Anti-wild lysobacter drug and application thereof

Abstract

The invention belongs to the technical field of antibacterial drugs, and discloses an anti-wild lysobacter drug and an application thereof, and the anti-wild lysobacter drug is composed of 2 [mu]g / mLTPAD and 5 pM LED209. A low concentration of TPAD is capable of activating a QseC / B bi-component system (QseC is a membrane-bound sensor protein having histidine kinase activity and QseB is a cytoplasmic response modulator). In the lysobacter with the QseC or QseB gene knocked out, the TPAD can play a stronger antibacterial effect. The invention finds that efficient antibacterial activity can be generated when 2[mu] g / mL of TPAD and 5pM LED209 are used in combination.

Description

technical field [0001] The invention belongs to the technical field of antimicrobial drugs, in particular to a drug against wild roebacteria and its application. Background technique [0002] Currently, the closest prior art: TAL is a class of antimicrobial peptides present in lymphatic granulosa cells of horseshoe crabs. Among them, Tachyplesin I (TPI) was isolated from the stem cells of Tachypleus tridentatus for the first time. TPI has broad-spectrum antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. However, follow-up studies have shown that: as a polypeptide, TPI has poor stability in plasma and is easily degraded. TPI can easily cause mammalian red blood cell membrane rupture and hemolysis during the antibacterial process. In addition, the antibacterial activity of TPI is still not strong enough, and the antibacterial activity is lower than that of current clinical drugs. This shortcoming greatly limits its clinical application. [00...

AI Technical Summary

Problems solved by technology

However, follow-up studies have shown that: as a polypeptide, TPI has poor stability in plasma and is easily degraded. TPI can easily cause mammalian red blood cell membrane rupture and hemolysis during the antibacterial process.

In addition, the antibacterial activity of TPI is still not strong enough, and the antibacterial activity is lower than that of current clinical drugs.

This shortcoming greatly limits its clinical application

[0003] In summary, the existing problems in the prior art are: TPI has insufficient activity and poor stability in the antibacterial process, and is easily degraded. In addition, it is also easy to cause hemolysis of mammalian erythrocytes, which greatly limits its clinical application. application

[0005] At present, the modification of TPI activity is mainly based on the sequence scanning screening method, but the extent of its activity improvement is very limited

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