Cationic antimicrobial peptides (CAMPs) play an important role in host defense against microbial infection and are key components of the innate immune response. These are found among all classes of life ranging from prokaryotes to humans. In addition to the natural peptides, thousands of synthetic variants have been produced. CAMPs weaken the integrity of the bacterial inner and outer membranes and subsequently kill bacterial cells. On the other hand, bacteria have developed a number of mechanisms against CAMPs. These resistance mechanisms include decreased affinity to CAMPs by substitution of anionic cell surface constituents with cationic molecules; biosynthesis and crosslinking of cell envelope components; external trapping mechanisms that bind or neutralize the CAMPs by direct secretion of proteins, or the release of CAMPs binding molecules from the host cell surface; membrane efflux pumps; and production of peptidases.
A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose.
Transcriptome profiling reveals links between ParS/ParR, MexEF-OprN, and quorum sensing in the regulation of adaptation and virulence in Pseudomonas aeruginosa.
GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus.
A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.
Weatherspoon-Griffin N, Yang D, Kong W, Hua Z, Shi Y
Title
The CpxR/CpxA two-component regulatory system up-regulates the multidrug resistance cascade to facilitate Escherichia coli resistance to a model antimicrobial peptide.
