratuberculosis is present, which immunocomplex may then be detected. Hybridoma cell lines which produce and secrete monoclonal antibodies which selectively bind to Mycobacterium avium subspecies paratuberculosis have been produced.

Animal Health

105.09

METHOD FOR FLOCCULANTING SUSPENSION USING BIOBASED RENEWABLE FLOCCULANTS

Methods for producing flocculants from chicken blood. 

Animal Health

70.10

PRODUCTION OF ANTI-PEPTIDE MONOCLONAL ANTIBODIES TO DISTINGUISH
EXOTIC NEW CASTLE DISEASES VIRUS FROM VACCINE STRAINS OF NEWCASTLE DISEASE VIRUS

Anti-peptide monoclonal antibodies(MAb's) specific for Exotic Newcastle Disease (END) are used for rapid diagnostic identification between poultry infected with vaccine strains of NDV (LaSota/B1) and END virus (ENDV).

Animal Health

161.12

RECOMBINANT MYCOBACTERIUM AVIUM SUBSP. PARATUBERCULOSIS PROTEINS INDUCE IMMUNITY AND PROTECT AGAINST INFECTION

The invention is a vaccine for paratuberculosis (Johne’s Disease) comprised of Mycobacterium avium subsp. paratuberculosis (MAP) proteins.  Induction of the immune response significantly reduces or eliminates colonization of the animal by MAP, and consequently reduces or eliminates fecal shedding of MAP.  Vaccination with the compositions provides protection against clinical disease and reduce transmission of MAP infection within a herd.

Animal Health

23.08

AVIAN VIRUS VACCINES AND USES THEREOF

The invention relates to poultry vaccines for protection from Newcastle Disease.

Animal Health

186.11

HIGH AFFINITY MONOCLONAL ANTIBODIES FOR DETECTION OF SHIGA TOXIN 2 (STX2)

High affinity monoclonal antibodies against Shiga toxin strain Stx2 and hybridomas that produce such antibodies are described. The antibodies may be used in a kit for detecting Stx2 and variants thereof in a sample.

Animal Health (Prion)

30.11

NOVEL POLYMORPHISM IN BOVINE PRION PROTEIN GENE SEQUENCE

This SNP may be used as a marker for selecting bovines susceptible to BSE for disposal and/or removal from breeding, the human food and animal feed supplies.

Animal Health (Prion)

131.07

PEPTIDE SEQUENCES FOR BINDING INFECTIOUS PRIONS

The invention relates to novel peptide sequences that specifically bind infectious prion protein.

Animal Health (Prion)

144.09 + 181.13

HIGH-AFFINITY MONOCLONAL ANTI-PRION ANTIBODIES

Peptide sequences that specifically bind infectious prion protein for the generation of antibodies and therapeutic agents.

Animal Health

113.08

TRIPLE ACTING ANTIMICROBIALS THAT ARE REFRACTORY TO RESISTANCE DEVELOPMENT

Multi-drug resistant superbugs are a persistent problem in modern health care. This invention provides an antimicrobial endolysin-Lysostaphin triple fusion protein, comprising (1) an endolysin CHAP endopeptidase domain, (2) an endolysin amidase domain, and (3) a Lysostaphin glycyl-glycine endopeptidase domain. The domains are derived from two proteins that show antimicrobial synergy when used in combination. The protein has specificity and exolytic activity for the peptidoglycan cell wall of untreated, live Staphylococcus aureus from many growth phases i.e. stationary, logarithmic and biofilm growth. The recombinant triple fusion protein comprising the three functional antimicrobial domains is designed to be refractory to resistance development.

Animal Health

180.04

NUCLEIC ACID ENCODING ENDOLYSIN FUSION PROTEIN

The invention concerns a recombinant nucleic acid molecule encoding an antimicrobial fusion peptidoglycan endopeptidase. The recombinant nucleic acid molecule according to the invention is formed from a nucleic acid encoding a bacterial endopeptidase (lysostaphin) from Staphylococcus simulans and a nucleic acid encoding a second endopeptidase (endolysin) module from Group B streptococcal bacteriophage B30. The encoded fusion endopeptidase has antimicrobial activity and kills both Staphylococcus bacteria and Streptococcus bacteria.

Animal Health

151.09

CREATING DESIGNER ANTIMICROBIALS: PEPTIDOGLYCAN HYDROLASE MODULE SHUFFLING

The invention concerns a nucleic acid encoding a recombinant bifunctional fusion peptidoglycan hydrolase protein formed from a nucleic acid encoding a peptidoglycan hydrolase module and a nucleic acid encoding a second peptidoglycan hydrolase module. The fusion, dual (or multiples thereof) peptidoglycan hydrolase modules can be used to treat disease caused by the bacteria for which the individual modules of the fusion protein are specific.

