Lysostaphin

lysostaphin is an endopeptidase produced by Staphylococcus staphylolyticus that can cleave S. aureus. The hydrolysis site is the glycyl-glycyl peptide bridge in the staphylococcal peptidoglycan molecule. It can be used to reduce the number of staphylococci in the patient's nasal cavity and throat. It can also be used to treat infections caused by staphylococci that are resistant to β-lactam antibiotics.

Introductions

Lysostaphin is a kind of Staphylococcus aureus mimicking metal endopeptidase (crystal structure of lysostaphin). It can be used as an antibacterial agent against Staphylococcus aureus. Lysostaphin is a 27 KDa glycylglycine endopeptidase, an antibacterial enzyme that can cleave the cross-linked pentaglycine bridges found in certain staphylococcal cell wall peptidoglycans. Lysostaphin was first isolated by Schindler and Schulter from staphylococcus simulans culture in 1964. Staphylococcus aureus cell walls contain a high proportion of pentaglycine, making lysostaphin a highly effective drug against active and stationary bacteria.

Harm

Staphylococcus aureus and Staphylococcus epidermidis infections are still major problems in clinical settings, especially those with implantable devices. Staphylococci cause a large number of device infections, and like many other pathogens, they do not live in the form of free planktonic cells within the host, but rather have the formation of sessile bacterial cells (called biofilms) on implantable devices. The ability of the stratum community. Once the "staphylococcus" biofilm is formed on the implanted medical device, it is difficult to destroy due to its drug resistance and protection against bacterial action.

Research progress

Since the isolation of lysostaphin, many studies have previously been conducted in vivo and in vitro. Lysostaphin has been shown to eradicate susceptible S. aureus biofilms. According to reports, despite the higher concentration of the enzyme, it can effectively destroy the biofilm of Staphylococcus epidermidis in vitro. Compared with commonly used antibiotics such as vancomycin, lysostaphin has shown higher antibacterial activity in vitro. In rabbit models, the enzyme has been shown to be effective against methicillin-sensitive Staphylococcus aureus (MSSA) and methicillin-resistant Staphylococcus aureus (MRSA)-mediated keratitis. In addition, it has been shown that the combination of lysostaphin and antimicrobial drugs such as cefazolin, clarithromycin, doxycycline, levofloxacin, linezolid, and quinupristin/dafopristine is synergistic to the bacterial MSSA strains effect. A study published by Belyansky et al. As an example, the lysostaphin-conjugated mesh showed a surprising preservation effect in the rat model. The use of lysostaphin to treat "staphylococcus" biofilm-related infections may prove to be preferable to antibiotics, because the enzyme may be administered at a relatively low dose and destroy the staphylococcus biofilm, so there is no need to remove the infected device by surgery.

Conclusions

Lysostaphin (lysostaphin, Lys) is a protein produced by gene cloning technology to enable exogenous expression of lysostaphin gene. It is a Zn²⁺-dependent metalloprotease with endopeptidase activity, which can specifically hydrolyze the staphylococcus cell wall Gly pentapeptide bridge, so that the cell wall of Staphylococcus aureus (especially MRSA) is ruptured to achieve bacteriolysis and disinfection Does not produce drug resistance. As an antibacterial agent, it has great application potential in veterinary medicine and clinical fields.

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