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A novel function of a Bacillus subtilis GGT protein degradation product and antimicrobial peptide identification for the product

A Bacillus subtilis, protein degradation technology, applied in the direction of chemicals for biological control, animal repellents, plant growth regulators, etc.

Active Publication Date: 2018-12-04
HEILONGJIANG BAYI AGRICULTURAL UNIVERSITY
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

During the cultivation of Bacillus, a large amount of the enzyme and its degradation fragments can be detected in the supernatant for a long time, but there is no report about the relationship between the enzyme and its degradation fragments and antibacterial activity

Method used

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  • A novel function of a Bacillus subtilis GGT protein degradation product and antimicrobial peptide identification for the product
  • A novel function of a Bacillus subtilis GGT protein degradation product and antimicrobial peptide identification for the product
  • A novel function of a Bacillus subtilis GGT protein degradation product and antimicrobial peptide identification for the product

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Experimental program
Comparison scheme
Effect test

Embodiment 1

[0034] Purification and mass spectrometry identification of Bacillus subtilis GGT protein.

[0035] Inoculate Bacillus subtilis BU412 into YME liquid medium (maltose 10g / L, yeast extract powder 4g / L, glucose 4g / L, pH 7.5) for overnight culture, centrifuge at 12000g to collect the supernatant, and use 80% ammonium sulfate precipitation to obtain For protein components, use 20mM Tris-HCl (pH7.5) buffer to dissolve the precipitate, filter through a 0.22μm filter membrane, and use an AKTA protein purification instrument for anion exchange chromatography. The purification column used is Q hp anion exchange from GE. Column (column volume is 5 mL). Use 20mM Tris-HCl (pH7.5) buffer to load and equilibrate, perform 0-100% linear gradient elution with 0.5M NaCl, 20mM Tris-HCl (pH7.5) buffer, and collect protein according to the absorption peak Components P1-P3 ( figure 1 ), using the Oxford cup method to measure the antibacterial activity of each isolated component to Streptomyces sca...

Embodiment 2

[0038] Prediction of antimicrobial peptides from Bacillus subtilis GGT proteins.

[0039] The amino acid sequence of the GGT protein (Genbank accession number is KIU12867.1) in CAMP R3 Online prediction of the antimicrobial peptide region on the database found that multiple polypeptides of GGT may constitute antimicrobial peptides, combined with the secondary structure and positioning of these polypeptides in the three-dimensional structure of the GGT protein ( Image 6 ), from which 3 polypeptides (Table 1) were selected for online analysis in the APD database. The results showed that all three peptides could form α-helices with hydrophobic surfaces, which may have the activity of antimicrobial peptides. According to the number of amino acids in the three polypeptide chains, they were named LT30, AE26 and IF20, respectively. In addition, the three-dimensional structure of the GGT protein was queried from the PDB database and the three peptide chains were spatially positioned ...

Embodiment 3

[0044] Synthesis and activity detection of predicted antimicrobial peptides.

[0045] Three candidate antibacterial peptides of the GGT protein of Bacillus subtilis were synthesized by solid-phase peptide synthesis technology. The N-terminus of the synthesized peptides was acetylated and the C-terminus was amidated, with a purity of more than 95%. The polypeptide was dissolved in 20 mM Tris-HCl (pH 8.0) buffer at a final concentration of 50 mM. The antibacterial activity of these three polypeptides against Streptomyces scabies was determined by the Oxford cup method. The results showed that polypeptide LT30 had no inhibitory effect on Streptomyces scabica, AE26 and IF20 had inhibitory effect on Streptomyces scabica, and the effect of IF20 was better than that of AE26 ( Figure 7 ).

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Abstract

The invention relates to a novel function of a Bacillus subtilis GGT protein degradation product, namely an anti-Streptomyces scabies application. The invention also provides antimicrobial peptides from Bacillus subtilis GGT protein. That the known Bacillus subtilis GGT protein after degradation has an anti-Streptomyces scabies activity is found, and the antimicrobial peptide sequences are identified from a degradation product of the Bacillus subtilis GGT protein, thus providing a novel way of thinking for biological control of potato common scab.

Description

technical field [0001] The invention belongs to the field of plant protection and biological control, and relates to a novel function of a degradation product of Bacillus subtilis GGT protein and identification of an antibacterial peptide. Background technique [0002] Potatoes are widely planted as the main food crop in my country, second only to rice, wheat and corn. In recent years, potatoes have gradually become an important economic source in many provinces, and high-quality seed potatoes are the basis of this economic source. Potato scab mainly spreads in the soil and is highly susceptible to infection during potato planting. In recent years, potato scab caused by Streptomyces scabica has become increasingly serious, directly affecting the quality of potatoes and causing huge economic losses to the potato industry. [0003] Plant diseases caused by pathogenic microorganisms have seriously hindered the development of agriculture in our country. Extensive use of chemica...

Claims

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Application Information

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IPC IPC(8): C12N9/10A01N37/46A01N63/00A01P1/00
CPCA01N37/46A01N63/00C12N9/1044C12Y203/02013
Inventor 刘权殷奎德申永瑞宋烨向君亮王佳琦张竹君
Owner HEILONGJIANG BAYI AGRICULTURAL UNIVERSITY
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