TH50841C3 - Pestivirus that has been weakened - Google Patents

Abstract

DC60 (28/09/55) This invention involved a characteristically weakened pestiviral pestivirus that by depleting the activity of its enzyme in ERNS glycoproteins. Effects, Methods of Preparation, Usage and Detection of them A diffuser device for the dispersing of the active substance into the air consists of a container (10) for the active substance. Which containers (10) will be used The work for the transport of the active substance to the diffusion (20), where the diffusion (20) is adapted to accelerate the diffusion of the active substance. Where the container (10) and the diffusion part (20) work together with the coordination path (14), which is adjusted. Used to help the container (10) and the diffusion part (20) be bonded to each other. The interlocking path (14) includes the method for bonding (16a / b, 40) and the method for Part adhesion for diffusion (24a / b, 42a / b / c) adapted to work together. Where a combination of both the container bonding path (16a / b, 40) and the method for bonding Section for diffusion (24a / b, 42a / b / c) is defined for the efficiency of the harvesting. Solder of the container (10) and the diffusion part (20).

Claims (2)

Disclaimer (ALL) that will not appear on the advertisement page: 1. A diffuser device for the dispersing of the active substance into the air will consist of a container for the active substance. In which the container will be introduced They are used for the transport of active ingredients to diffusion parts with openings. Which parts for diffusion It will be adapted to accelerate the diffusion of the active ingredient. Where the container and the dispersion work in conjunction with the means of intervention. Optimized joint bond to help the container and diffuser be firmly bonded. Get together Methods for the coordination include a method for container adhesion and A mutually adapted path for diffusion adhesion. Where the way for connection Solder shall include threaded, joint and / or bonded components. The spirals on the spread section and the container Where the combination of both the method for fixing the container and the method for The diffusion adhesion is determined for the efficiency of the bonding. Of containers and parts for diffusion Where the path for the attachment of the diffusion part is at least included. With one overhang extending into the opening in the diffusion section. Where the method for fixing the container would at least consist of one A support shaped groove at least one path overhang to attach the diffusion part and where at least one groove forms a gap in the threaded or formed ridge. On the container 2. Vaccine of claim 1 which inactivated RNase activity by Disintegration and / or becoming At least 1 amino acid of the said glycoprotein 3. Vaccine of claim 2, with disintegration and / or The mutation is at location 295 to 307 and / or low at 338 to 357 of the glycoprotein. Described in Figure 1 for the CSFV, the Alfort strain, in its illustrated form, or that matches it in another species. 4. Vaccine pursuant to any of claims 1 through 3, which inactivates such RNase activity. By dissolution or mutation of the amino acid at position 346 of the glycoprotein as described in Figure 1 for the Alfort strain of CSFV, in a sample elevated form, or corresponding to it in other strains. 5. Vaccine pursuant to any of claims 1 through 4, which inactivates such RNase activity. The histidine residue at position 346 of that glycoprotein, as described in Figure 1 for Alfort strains CSFV, in a sample elevated form, or corresponding to it in the Alfort strains is disintegrated. Other varieties 6. Vaccines pursuant to any of claims 1 through 5, containing BVDV pestivirus, which inactivate the RNase activity by disintegrating the histidine. (Histidine residue) at position 346 of the loud glycoprotein As described in Figure 1, for the CSFV, the Alfort strain in the model illustrated or matches it in Other BVDV variants 7. Pestivirus by inducing RNase activity in ERNS glycoproteins inactivated by Multiple shedding and / or amino acid At least one amino of the aforementioned glycoprotein was conditional that the amino acid at position 297 and / or 346 of that glycoprotein was not lysine as described in Figure 1 for the Alfort strain of CSFV in the figure. 8. Pestivirus according to claim 7, which inactivates the RNase activity by Multiple disconnection and / or mutilation Addresses amino acids at positions 295 to 307 and / or at positions 338 to 357 of that glycoprotein, as described in Figure 1 for Alfort strain CSFV, in the illustrative form or corresponding to it. In other species 9. Pestivirus of Claim 7 or 8, which inactivates such RNase activity by disintegration or Amino acid conversion at position 346 of glycoproteins. Such as Described in Figure 1 for the Alfort strain CSFV, in an example, or that matches it in other strains 1 0. Pestivirus according to any of claims 7 through 9, the app The activity of RNase was inactivated by histidine residue at position 346 of the glycoprotein as described in Figure 1 for Alfort strains CSFV in elevated form. Examples or corresponding to them in other variants 1. 1. Pestivirus BVDV pursuant to any of Claims 7 through 10 that inactivated the RNase activity. The histidine residue at position 346 of that glycoprotein, as described in Figure 1 for Alfort strain CSFV, in a sample model or corresponding to it in the species, was disintegrated by histidine residue at position 346. Other 1 2. Nucleic acid code for ERNS glycoprotein by inducing the activity of RNase contained in that glycoprotein. Inactivated by dissolution and / or the formation of amino acids At least one such glycoprotein was conditional that the amino acid at position 297 and / or 346 of that glycoprotein was not lysine as described in Figure 1 for Alfort strain CSFV in raised form. It is an example that matches it in other strains 1. 