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Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
The role of cationic host-defense peptides in modulating the innate immune response and boosting infection-resolving immunity while dampening potentially harmful pro-inflammatory (septic) responses gives these peptides the potential to become an entirely new therapeutic approach against bacterial infections.
The co-evolution of host cationic antimicrobial peptides and microbial resistance
It is proposed that CAMPs and CAMP-resistance mechanisms have co-evolved, leading to a transient host–pathogen balance that has shaped the existing CAMP repertoire.
Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.
This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. The
Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic.
It is shown that vancomycin and the antibacterial peptide nisin Z use the same target: the membrane-anchored cell wall precursor Lipid II, thus causing the peptide to be highly active (in the nanomolar range).
Specific Binding of Nisin to the Peptidoglycan Precursor Lipid II Combines Pore Formation and Inhibition of Cell Wall Biosynthesis for Potent Antibiotic Activity*
Genetically engineered nisin variants are used to identify the structural requirements for the interaction of the peptide with lipid II, and the remaining in vivo activity is found to result from the unaltered capacity of the mutated peptide to bind to lipid II and thus to inhibit its incorporation into the peptidoglycan network.
Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria.
The fundamental aspects of the biosynthetic machinery, which include information for the antibiotic prepeptide, the modification enzymes and accessory functions such as dedicated proteases and ABC transporters as well as immunity factors and regulatory proteins, are discussed along with the biotechnological potential of the peptides and of the enzymes, which could be used for construction of novel, peptide-based biomedical effector molecules.
Lantibiotics: mode of action, biosynthesis and bioengineering.
In vitro modification systems have successfully been used to introduce thioether rings into other biologically active peptides and at least one promising new lantibiotic with strong activity against multiresistant pathogens has been described.
Dysregulation of bacterial proteolytic machinery by a new class of antibiotics
A new class of antibiotics is shown to have antibacterial activity against Gram-positive bacteria in vitro and in several rodent models of bacterial infection, implying a new target, which is identified as ClpP, the core unit of a major bacterial protease complex.
Biosynthesis and biological activities of lantibiotics with unique post-translational modifications.
Lantibiotics are biologically active peptides which contain the thioether amino acid lanthionine as well as several other modified amino acids which are synthesised on the ribosome as a prepeptide which undergoes several post-translational modification events, including dehydration of specific hydroxyl amino acids to form dehydroamino acids.
Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC. Evidence for a role of PepC in thioether formation.
It is demonstrated that PepC is a thioether-forming protein and strongly suggest that PepB is responsible for dehydration of serine and threonine in the cells without excretion of processed peptide.