Animal Health

34.09

FUSION OF A  PEPTIDOGLYCAN HYDROLASE ENZYMES TO A PROTEIN TRASDUCTION DOMAIN ALLOWS DELIVERY OF PROTEIN ANTIMICROBIALS TO INTRACELLULAR PATHOGENS

Lysostaphin is a bacteriocin secreted by S. simulans to kill S. aureus, and has been shown to also be a potent antimicrobial for many antibiotic-resistant strains of S. aureus. By adding a ˜13 amino acid protein transduction domain (PTD) from the HIV-TAT protein to lysostaphin to form lysostaphin-PTD, both extracellular and intracellular forms of S. aureus and MRSA are killed in all (multiple) cell types examined.

Animal Health

45.10

STAPHYLOCOCCAL PHAGE 2638A ENDOLYSIN AMIDASE DOMAIN IS LYTIC FOR STAPHYLOCOCCUS AUREUS

Staphylococcus aureus is notorious for developing resistance to virtually all antibiotics to which it is exposed. Staphylococcal phage 2638A endolysin is a peptidoglycan hydrolase that is lytic for S. aureus when exposed externally, making it a new antimicrobial candidate. It shares a common protein organization with over 40 other staphylococcal peptidoglycan hydrolases: a CHAP endopeptidase domain, a mid-protein amidase 2 domain and a C-terminal SH3b cell wall binding domain. It is the first phage endolysin reported with a cryptic translational start site between the CHAP and amidase domains. Deletion analysis indicates that the amidase domain confers most of the lytic activity and requires the full SH3b domain for maximal activity. It is common for one domain to demonstrate dominant activity over another; however, the phage 2638A endolysin is the first to show high amidase domain activity dominant over the N-terminal CHAP domain, an important finding for targeting novel peptidoglycan bonds.

Animal Health

65.08

LYSK ENDOLYSIN IS SYNERGISTIC WITH LYSOSTAPHIN AGAINST MRSA

Multi-drug resistant superbugs are a persistent problem in modern health care. LysK is a staphylococcal bacteriophage endolysin from the phage K. It is a peptidoglycan hydrolase enzyme that can lyse many staphylococcal strains and thus is a potent antimicrobial against S. aureus, including MRSA. Lysostaphin is a bacteriocin secreted by S. simulans to kill S. aureus, and has been shown to also be a potent antimicrobial for many antibiotic resistant strains of S. aureus. This study describes optimal reaction conditions for the recombinant His-tagged LysK protein, compares its MIC and antimicrobial activity to lysostaphin and demonstrates synergy when the two are used in combination against the MRSA USA300.

Animal Health

112.08

BACTERIOPHAGE LYTIC ENZYMES AS ALTERNATIVE ANTIMICROBIALS

The present invention relates to isolated Clostridium perfringens bacteriophage lytic enzymes from baccteriophages CP26F and CP39O, and uses in controlling Clostridium perfringens.

Animal Health

112.10

ENHANCED ANTIMICROBIAL LYTIC ACTIVITY OF CHIMERIC PLY 187 ENDOLYSIN

Peptidoglycan hydrolases are an effective new source of antimicrobials. A chimeric fusion protein of the Ply187 endopeptidase domain and LysK SH3b cell wall binding domain is a potent agent against Staphylococcus aureus in three functional assays.

Animal Health

136.11

ENHANCED STAPHYLOLYTIC ACTIVITY OF THE STAPHYLOCOCCUS AUREUS BACTERIOPHAGE VB_SAUS-PHILPLA88  VIRION-ASSOCIATED PEPTIDOGLYCAN HYDROLASE HYDH5: FUSIONS, DELETIONS AND SYNERGY WITH LYSH5

Virion-associated peptidoglycan hydrolases have a potential as antimicrobial agents due to their ability to lyse Gram positive bacteria on contact. Full-length HydH5, a virion-associated peptidoglycan hydrolase from the Staphylococcus aureus bacteriophage vB_SauS-phi-IPLA88, and two truncated derivatives, containing only the CHAP domain, exhibited high lytic activity against live S. aureus cells. Three different fusion proteins were created and showed higher staphylolytic activity than the parental enzyme or its deletion construct. Parental and, fusion proteins lysed S. aureus cells in zymograms, plate lysis and turbidity reduction assays. In plate lysis assays, HydH5 and its derivative fusions lysed bovine and human S. aureus, S. aureus MRSA N315 strain, and human Staphylococcus epidermidis strains. HydH5 and its derivative fusions proteins displayed antimicrobial synergy with the endolysin LysH5 in vitro suggesting that the two enzymes have distinct cut sites and thus may be more efficient in combination for the elimination of staphylococcal infections.

 

 

 


Last Modified: 12/19/2014
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