scholarly journals Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogens

2015 ◽  
Vol 1848 (11) ◽  
pp. 3047-3054 ◽  
Author(s):  
Christopher N. LaRock ◽  
Victor Nizet
Keyword(s):  
Antimicrobial Peptide ◽  
Resistance Mechanisms ◽  
Cationic Antimicrobial Peptide ◽  
Antimicrobial Peptide Resistance

scholarly journals Experimental Induction of Bacterial Resistance to the Antimicrobial Peptide Tachyplesin I and Investigation of the Resistance Mechanisms

2016 ◽  
Vol 60 (10) ◽  
pp. 6067-6075 ◽  
Author(s):  
Jun Hong ◽  
Jianye Hu ◽  
Fei Ke
Keyword(s):  
Antimicrobial Peptide ◽  
Bacterial Resistance ◽  
Antimicrobial Agents ◽  
Resistance Mechanisms ◽  
Cross Resistance ◽  
Antibacterial Drug ◽  
Cationic Antimicrobial Peptide ◽  
Content Type ◽  
Tachyplesin I

ABSTRACTTachyplesin I is a 17-amino-acid cationic antimicrobial peptide (AMP) with a typical cyclic antiparallel β-sheet structure that is a promising therapeutic for infections, tumors, and viruses. To date, no bacterial resistance to tachyplesin I has been reported. To explore the safety of tachyplesin I as an antibacterial drug for wide clinical application, we experimentally induced bacterial resistance to tachyplesin I by using two selection procedures and studied the preliminary resistance mechanisms.Aeromonas hydrophilaXS91-4-1,Pseudomonas aeruginosaCGMCC1.2620, andEscherichia coliATCC 25922 and F41 showed resistance to tachyplesin I under long-term selection pressure with continuously increasing concentrations of tachyplesin I. In addition,P. aeruginosaandE. coliexhibited resistance to tachyplesin I under UV mutagenesis selection conditions. Cell growth and colony morphology were slightly different between control strains and strains with induced resistance. Cross-resistance to tachyplesin I and antimicrobial agents (cefoperazone and amikacin) or other AMPs (pexiganan, tachyplesin III, and polyphemusin I) was observed in some resistant mutants. Previous studies showed that extracellular protease-mediated degradation of AMPs induced bacterial resistance to AMPs. Our results indicated that the resistance mechanism ofP. aeruginosawas not entirely dependent on extracellular proteolytic degradation of tachyplesin I; however, tachyplesin I could induce increased proteolytic activity inP. aeruginosa. Most importantly, our findings raise serious concerns about the long-term risks associated with the development and clinical use of tachyplesin I.

scholarly journals Identification of a Genetic Locus Responsible for Antimicrobial Peptide Resistance inClostridium difficile

2010 ◽  
Vol 79 (1) ◽  
pp. 167-176 ◽  
Author(s):  
Shonna M. McBride ◽  
Abraham L. Sonenshein
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Abc Transporter ◽  
Genetic Locus ◽  
Polymyxin B ◽  
Transcriptional Analysis ◽  
Cationic Antimicrobial Peptide ◽  
Low Levels ◽  
Antimicrobial Peptide Resistance ◽  
Abc Transporter Genes

ABSTRACTClostridium difficilecauses chronic intestinal disease, yet little is understood about how the bacterium interacts with and survives in the host. To colonize the intestine and cause persistent disease, the bacterium must circumvent killing by host innate immune factors, such as cationic antimicrobial peptides (CAMPs). In this study, we investigated the effect of model CAMPs on growth and found thatC. difficileis not only sensitive to these compounds but also responds to low levels of CAMPs by expressing genes that lead to CAMP resistance. By plating the bacterium on medium containing the CAMP nisin, we isolated a mutant capable of growing in three times the inhibitory concentration of CAMPs. This mutant also showed increased resistance to the CAMPs gallidermin and polymyxin B, demonstrating tolerance to different types of antimicrobial peptides. We identified the mutated gene responsible for the resistance phenotype as CD1352. This gene encodes a putative orphan histidine kinase that lies adjacent to a predicted ABC transporter operon (CD1349 to CD1351). Transcriptional analysis of the ABC transporter genes revealed that this operon was upregulated in the presence of nisin in wild-type cells and was more highly expressed in the CD1352 mutant. The insertional disruption of the CD1349 gene resulted in significant decreases in resistance to the CAMPs nisin and gallidermin but not polymyxin B. Because of their role in cationic antimicrobial peptide resistance, we propose the designationcprABCfor genes CD1349 to CD1351 andcprKfor the CD1352 gene. These results provide the first evidence of aC. difficilegene associated with antimicrobial peptide resistance.

scholarly journals Antimicrobial Peptide Resistance Mechanisms of Gram-Positive Bacteria

Antibiotics ◽  
2014 ◽  
Vol 3 (4) ◽  
pp. 461-492 ◽  
Author(s):  
Kathryn Nawrocki ◽  
Emily Crispell ◽  
Shonna McBride
Keyword(s):  
Antimicrobial Peptide ◽  
Resistance Mechanisms ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Antimicrobial Peptide Resistance

Potential Antimicrobial Peptides Elucidation From The Marine Bacteria

2020 ◽  
Vol 18 ◽  
Author(s):  
Adyasa Barik ◽  
Pandiyan Rajesh ◽  
Manthiram Malathi ◽  
Vellaisamy Balasubramanian
Keyword(s):  
Antimicrobial Peptide ◽  
Marine Bacteria ◽  
Unnatural Amino Acids ◽  
Wide Spectrum ◽  
Drug Resistant ◽  
Medical Field ◽  
The World ◽  
Pathogenic Microbes ◽  
Antimicrobial Peptide Resistance ◽  
Significant Attention

: In recent years, over use of antibiotics has been raising its head to a serious problem all around the world as pathogens become drug resistant and create challenges to the medical field. This failure of most potent antibiotics that kill pathogens increases the thirst for research to look further way of killing pathogens. It has been led to the findings of antimicrobial peptide which is the most potent peptide to destroy pathogens. This review gives special emphasis to the usage of marine bacteria and other microorganisms for antimicrobial peptide (AMP) which are eco friendly as well as a developing class of natural and synthetic peptides with a wide spectrum of targets to pathogenic microbes. Consequently, a significant attention has been paid mainly to (i) the structure and types of anti microbial peptides and (ii) mode of action and mechanism of antimicrobial peptide resistance to pathogens. In addition to this, the designing of AMPs has been analysed thoroughly for reducing toxicity and developing better potent AMP. It has been done by the modified unnatural amino acids by amidation to target the control of biofilm and persister cell.

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