3. The nucleic acid of claim 12, which inactivates the RNase activity. By being lost and / or The conversion at the amino acid position 295 to 307 and / or position 338 to 357 of the glycoprotein, according to Described in Figure 1 for the Alfort strain CSFV, in its exemplary form or that it matches it in other strains 1 4. The nucleic acid of claim 12 or 13, with the application The activism of such RNase is ineffective by disintegration. And / or the amino acid mutation, position 346 of the said glycoprotein, as described in Figure 1 for CSFV, Alfort strains in the exemplary form or corresponding to it in other strains 1 5. Nucleic acid according to any of claims 12 through 14, inactivating such RNase activity by dissolving the histidine residue at the site. 346 of such glycoproteins, according to Described in Figure 1 for the Alfort strain CSFV in a raised form. 1 6. BVDV nucleic acid according to any Clause 12 to 15, which inactivates the RNase activity by: The deterioration of histidine residue at position 346 of the glycoprotein, according to Described in Figure 1 for the Alfort strain CSFV, in an illustrated scheme that matches it in other BVDV strains 1 7. The use of nucleic acids in accordance with any of Claims 12 through 16. For the preparation of nucleotides, vaccines and / or vaccines. One of the claims 1 through 6 and / or Pestivirus, according to clause. Any clause of Claims 7 through 11 and / or Nucleotide sequence pursuant to Clause 12 through 16 1 9. Methods for the weakening of Pestivirus is characterized by Inactivating RNase activity in ERNS glycoprotein 2 0. Method of claim 19 by inactivating RNase activity by Disintegration and / or becoming At least one amino acid of the glycoprotein 2 1. Method of claim 19 or 20, with dissolution And / or the change in acid The 295 to 307 and / or 338 to 357 position of the glycoprotein, as described in Figure 1 for the Alfort strain CSFV, in the illustrated scheme that matches it in other strains. 2 2. Any of the methods of Claims 19 to 21 that inactivate the RNase activity by Disintegration or mutation of the amino acid at position 346 of the glycoprotein as described in Figure 1 for Alfort strain CSFV in the exemplary form or corresponding to it in other strains 2 3. Any method of claims 19 through 22 inactivating the RNase activity by: Loss of histidine at position 346 of the said glycoprotein, as Described in Figure 1 for the Alfort strain CSFV in an illustrated format. Or that matches it in other species. 2 4. Methods for producing vaccines that have been weakened. Specifically expressing the nature by doing Inactivated RNase activity in ERNS glycoprotein 2 5. Method of claim 24 by inactivating RNase activity by Loss and / or dislocation At least one amino of the glycoprotein 2 6. Method of claim 24 or 25, with dissolution And / or the change in acid The 295 to 307 amino and / or 338 to 357 position of the glycoprotein, as described in Figure 1 for the Alfort strain CSFV, in the exemplary form or that match it in other strains. 2 7. Means according to any of Claims 24 to 26, whereby such RNase activity is inactivated by disintegration or disintegration of Amino acid at position 346 of glycoprotein As described in Figure 1 for the Alfort strain CSFV, in an exemplary or direct form. 2 8. Any method of claim 24 through 27 in which RNase activity inactivated by disintegration of histidine at position 346. Of such glycoproteins, as Described in Figure 1 for the Alfort strain CSFV in an illustrated scheme that matches it in other strains 2. 9. Methods for labeling the detectable pestivirus shown. Inactivated RNase activity in ERNS glycoprotein 3 0. Proposition 29, which inactivated RNase activity by means of Disintegration and / or becoming At least one amino acid of the said glycoprotein 3 1. Method of claim 29 or 30, where dissolution And / or the change in acid The 295 to 307 amino and / or 338 to 357 position of the glycoprotein, as described in Figure 1 for the Alfort strain CSFV, in the exemplary form or that match it in other strains. 3 2. Any of the methods of Claims 29 to 31 that inactivate the RNase activity by disconnection. Loss or conversion of amino acids at position 346 of glycoproteins. This is as described in Figure 1 for the Alfort species CSFV, in its exemplary form, or that matches it in the other species. 3. 3. Method for any of the claims 29 through 32, whereby Inactivate the RNase activity by dislodging The histidine portion at 346 of glycoprotein was recovered. Such as Described in Figure 1 for the Alfort strain CSFV, in an exemplary fashion or that matches it in other strains 3. 4. Use of the vaccine in accordance with either Clause 1 to 6 or a pharmaceutical mix. According to claim 18 to produce drugs for Prevention and Treatment of Pestivirus Infection in Animals 3 5. The process for preparing the treated pestivirus. Specifically weak as shown It was characterized by inactivating RNase activity in ERNS glycoprotein 3 6. Process of claim 35 with inactivation of RNase activity. By being lost and / or becoming 3 7. Process of claim 35 or 36, with the release of at least one amino acid of the glycoprotein. Healed and / or such becoming It is at the amino acid position 295 to 307 and / or position 338 to 357 of the glycoprotein as described in Figure 1 for the Alfort strain CSFV. Other variants 3. 