Uncoupling Amphipathicity and Hydrophobicity: Role of Charge Clustering in Membrane Interactions of Cationic Antimicrobial Peptides

Biochemistry ◽  
2021 ◽  
Author(s):  
Shelley He ◽  
Tracy A. Stone ◽  
Charles M. Deber
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Interactions ◽  
Cationic Antimicrobial Peptides

scholarly journals Roles of Hydrophobicity and Charge Distribution of Cationic Antimicrobial Peptides in Peptide-Membrane Interactions

2012 ◽  
Vol 287 (10) ◽  
pp. 7738-7745 ◽  
Author(s):  
Lois M. Yin ◽  
Michelle A. Edwards ◽  
Jessica Li ◽  
Christopher M. Yip ◽  
Charles M. Deber
Keyword(s):  
Antimicrobial Peptides ◽  
Charge Distribution ◽  
Membrane Interactions ◽  
Cationic Antimicrobial Peptides

scholarly journals Membrane interactions of designed cationic antimicrobial peptides: The two thresholds

Biopolymers ◽  
2008 ◽  
Vol 89 (5) ◽  
pp. 360-371 ◽  
Author(s):  
Evgenia Glukhov ◽  
Lori L. Burrows ◽  
Charles M. Deber
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Interactions ◽  
Cationic Antimicrobial Peptides

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.

Role of amphipathicity and hydrophobicity in the balance between hemolysis and peptide–membrane interactions of three related antimicrobial peptides

2016 ◽  
Vol 141 ◽  
pp. 528-536 ◽  
Author(s):  
Axel Hollmann ◽  
Melina Martínez ◽  
Martín E. Noguera ◽  
Marcelo T. Augusto ◽  
Anibal Disalvo ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Interactions

scholarly journals Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control

2016 ◽  
Vol 291 (25) ◽  
pp. 13301-13317 ◽  
Author(s):  
Aritreyee Datta ◽  
Dipita Bhattacharyya ◽  
Shalini Singh ◽  
Anirban Ghosh ◽  
Artur Schmidtchen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Antimicrobial Peptides ◽  
Disease Control ◽  
Plant Disease ◽  
Aromatic Amino Acids ◽  
Membrane Interactions ◽  
Plant Disease Control

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.

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