Subcellular Proteomics for Understanding Host Defense Peptides Mechanism of Action

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Carlos López-Abarrategui ◽  
Anselmo J. Otero-González

AbstractHost defense peptides occurring in plants, invertebrates and vertebrates, represent a primary and heterogeneous group of molecules against infectious agents which may act directly on microorganisms or exert a redirectional enhancement of the immune response to them. Such molecules are an alternative if not for substituting at least complementing the classical antibiotics in anti-infective therapies. Several mechanisms of actions have been described for the majority of host defense peptides mostly acting at level of plasma membrane but some of them interacting with intracellular targets. The elucidation of their mechanisms of action besides completing their functional characterization is important for the development of more efficient subsequent molecular variants. Proteomic analyses have been applied for identifying new host defense peptides but few of them have been described for explaining their mechanism of action. In this paper we would like to update the subject remaking the importance of organelle proteomics for such purpose.

2021 ◽  
Author(s):  
Lulu Wei ◽  
Ruixuan Gao ◽  
Minghui Wang ◽  
Yafeng Wang ◽  
Yan Shi ◽  
...  

We report the design and investigation of a class of short dimeric antimicrobial lipo-α/sulfono-γ-AA hybrid peptides by mimicking the mechanism of action of host-defense peptides.


2014 ◽  
Vol 4 (4) ◽  
pp. 288-297
Author(s):  
LING Guiying ◽  
LI Li ◽  
GAO Jiuxiang ◽  
YU Haining ◽  
WANG Yipeng ◽  
...  

2017 ◽  
Vol 24 (7) ◽  
pp. 654-672 ◽  
Author(s):  
Malgorzata Anna Dawgul ◽  
Katarzyna E. Greber ◽  
Wieslaw Sawicki ◽  
Wojciech Kamysz

Antibiotics ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 404
Author(s):  
Michael R. Yeaman ◽  
Liana C. Chan ◽  
Nagendra N. Mishra ◽  
Arnold S. Bayer

Streptococcus mitis-oralis (S. mitis-oralis) infections are increasingly prevalent in specific populations, including neutropenic cancer and endocarditis patients. S. mitis-oralis strains have a propensity to evolve rapid, high-level and durable resistance to daptomycin (DAP-R) in vitro and in vivo, although the mechanism(s) involved remain incompletely defined. We examined mechanisms of DAP-R versus cross-resistance to cationic host defense peptides (HDPs), using an isogenic S. mitis-oralis strain-pair: (i) DAP-susceptible (DAP-S) parental 351-WT (DAP MIC = 0.5 µg/mL), and its (ii) DAP-R variant 351-D10 (DAP MIC > 256 µg/mL). DAP binding was quantified by flow cytometry, in-parallel with temporal (1–4 h) killing by either DAP or comparative prototypic cationic HDPs (hNP-1; LL-37). Multicolor flow cytometry was used to determine kinetic cell responses associated with resistance or susceptibility to these molecules. While overall DAP binding was similar between strains, a significant subpopulation of 351-D10 cells hyper-accumulated DAP (>2–4-fold vs. 351-WT). Further, both DAP and hNP-1 induced cell membrane (CM) hyper-polarization in 351-WT, corresponding to significantly greater temporal DAP-killing (vs. 351-D10). No strain-specific differences in CM permeabilization, lipid turnover or regulated cell death were observed post-exposure to DAP, hNP-1 or LL-37. Thus, the adaptive energetics of the CM appear coupled to the outcomes of interactions of S. mitis-oralis with DAP and selected HDPs. In contrast, altered CM permeabilization, proposed as a major mechanism of action of both DAP and HDPs, did not differentiate DAP-S vs. DAP-R phenotypes in this S. mitis-oralis strain-pair.


RSC Advances ◽  
2017 ◽  
Vol 7 (31) ◽  
pp. 19081-19084
Author(s):  
Andrea Valsesia ◽  
Patrizia Iavicoli ◽  
Helen Lewis ◽  
Cloé Desmet ◽  
Dora Mehn ◽  
...  

Nanomechanical monitoring of known mechanisms of membrane poration mediated by host defense peptides is reported.


Peptides ◽  
2013 ◽  
Vol 45 ◽  
pp. 1-8 ◽  
Author(s):  
Milena Mechkarska ◽  
Manju Prajeep ◽  
Jérôme Leprince ◽  
Hubert Vaudry ◽  
Mohammed A. Meetani ◽  
...  

1996 ◽  
Vol 14 (7) ◽  
pp. 804-804
Author(s):  
Robert L. Erwin

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