The co-evolution of host cationic antimicrobial peptides and microbial resistance
By A. Peschel, H. Sahl. Nature Reviews Microbiology, 2006
1,080 citations recorded by the source corpus.
Subfields: Food Science, Microbiology, Molecular Medicine
View Paper: https://www.semanticscholar.org/paper/4f03083224766c7f3f64ee733aea12b764e79b7d
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Food Science
In Microbiology
- Robert E. W. Hancock
- H. Jenssen
- Christopher Weidenmaier
- G. Diamond
- Christopher D. Fjell
- A. Peschel
- H. Sahl
- N. Beckloff
In Molecular Medicine
- Robert E. W. Hancock
- Christopher Weidenmaier
- A. Peschel
- Carolina S. Silva
- Stefan H. E. Kaufmann
- M. O. Santos
- William R. Miller
- V. C. de Souza
Citations in the corpus
- Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies (2006, background): “It seems possible that the rapid coevolution of host-defense peptides, of innate immune systems of which they are a part, as well as of corresponding microbial counter strategies, including resistance and virulence (anti-immunity) strategies, has helped to drive diversity in all biological kingdom”
- Comparative Metagenomics Revealed Commonly Enriched Gene Sets in Human Gut Microbiomes (2007, background): “Host intestinal cells produce various cationic antimicrobial peptides (CAMPs), such as beta-defensins.(43) Many microorganisms also produce CAMPs to compete with other microbes sharing the same niche.”
- Mycobacterium tuberculosis: Success through dormancy (2012, background): “Microorganisms lower their affinity to CAMPs by reduction of their negative surface charge (Peschel & Sahl, 2006).”
- Mechanisms of antibiotic resistance in enterococci (2014, background): “These CAMPs possess a wide array of antimicrobial properties (including the ability to disrupt peptidoglycan synthesis, CM structure and activate autolysins) and individual proteins often display multiple modes of action, which may in part explain their effectiveness in the face of everevolving bact”
- Highly active and selective endopeptidases with programmed substrate specificities. (2008, background): “The β -defensins are cationic antimicrobial peptides that consist of compactly folded β -sheets held together by multiple disulfide bonds, which renders them resistant to bacterial proteolysis 24 .”
- Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions (2008, result): “This could explain the limited impact of CWG deficiency under laboratory conditions, and is supported by previous findings which show that altering the structure or amounts of CWGs increases the susceptibility of bacteria to cationic antimicrobial peptides and antibiotic”
- Strategies and molecular tools to fight antimicrobial resistance: resistome, transcriptome, and antimicrobial peptides (2013, background): “…antimicrobial peptides (CAMPs) or ribosomally synthesized antimicrobial peptides (RAMPs) (Perron et al., 2006), and requires interaction with microbial membrane lipids and hydrophobic properties to enable integration of the peptide into the hydrophobic core of the membrane (Peschel and Sahl, 2006).”
- Designing antimicrobial peptides: form follows function (2011, background): “…AMPs include cell surface modification (which can occur adaptively through the twocomponent regulator PhoPQ, for example), exter nal trapping of AMPs, active efflux of AMPs, proteolytic degradation, as well as the suppression of host path ways by the pathogen for the production of AMPs 39,41 .”
- The Roles of Antimicrobial Peptides in Innate Host Defense (2009, background): “Regardless, bacterial species have developed mechanisms to modify even these important structures by even partially neutralizing the envelope and inhibiting the interactions with the peptides (reviewed in [93]).”
- Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs. (2009, background): “For different peptides this can result in either disruption of membrane barriers or translocation across the membrane to attack cytosolic targets, and most peptides are considered “dirty drugs” that attack multiple targets (11).”