Evolutionary constraints on the acquisition of antimicrobial peptide resistance in bacterial pathogens

2021 ◽  
Author(s):  
Pramod K. Jangir ◽  
Lois Ogunlana ◽  
R. Craig MacLean
Keyword(s):  
Antimicrobial Peptide ◽  
Bacterial Pathogens ◽  
Evolutionary Constraints ◽  
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.

Aminoarabinose is essential for lipopolysaccharide export and intrinsic antimicrobial peptide resistance inBurkholderia cenocepacia†

2012 ◽  
Vol 85 (5) ◽  
pp. 962-974 ◽  
Author(s):  
Mohamad A. Hamad ◽  
Flaviana Di Lorenzo ◽  
Antonio Molinaro ◽  
Miguel A. Valvano
Keyword(s):  
Antimicrobial Peptide ◽  
Antimicrobial Peptide Resistance

scholarly journals In vitroeffectiveness of the antimicrobial peptide eCATH1 against antibiotic-resistant bacterial pathogens of horses

2013 ◽  
Vol 350 (2) ◽  
pp. 216-222 ◽  
Author(s):  
Margot Schlusselhuber ◽  
Kristen Guldbech ◽  
Corinne Sevin ◽  
Matthias Leippe ◽  
Sandrine Petry ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Bacterial Pathogens ◽  
Antibiotic Resistant

scholarly journals Antimicrobial peptide based magnetic recognition elements and Au@Ag-GO SERS tags with stable internal standards: a three in one biosensor for isolation, discrimination and killing of multiple bacteria in whole blood

2018 ◽  
Vol 9 (47) ◽  
pp. 8781-8795 ◽  
Author(s):  
Kaisong Yuan ◽  
Qingsong Mei ◽  
Xinjie Guo ◽  
Youwei Xu ◽  
Danting Yang ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Whole Blood ◽  
Bacterial Pathogens ◽  
Internal Standards ◽  
Recognition Elements ◽  
Sers Tags

A SERS based biosensor has been developed for isolation, detection and killing of multiple bacterial pathogens.

scholarly journals An iron-regulated LysR-type element mediates antimicrobial peptide resistance and virulence in Yersinia pseudotuberculosis

Microbiology ◽  
2009 ◽  
Vol 155 (7) ◽  
pp. 2168-2181 ◽  
Author(s):  
Sonia Arafah ◽  
Marie-Laure Rosso ◽  
Linda Rehaume ◽  
Robert E. W. Hancock ◽  
Michel Simonet ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Yersinia Pseudotuberculosis ◽  
Polymyxin B ◽  
Uptake System ◽  
Mesenteric Lymph Nodes ◽  
Iron Starvation ◽  
Iron Deprivation ◽  
Genes Encoding ◽  
Antimicrobial Peptide Resistance

During the course of its infection of the mammalian digestive tract, the entero-invasive, Gram-negative bacterium Yersinia pseudotuberculosis must overcome various hostile living conditions (notably, iron starvation and the presence of antimicrobial compounds produced in situ). We have previously reported that in vitro bacterial growth during iron deprivation raises resistance to the antimicrobial peptide polymyxin B; here, we show that this phenotype is mediated by a chromosomal gene (YPTB0333) encoding a transcriptional regulator from the LysR family. We determined that the product of YPTB0333 is a pleiotropic regulator which controls (in addition to its own expression) genes encoding the Yfe iron-uptake system and polymyxin B resistance. Lastly, by using a mouse model of oral infection, we demonstrated that YPTB0333 is required for colonization of Peyer's patches and mesenteric lymph nodes by Y. pseudotuberculosis.

scholarly journals SSD1 Is Integral to Host Defense Peptide Resistance in Candida albicans

2008 ◽  
Vol 7 (8) ◽  
pp. 1318-1327 ◽  
Author(s):  
Kimberly D. Gank ◽  
Michael R. Yeaman ◽  
Satoshi Kojima ◽  
Nannette Y. Yount ◽  
Hyunsook Park ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Host Defense ◽  
Genomic Library ◽  
Inflammatory Responses ◽  
Host Defense Peptides ◽  
Antimicrobial Peptide Resistance ◽  
Null Mutants

ABSTRACT Candida albicans is usually a harmless human commensal. Because inflammatory responses are not normally induced by colonization, antimicrobial peptides are likely integral to first-line host defense against invasive candidiasis. Thus, C. albicans must have mechanisms to tolerate or circumvent molecular effectors of innate immunity and thereby colonize human tissues. Prior studies demonstrated that an antimicrobial peptide-resistant strain of C. albicans, 36082R, is hypervirulent in animal models versus its susceptible counterpart (36082S). The current study aimed to identify a genetic basis for antimicrobial peptide resistance in C. albicans. Screening of a C. albicans genomic library identified SSD1 as capable of conferring peptide resistance to a susceptible surrogate, Saccharomyces cerevisiae. Sequencing confirmed that the predicted translation products of 36082S and 36082R SSD1 genes were identical. However, Northern analyses corroborated that SSD1 is expressed at higher levels in 36082R than in 36082S. In isogenic backgrounds, ssd1Δ/ssd1Δ null mutants were significantly more susceptible to antimicrobial peptides than parental strains but had equivalent susceptibilities to nonpeptide stressors. Moreover, SSD1 complementation of ssd1Δ/ssd1Δ mutants restored parental antimicrobial peptide resistance phenotypes, and overexpression of SSD1 conferred enhanced peptide resistance. Consistent with these in vitro findings, ssd1 null mutants were significantly less virulent in a murine model of disseminated candidiasis than were their parental or complemented strains. Collectively, these results indicate that SSD1 is integral to C. albicans resistance to host defense peptides, a phenotype that appears to enhance the virulence of this organism in vivo.

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