A kind of pit-1 monoclonal antibody, preparation method and application
A technology of antibody and epitope, applied in application, chemical instruments and methods, anti-animal/human immunoglobulin, etc., to achieve the effect of reducing resource waste and environmental pollution, reducing phosphorus content, and efficient absorption
Active Publication Date: 2021-06-25
NORTHWEST A & F UNIV
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Problems solved by technology
At present, there is no technology to directly interfere with the phosphorus sensing function of intestinal PiT-1, change the expression of intestinal NaPi-IIb, and then regulate the efficiency of intestinal phosphorus absorption in livestock and poultry
Method used
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Embodiment 1
[0034] (1) Chicken PiT-1 antibody was constructed using synthetic peptide vaccine technology
[0035] In this example, the chicken PiT-1 amino acid sequence (NCBI number XP_015152988.1) was imported into BepiPred-2.0 analysis software to predict the epitope. Such as figure 1 As shown, the chicken PiT-1 amino acid sequence was compared with the human PiT-1 amino acid sequence (NCBI number NP_005406.3). Such as figure 2 As shown, by comparing the transmembrane structure of human PiT-1 protein, five chicken PiT-1 antigen epitopes located outside the cell membrane were selected, which were internally named EP-1 (IRKGLIDV), EP-2 (MYNATQEL), EP- 3 (KWSELLKI), EP-4 (LGFDKLPL) and EP-5 (DVATKVAT).
[0036] Synthesize the above peptides, divide the laying hens into an experimental group and a control group, the experimental group is injected with the vaccine made of the peptides and adjuvant, and the control group is only injected with the corresponding adjuvant (ie Freund's adjuva...
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The disclosure belongs to the technical field of regulating phosphorus absorption in the intestinal tract of livestock and poultry, and specifically relates to a PiT-1 monoclonal antibody, a preparation method and an application. The utilization efficiency of phosphorus in feed by livestock and poultry is low, which not only wastes non-renewable inorganic phosphate resources, but also causes environmental pollution. In view of the above situation, the present disclosure obtains the epitope peptide sequence of PiT-1 located outside the cell membrane through screening, and specifically designs the corresponding PiT-1 monoclonal egg yolk antibody, which can neutralize and inhibit PiT-1 on the apical membrane of intestinal epithelial cells 1’s phosphorus sensing function, maintain the expression of NaPi‑IIb protein in the intestine, and promote the absorption and transport of phosphorus in the intestine. When livestock and poultry eat the feed mixed with the antibody, the phosphorus content in serum is significantly increased, and the phosphorus content in excreta is significantly reduced, saving resources and protecting the environment.
Description
technical field [0001] The disclosure belongs to the technical field of regulation and control of phosphorus absorption in the intestinal tract of livestock and poultry, and in particular relates to the application of PiT-1 antibody in the preparation of feed and nutrition for livestock and poultry. Background technique [0002] The information disclosed in this Background section is only intended to increase the understanding of the general background of the disclosure, and is not necessarily to be taken as an acknowledgment or any form of suggestion that the information constitutes prior art that is already known to those skilled in the art. [0003] Phosphorus is an essential mineral element for the survival, growth, and production of livestock and poultry. It is a nutrient that must be supplied in sufficient quantities and added in large amounts when formulating livestock and poultry feed formulations. However, the utilization efficiency of phosphorus in feed by livestoc...
Claims
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IPC IPC(8): C07K14/47C07K14/465C07K16/18C07K16/02A23K50/30A23K50/75A23K20/147A23L33/17
CPCA23V2002/00A23K20/147A23K50/30A23K50/75A23L33/17C07K14/465C07K14/47C07K16/02C07K16/18C07K2317/11A23V2200/32
Inventor 任周正颜家坤杨小军杨欣张文晔
Owner NORTHWEST A & F UNIV