8. Process by any of the Articles 35 to 37 that inactivated the RNase activity by Disintegration or mutation of the amino acid at position 346 of the glycoprotein as described in Figure 1 for Alfort strain CSFV in a sample elevated form or corresponding to it in other strains 3. 9. Process according to any of Claims 36 to 38, which inactivates such RNase activity by: The histidine fraction at position 346 of the glycoprotein is described in Figure 1 for Alfort-type CSFV in an exemplary variation that matches it in other strains 4 0. Specifically labeled pestivirus preparations shown Characterized by inactivating RNase activity in ERNS glycoprotein 4 1. Process of claim 40 with inactivity of RNase activity. By being lost and / or becoming Of at least one amino acid of the glycoprotein 4 2. The process of claim 40 or 41, with dissolution And / or the aforementioned It is at the amino acid position 295 to 307 and / or position 338 to 357 of the glycoprotein as described in Figure 1 for the Alfort strain CSFV. Other variants 4 3. Process by any of the Claims 40 to 42 that inactivated the RNase activity by Disintegration or mutation of the amino acid at position 346 of the glycoprotein as described in Figure 1 for Alfort strain CSFV in a sample elevated form or corresponding to it in other strains 4. 4. Process according to any of Claims 40 through 43, which inactivates the RNase activity by: The histidine loss at position 346 of the glycoprotein is described in Figure 1 for Alfort-type CSFV in either a sample model or a corresponding to it in other strains. Use a vaccine of any of Claims 1 through 6 for prevention and treatment. Animal Pestivirus Infection 4 6. Use of the Pharmacy Mixture of claim 18 for the prevention and treatment of infection. Pestivirus in animals 4. 7. Use of pestivirus of any of the Clause 7 through 11 and / or No. Nucleotides according to any claim 12 through 16 for vaccine preparation or pharmaceutical mixtures 4 8. Method for differentiating animal infected with PHE. The virus consciousness left the affected animal. Vaccine with pestivirus obtained Been specifically weakened Which weakened the specific inactivated pestivirus In any case of claims 19 through 23, the procedure includes the following steps: (1) Obtaining a sample from a resident animal. In suspected pestivirus infection or vaccinated animal (2), pestivirus nucleotide sequence identification in The example above (3) illustrates the association of disintegration. And / or mutation of ERNS nucleotide sequences present in the vaccine to the vaccinated animal and show an association of There is no loss and / or Become such an infection. The virus consciousness of such animals 4 9. Clause 48 method includes the following steps: (1) Obtaining a sample from an animal of interest to the animal. Pestiviral or vaccinated animal infection is suspected (2). Indication of Pestin-modified glycoprotein ERNS. Softened virus Specific gripping effect of The manoclonal or polycrystalline antibody against the ERNS glycoprotein present in the sample. The glycoprotein has been modified. Modified by any of the methods of claims 19 to 23, where such monoclonal albodi or polyclonal antibodies do not bind to missed ERNS glycoproteins. The modification (3) shows the binding affinity of the mono. Colonal or polyclonal antibodies As mentioned with the receiving animal Vaccines and demonstrated an association of the absence of antibodies against pestiviral infection of such animals under the condition that other pestiviral materials were generated in such animals and / or in the samples. 5 0. Clause 49 method includes the following steps: (1) Obtain a sample from an animal of interest to Pestiviral or vaccinated animal infection is suspected (2). Non-modified ERNS glycoprotein identification of pestin. Softened virus Specific gripping effect of The manoclonal or policlonal antibody against ERNS glycoprotein present in the sample. Such glycoproteins are not modified. Modified by any of the methods of claims 19 to 23, where such monodonal, amphibody or polyclonal antibodies do not bind to non-modified ERNS glycoproteins ( 3) Show the binding affinity of the mono. Colonal or polygonal antibodies It is associated with the absence of antibodies in those animals. Handle with vaccinated animals Under the condition that another pestiviral material has been generated in the said animal and / or in such example 5. 1. Method of claim 48 that includes the following steps: (1) Obtaining a sample from an animal of interest to Pestiviral or vaccinated animal infection is suspected (2). Determination of ERNS glycoprotein RNase or RNase presence in the sample (3) has shown an association. RNase deficiency of ERNS glycoprotein was observed in vaccinated animals and demonstrated a correlation of hypokalemia. The manner in which pestivirus infection of such animals 5 2. Method of claim 48 that includes the following steps: (1) Obtaining an animal sample of polyclonal antibody. In the interest of detecting infection Pestivirus or animal (2) Any specific binding indication of such policlonal antibody to unmodified ERNS glycoprotein or ERNS glycoprotein was modified according to the vaccine. Invent (3) shows the connection of the capture of Paulicollon. Such antibodies against ERNS glycoproteins are unmodified. Variable with pestivirus infection And show the association of binding of policlonan antibodies to ERNS glycoproteins that are fabricated according to the fabrication and Vaccination