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

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.

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.

scholarly journals Beta-Lactamase Repressor BlaI Modulates Staphylococcus aureus Cathelicidin Antimicrobial Peptide Resistance and Virulence

PLoS ONE ◽  
2015 ◽  
Vol 10 (8) ◽  
pp. e0136605 ◽  
Author(s):  
Morgan A. Pence ◽  
Nina M. Haste ◽  
Hiruy S. Meharena ◽  
Joshua Olson ◽  
Richard L. Gallo ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Antimicrobial Peptide ◽  
Beta Lactamase ◽  
Antimicrobial Peptide Resistance

scholarly journals A Protein Important for Antimicrobial Peptide Resistance, YdeI/OmdA, Is in the Periplasm and Interacts with OmpD/NmpC

2009 ◽  
Vol 191 (23) ◽  
pp. 7243-7252 ◽  
Author(s):  
M. Carolina Pilonieta ◽  
Kimberly D. Erickson ◽  
Robert K. Ernst ◽  
Corrella S. Detweiler
Keyword(s):  
Gene Expression ◽  
Antimicrobial Peptide ◽  
Bacterial Resistance ◽  
Cell Types ◽  
Polymyxin B ◽  
Sensor Kinase ◽  
Multiple Cell ◽  
Ob Fold ◽  
Antimicrobial Peptide Resistance ◽  
Multicellular Organisms

ABSTRACT Antimicrobial peptides (AMPs) kill or prevent the growth of microbes. AMPs are made by virtually all single and multicellular organisms and are encountered by bacteria in diverse environments, including within a host. Bacteria use sensor-kinase systems to respond to AMPs or damage caused by AMPs. Salmonella enterica deploys at least three different sensor-kinase systems to modify gene expression in the presence of AMPs: PhoP-PhoQ, PmrA-PmrB, and RcsB-RcsC-RcsD. The ydeI gene is regulated by the RcsB-RcsC-RcsD pathway and encodes a 14-kDa predicted oligosaccharide/oligonucleotide binding-fold (OB-fold) protein important for polymyxin B resistance in broth and also for virulence in mice. We report here that ydeI is additionally regulated by the PhoP-PhoQ and PmrA-PmrB sensor-kinase systems, which confer resistance to cationic AMPs by modifying lipopolysaccharide (LPS). ydeI, however, is not important for known LPS modifications. Two independent biochemical methods found that YdeI copurifies with OmpD/NmpC, a member of the trimeric β-barrel outer membrane general porin family. Genetic analysis indicates that ompD contributes to polymyxin B resistance, and both ydeI and ompD are important for resistance to cathelicidin antimicrobial peptide, a mouse AMP produced by multiple cell types and expressed in the gut. YdeI localizes to the periplasm, where it could interact with OmpD. A second predicted periplasmic OB-fold protein, YgiW, and OmpF, another general porin, also contribute to polymyxin B resistance. Collectively, the data suggest that periplasmic OB-fold proteins can interact with porins to increase bacterial resistance to AMPs.

scholarly journals Antimicrobial peptide resistance mediates resilience of prominent gut commensals during inflammation

Science ◽  
2015 ◽  
Vol 347 (6218) ◽  
pp. 170-175 ◽  
Author(s):  
T. W. Cullen ◽  
W. B. Schofield ◽  
N. A. Barry ◽  
E. E. Putnam ◽  
E. A. Rundell ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Antimicrobial Peptide Resistance

scholarly journals ABC Transporter DerAB of Lactobacillus casei Mediates Resistance against Insect-Derived Defensins

2020 ◽  
Vol 86 (14) ◽  
Author(s):  
Ainhoa Revilla-Guarinos ◽  
Qian Zhang ◽  
Christoph Loderer ◽  
Cristina Alcántara ◽  
Ariane Müller ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Abc Transporter ◽  
Lactobacillus Casei ◽  
Biological Effects ◽  
Gc Content ◽  
Resistance Response ◽  
Content Type ◽  
Antimicrobial Peptide Resistance ◽  
High Level

ABSTRACT Bce-like systems mediate resistance against antimicrobial peptides in Firmicutes bacteria. Lactobacillus casei BL23 encodes an “orphan” ABC transporter that, based on homology to BceAB-like systems, was proposed to contribute to antimicrobial peptide resistance. A mutant lacking the permease subunit was tested for sensitivity against a collection of peptides derived from bacteria, fungi, insects, and humans. Our results show that the transporter specifically conferred resistance against insect-derived cysteine-stabilized αβ defensins, and it was therefore renamed DerAB for defensin resistance ABC transporter. Surprisingly, cells lacking DerAB showed a marked increase in resistance against the lantibiotic nisin. This could be explained by significantly increased expression of the antimicrobial peptide resistance determinants regulated by the Bce-like systems PsdRSAB (formerly module 09) and ApsRSAB (formerly module 12). Bacterial two-hybrid studies in Escherichia coli showed that DerB could interact with proteins of the sensory complex in the Psd resistance system. We therefore propose that interaction of DerAB with this complex in the cell creates signaling interference and reduces the cell’s potential to mount an effective nisin resistance response. In the absence of DerB, this negative interference is relieved, leading to the observed hyperactivation of the Psd module and thus increased resistance to nisin. Our results unravel the function of a previously uncharacterized Bce-like orphan resistance transporter with pleiotropic biological effects on the cell. IMPORTANCE Antimicrobial peptides (AMPs) play an important role in suppressing the growth of microorganisms. They can be produced by bacteria themselves—to inhibit competitors—but are also widely distributed in higher eukaryotes, including insects and mammals, where they form an important component of innate immunity. In low-GC-content Gram-positive bacteria, BceAB-like transporters play a crucial role in AMP resistance but have so far been primarily associated with interbacterial competition. Here, we show that the orphan transporter DerAB from the lactic acid bacterium Lactobacillus casei is crucial for high-level resistance against insect-derived AMPs. It therefore represents an important mechanism for interkingdom defense. Furthermore, our results support a signaling interference from DerAB on the PsdRSAB module that might prevent the activation of a full nisin response. The Bce modules from L. casei BL23 illustrate a biological paradox in which the intrinsic nisin detoxification potential only arises in the absence of a defensin-specific ABC transporter.

Sign in / Sign up

Export Citation Format

Share Document