Investigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action

2013 ◽  
Vol 115 (3) ◽  
pp. 663-672 ◽  
Author(s):  
X. Bi ◽  
C. Wang ◽  
L. Ma ◽  
Y. Sun ◽  
D. Shang
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Action ◽  
Cationic Antimicrobial Peptides ◽  
Tryptophan Residues

scholarly journals A comparative, cross-species investigation of the properties and roles of transferrin- and lactoferrin-binding protein B from pathogenic bacteria

2017 ◽  
Vol 95 (1) ◽  
pp. 5-11 ◽  
Author(s):  
N. Ostan ◽  
A. Morgenthau ◽  
R.H. Yu ◽  
S.D. Gray-Owen ◽  
A.B. Schryvers
Keyword(s):  
Antimicrobial Peptides ◽  
Protective Effect ◽  
Transgenic Mouse ◽  
Pathogenic Bacteria ◽  
Binding Protein ◽  
Host Proteins ◽  
Cationic Antimicrobial Peptides ◽  
Surface Receptors ◽  
Protein B

Pathogenic bacteria from the families Neisseriaeceae and Moraxellaceae acquire iron from their host using surface receptors that have the ability to hijack iron from the iron-sequestering host proteins transferrin (Tf) and lactoferrin (Lf). The process of acquiring iron from Tf has been well-characterized, including the role of the surface lipoprotein transferrin-binding protein B (TbpB). In contrast, the only well-defined role for the homologue, LbpB, is in its protection against cationic antimicrobial peptides, which is mediated by regions present in some LbpBs that are highly enriched in glutamic or aspartic acid. In this study we compare the Tf-TbpB and the Lf-LbpB interactions and examine the protective effect of LbpB against extracts from human and transgenic mouse neutrophils to gains insights into the physiological roles of LbpB. The results indicate that in contrast to the Tf-TbpB interaction, Lf-LbpB interaction is sensitive to pH and varies between species. In addition, the results with transgenic mouse neutrophils raise the question of whether there is species specificity in the cleavage of Lf to generate cationic antimicrobial peptides or differences in the potency of peptides derived from mouse and human Lf.

scholarly journals MprF-Mediated Lysinylation of Phospholipids in Staphylococcus aureus Leads to Protection against Oxygen-Independent Neutrophil Killing

2003 ◽  
Vol 71 (1) ◽  
pp. 546-549 ◽  
Author(s):  
Sascha A. Kristian ◽  
Manuela Dürr ◽  
Jos A. G. Van Strijp ◽  
Birgid Neumeister ◽  
Andreas Peschel
Keyword(s):  
Staphylococcus Aureus ◽  
Antimicrobial Peptides ◽  
Host Defense ◽  
Membrane Lipids ◽  
Human Monocytes ◽  
Wild Type ◽  
Cationic Antimicrobial Peptides ◽  
The Impact ◽  
Defense Molecules

ABSTRACT Staphylococcus aureus achieves resistance to defensins and similar cationic antimicrobial peptides (CAMPs) by modifying anionic membrane lipids via MprF with l-lysine, which leads to repulsion of these host defense molecules. S. aureus ΔmprF, which lacks the modification, was very efficiently killed by neutrophil defensins and CAMP-producing leukocytes, even when oxygen-dependent killing was disrupted, but was as susceptible as wild-type bacteria to inactivation by myeloperoxidase or human monocytes lacking defensins. These results demonstrate the impact and specificity of MprF-mediated CAMP resistance and underscore the role of defensin-like peptides in innate host defense.

scholarly journals The Staphylococcus aureus Two-Component Regulatory System, GraRS, Senses and Confers Resistance to Selected Cationic Antimicrobial Peptides

2011 ◽  
Vol 80 (1) ◽  
pp. 74-81 ◽  
Author(s):  
Soo-Jin Yang ◽  
Arnold S. Bayer ◽  
Nagendra N. Mishra ◽  
Michael Meehl ◽  
Nagender Ledala ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Positive Charge ◽  
Efflux Pump ◽  
Regulatory System ◽  
Polymyxin B ◽  
Cationic Antimicrobial Peptides ◽  
Two Component ◽  
Mrsa Strains ◽  
Reduced Surface

ABSTRACTThe two-component regulatory system, GraRS, appears to be involved in staphylococcal responses to cationic antimicrobial peptides (CAPs). However, the mechanism(s) by which GraRS is induced, regulated, and modulated remain undefined. In this study, we used two well-characterized MRSA strains (Mu50 and COL) and their respective mutants ofgraRandvraG(encoding the ABC transporter-dependent efflux pump immediately downstream ofgraRS), and show that (i) the expression of two key determinants of net positive surface charge (mprFanddlt) is dependent on the cotranscription of bothgraRandvraG, (ii) reduced expression ofmprFanddltingraRmutants was phenotypically associated with reduced surface-positive charge, (iii) this net reduction in surface-positive charge ingraRandvraGmutants, in turn, correlated with enhanced killing by a range of CAPs of diverse structure and origin, including those from mammalian platelets (tPMPs) and neutrophils (hNP-1) and from bacteria (polymyxin B), and (iv) the synthesis and translocation of membrane lysyl-phosphatidylglycerol (anmprF-dependent function) was substantially lower ingraRandvraGmutants than in parental strains. Importantly, the inducibility ofmprFanddlttranscription via thegraRS-vraFGpathway was selective, with induction by sublethal exposure to the CAPs, RP-1 (platelets), and polymyxin B, but not by other cationic molecules (hNP-1, vancomycin, gentamicin, or calcium-daptomycin). AlthoughgraRregulates expression ofvraG, the expression ofgraRwas codependent on an intact downstreamvraGlocus. Collectively, these data support an important role of thegraRSandvraFGloci in the sensing of and response to specific CAPs involved in innate host defenses.

Cationic Antimicrobial Peptides for Tuberculosis: A Mini-Review

2019 ◽  
Vol 20 (9) ◽  
pp. 885-892
Author(s):  
Sara Silva ◽  
Nuno Vale
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Resistance Mechanisms ◽  
Therapeutic Agents ◽  
Pharmacological Properties ◽  
Therapeutic Activity ◽  
Alternative Strategies ◽  
Cationic Antimicrobial Peptides ◽  
Specific Amino Acid

Cationic antimicrobial peptides (CAMPs) can be considered as new potential therapeutic agents for Tuberculosis treatment with a specific amino acid sequence. New studies can be developed in the future to improve the pharmacological properties of CAMPs and also understand possible resistance mechanisms. This review discusses the principal properties of natural and/or synthetic CAMPs, and how these new peptides have a significant specificity for Mycobacterium tuberculosis. Also, we propose some alternative strategies to enhance the therapeutic activity of these CAMPs that include coadministration with nanoparticles and/or classic drugs.

Membrane targeting cationic antimicrobial peptides

2019 ◽  
Vol 537 ◽  
pp. 163-185 ◽  
Author(s):  
Daniela Ciumac ◽  
Haoning Gong ◽  
Xuzhi Hu ◽  
Jian Ren Lu
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Targeting ◽  
Cationic Antimicrobial Peptides
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