Current antibiotics cannot eradicate uropathogenic Escherichia coli (UPEC) biofilms, leading to recurrent urinary tract infections. Here, we show that the insect antimicrobial peptide cecropin A (CecA) can destroy planktonic and sessile biofilm-forming UPEC cells, either alone or when combined with the antibiotic nalidixic acid (NAL), synergistically clearing infection in vivo without off-target cytotoxicity. The multi-target mechanism of action involves outer membrane permeabilization followed by biofilm disruption triggered by the inhibition of efflux pump activity and interactions with extracellular and intracellular nucleic acids. These diverse targets ensure that resistance to the CecA + NAL combination emerges slowly. The antimicrobia...
Microbes are known to colonize surfaces and form biofilms. These biofilms are communities of microbe...
Antimicrobial cationic peptides have been discovered in many different organisms and often possess a...
Cecropins are small helical secreted peptides with antimicrobial activity that are widely distribute...
Biofilms, sedimented microbial communities embedded in a biopolymer matrix cause vast majority of hu...
AbstractLong-chain proline-rich antimicrobial peptides such as bumblebee abaecin show minimal activi...
Long-chain proline-rich antimicrobial peptides such as bumblebee abaecin show minimal activity again...
Cecropin A and papiliocin are novel 37-residue cecropin-likeantimicrobial peptides isolated from ins...
The increasing prevalence of antibiotic resistance has created an urgent need for alternative drugs ...
The bacterial processivity factor, or sliding clamp (SC), is a target of choice for new antibacteria...
The rise of multidrug-resistant Acinetobacter baumannii and a concomitant decrease in antibiotic tre...
Cecropins, originally found in insects, are a group of cationic antimicrobial peptides. Most cecropi...
Bacteria are exceptionally adept at acquiring resistance to antibiotics and antiseptic agents, hence...
In recent decades much attention has been paid to antimicrobial peptides (AMPs) as natural antibioti...
The alarming escalation of infectious diseases resistant to conventional antibiotics requires urgent...
Antimicrobial peptides (AMPs) are ubiquitous components of the insect innate immune system. The mode...
Microbes are known to colonize surfaces and form biofilms. These biofilms are communities of microbe...
Antimicrobial cationic peptides have been discovered in many different organisms and often possess a...
Cecropins are small helical secreted peptides with antimicrobial activity that are widely distribute...
Biofilms, sedimented microbial communities embedded in a biopolymer matrix cause vast majority of hu...
AbstractLong-chain proline-rich antimicrobial peptides such as bumblebee abaecin show minimal activi...
Long-chain proline-rich antimicrobial peptides such as bumblebee abaecin show minimal activity again...
Cecropin A and papiliocin are novel 37-residue cecropin-likeantimicrobial peptides isolated from ins...
The increasing prevalence of antibiotic resistance has created an urgent need for alternative drugs ...
The bacterial processivity factor, or sliding clamp (SC), is a target of choice for new antibacteria...
The rise of multidrug-resistant Acinetobacter baumannii and a concomitant decrease in antibiotic tre...
Cecropins, originally found in insects, are a group of cationic antimicrobial peptides. Most cecropi...
Bacteria are exceptionally adept at acquiring resistance to antibiotics and antiseptic agents, hence...
In recent decades much attention has been paid to antimicrobial peptides (AMPs) as natural antibioti...
The alarming escalation of infectious diseases resistant to conventional antibiotics requires urgent...
Antimicrobial peptides (AMPs) are ubiquitous components of the insect innate immune system. The mode...
Microbes are known to colonize surfaces and form biofilms. These biofilms are communities of microbe...
Antimicrobial cationic peptides have been discovered in many different organisms and often possess a...
Cecropins are small helical secreted peptides with antimicrobial activity that are widely distribute...