Characterization of an abaecin-like antimicrobial peptide identified from a Pteromalus puparum cDNA clone

Shen, Xiaojing; Yè, Gōngyín; Cheng, Xiongying; Yu, Chunyan; Altosaar, Illimar; Hu, Cui

doi:10.1016/j.jip.2010.05.006

Cited by 15 publications

(13 citation statements)

References 38 publications

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“…While the non-lytic mechanism of PrAMPs had been investigated extensively (Gennaro et al 2002;Otvos 2002;Scocchi et al 2011), additional PrAMPs possessing different actions have been both isolated and chemically synthesized. PP30, isolated from Apocrita and similar to abaecin, acts against microbes causing morphological changes and membrane damage (Shen et al 2010). The designed PrAMP, A3-APO and arasin 1, exhibit a dual mode of action with both membrane disruption and probable intracellular target inhibition (Paulsen et al 2013;Rozgonyi et al 2009).…”

Section: Mechanism Of Actionmentioning

confidence: 99%

Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria

et al. 2014

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The increasing resistance of pathogens to antibiotics causes a huge clinical burden that places great demands on academic researchers and the pharmaceutical industry for resolution. Antimicrobial peptides, part of native host defense, have emerged as novel potential antibiotic alternatives. Among the different classes of antimicrobial peptides, proline-rich antimicrobial peptides, predominantly sourced from insects, have been extensively investigated to study their specific modes of action. In this review, we focus on recent developments in these peptides. They show a variety of modes of actions, including mechanism shift at high concentration, non-lytic mechanisms, as well as possessing different intracellular targets and lipopolysaccharide binding activity. Furthermore, proline-rich antimicrobial peptides display the ability to not only modulate the immune system via cytokine activity or angiogenesis but also possess properties of penetrating cell membranes and crossing the blood brain barrier suggesting a role as potential novel carriers. Ongoing studies of these peptides will likely lead to the development of more potent antimicrobial peptides that may serve as important additions to the armoury of agents against bacterial infection and drug delivery.

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Section: Mechanism Of Actionmentioning

confidence: 99%

Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria

et al. 2014

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“…Ovine bactenecin OaBac6 was discovered in 2005 (Huttner et al, 1998 ). Arasin was discovered in crabs in 2008 (Stensvag et al, 2008 ) and the abaecin-like peptide PP30 was identified in wasps in 2010 (Shen et al, 2010 ). From the bean bug ( Riptortus pedestris ), riptocin was discovered in 2015 (Kim et al, 2015 ) as was BnPRP1 (Cao et al, 2015 ), the first proline-rich peptide discovered in plants ( Brassica napus ).…”

Section: Introductionmentioning

confidence: 99%

(Re)Defining the Proline-Rich Antimicrobial Peptide Family and the Identification of Putative New Members

Welch

Hossain

et al. 2020

Front. Chem.

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As we rapidly approach a post-antibiotic era in which multi-drug resistant bacteria are ever-pervasive, antimicrobial peptides (AMPs) represent a promising class of compounds to help address this global issue. AMPs are best-known for their membrane-disruptive mode of action leading to bacteria cell lysis and death. However, many AMPs are also known to be non-lytic and have intracellular modes of action. Proline-rich AMPs (PrAMPs) are one such class, that are generally membrane permeable and inhibit protein synthesis leading to a bactericidal outcome. PrAMPs are highly effective against Gram-negative bacteria and yet show very low toxicity against eukaryotic cells. Here, we review both the PrAMP family and the past and current definitions for this class of peptides. Computational analysis of known AMPs within the DRAMP database (http://dramp.cpu-bioinfor.org/) and assessment of their PrAMP-like properties have led us to develop a revised definition of the PrAMP class. As a result, we subsequently identified a number of unknown and unclassified peptides containing motifs of striking similarity to known PrAMP-based DnaK inhibitors and propose a series of new sequences for experimental evaluation and subsequent addition to the PrAMP family.

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“…Further studies on artificial proline-rich peptides has verified that a number of proline sequences can travers bacterial membranes, e.g., poly-proline (P 14 ) peptide [ 203 ] as well as a polyprolines family of peptides (VXLPPP) n ( n = 1, 2, and 3; X correspond to histidine, arginine or lysine) [ 198 ]. Contrary to these findings there are also reports of proline-rich peptides and their ability to damage cell membranes, however these effects are highly concentration dependent [ 201 , 204 , 205 ].…”

Section: Structural Properties Of Specific Amino Acid Residues In mentioning

confidence: 89%

Peptides and Peptidomimetics for Antimicrobial Drug Design

2015

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The purpose of this paper is to introduce and highlight a few classes of traditional antimicrobial peptides with a focus on structure-activity relationship studies. After first dissecting the important physiochemical properties that influence the antimicrobial and toxic properties of antimicrobial peptides, the contributions of individual amino acids with respect to the peptides antibacterial properties are presented. A brief discussion of the mechanisms of action of different antimicrobials as well as the development of bacterial resistance towards antimicrobial peptides follows. Finally, current efforts on novel design strategies and peptidomimetics are introduced to illustrate the importance of antimicrobial peptide research in the development of future antibiotics.

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Characterization of an abaecin-like antimicrobial peptide identified from a Pteromalus puparum cDNA clone

Cited by 15 publications

References 38 publications

Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria

Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria

(Re)Defining the Proline-Rich Antimicrobial Peptide Family and the Identification of Putative New Members

Peptides and Peptidomimetics for Antimicrobial Drug Design

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