Antimicrobial activity of a bovine myeloid antimicrobial peptide (BMAP‐28) against methicillin‐susceptible and methicillin‐resistant <i>Staphylococcus aureus</i>

Takagi, S.; Hayashi, Shunji; Takahashi, Koichi; Isogai, Hiroshi; Bai, Lanlan; Yoneyama, Hiroshi; Ando, Tasuke; Ito, Kumiko; Isogai, Emiko

doi:10.1111/j.1740-0929.2011.00979.x

Cited by 19 publications

(25 citation statements)

References 17 publications

(33 reference statements)

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“…In general, the peptides under study showed a comparable efficacy to conventional antibiotics on a molar basis and moreover proved effective against a methicillin-resistant clinical isolate of S. epidermidis (MRSE). This adds to previous reports on the efficacy of BMAPs and their derivatives, as well as of P19, on antibiotic-resistant Gram-positives, including MRSA [23,25,44,50]. Moreover, peptides prevented S. epidermidis biofilm formation at microbicidal concentrations, with an all-or-nothing effect overall, likely due to rapid killing of bacteria before their deposition/attachment to the surface of microplate wells.…”

Section: Discussionsupporting

confidence: 64%

Evaluation of free or anchored antimicrobial peptides as candidates for the prevention of orthopaedic device‐related infections

D'Este

Oro

Boix‐Lemonche

et al. 2017

Journal of Peptide Science

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The prevention of implant-associated infection, one the most feared complications in orthopaedic surgery, remains a major clinical challenge and urges development of effective methods to prevent bacterial colonization of implanted devices. Alpha-helical antimicrobial peptides (AMPs) may be promising candidates in this respect due to their potent and broad-spectrum antimicrobial activity, their low tendency to elicit resistance and possible retention of efficacy in the immobilized state. The aim of this study was to evaluate the potential of five different helical AMPs, the cathelicidins BMAP-27 and BMAP-28, their (1-18) fragments and the rationally designed, artificial P19(9/G7) peptide, for the prevention of orthopaedic implant infections. Peptides were effective at micromolar concentrations against 22 Staphylococcus and Streptococcus isolates from orthopaedic infections, while only BMAP-28 and to a lesser extent BMAP-27 were active against Enterococcus faecalis. Peptides in solution showed activities comparable to those of cefazolin and linezolid, on a molar basis, and also a variable capacity to neutralize bacterial lipopolysaccharide, while devoid of adverse effects on MG-63 osteoblast cells at concentrations corresponding to the MIC. The (1-18) BMAP fragments and P19(9/G7) were selected for further examination, based on better selectivity indices, and showed effectiveness in the presence of hyaluronic acid and in synovial fluid, while human serum affected their activity to variable extents, with BMAP-27(1-18) best retaining activity. This peptide was immobilized on streptavidin-resin beads and retained activity against reference Staphylococcus epidermidis and Staphylococcus aureus strains, with negligible toxicity towards osteoblasts, underlining its potential for the development of infection-resistant biomaterials for orthopaedic application. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

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Section: Discussionsupporting

confidence: 64%

Evaluation of free or anchored antimicrobial peptides as candidates for the prevention of orthopaedic device‐related infections

D'Este

Oro

Boix‐Lemonche

et al. 2017

Journal of Peptide Science

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“…The activity was as good or better than those of vancomycin and other published antimicrobial peptides. [14][15][16][17]19,20 Although, host cytotoxicity and instability in vivo are major limitations of antimicrobial peptides in their application as antimicrobial drugs, we have reported recently that IP lacked toxicity to mammalian and human cells such as fibroblasts, colon epithelial cells and erythrocytes, and built a stable structure unlike other antimicrobial peptides. 12 Thus, IP combines the most important three advantages for clinical setting, which are potent bactericidal activity, low toxicity and structural stability.…”

Section: Discussionmentioning

confidence: 99%

“…2,3,14 Strains were stored in Trypto Soya (TS; Nissui, Tokyo, Japan) broth with 20% glycerol at − 80°C until use and maintained on TS agar.…”

Section: Bacterial Strainsmentioning

confidence: 99%

Activity of tick antimicrobial peptide from Ixodes persulcatus (persulcatusin) against cell membranes of drug-resistant Staphylococcus aureus

et al. 2016

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Persulcatusin (IP), which is an antimicrobial peptide found in Ixodes persulcatus midgut, is active against Gram-positive bacteria such as Staphylococcus aureus. Multidrug-resistant bacteria in particular methicillin-resistant S. aureus (MRSA), vancomycinintermediate S. aureus (VISA) and vancomycin-resistant S. aureus (VRSA) are a worldwide clinical concern. In the present study, to explore the potential of IP as a new agent against multidrug-resistant S. aureus infections, we evaluated the antimicrobial activity of IP against multidrug-resistant S. aureus strains by MIC 90 , morphological observation with scanning electron microscope (SEM), and the calcein leakage assay of membrane integrity. Among the six antimicrobial peptides used in this study, IP exhibited the lowest MIC 90 values for both vancomycin-susceptible and -resistant S. aureus strains. The IP MIC 90 against a VISA strain was equivalent to vancomycin, while the MIC 90 against VRSA was relatively low. SEM observations indicated that bacterial cells exposed to IP were crumpled and showed prominent structural changes. Moreover, IP influenced the cell membranes of both MRSA and VRSA in a mere 5 min, leading to leakage of the preloaded calcein. Although a VISA strain was resistant to the action of IP on cell membrane, the MIC 90 of IP was lower than that of Nisin, suggesting that IP had another bactericidal mechanism in addition to cell membrane attack. Our results indicate that the synthetic tick antimicrobial peptide, IP exhibits strong antibacterial activity against multidrug-resistant S. aureus strains, including VRSA, via both cell membrane attack and another unknown mechanism. IP represents a promising candidate for a new anti-VRSA therapy. The appearance of antibiotic-resistant bacteria has resulted in bacterial diseases re-emerging as a threat after the many decades since the introduction of the first antibiotic penicillin. 1 The development of new antibacterial agents is urgently required, and antimicrobial peptides are viewed as ideal candidate agents. 5 Antimicrobial peptides are integral components of the innate immune system of all living organisms, including mammals, plants and insects. 6 Antimicrobial peptides result in strong natural defense in arthropod, particularly antimicrobial peptides of silk moth 7,8 and beetle, 9 which belong to the defensin family. Persulcatusin (IP), a tick antimicrobial peptide found in the midgut of Ixodes persulcatus, exhibits antimicrobial activity against Gram-positive bacteria such as S. aureus. 10-12 Furthermore, we have reported previously that S. aureus strains could not be isolated from I. persulcatus during feeding. 13 This is attributable to the antimicrobial activity of IP, which is highly expressed during blood feeding. 10,11 We hypothesized that IP could exhibit antimicrobial activity against VISA and VRSA, as well as methicillin-susceptible S. aureus and MRSA.In this study, we evaluated the antimicrobial activity of IP against multidrug-resistant S. aureus strains using MIC, scanning electron m...

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“…; Takagi et al . ). It is also known as one of the representatives of the α‐helical type of cathelicidins (Zanetti ).…”

Section: Introductionmentioning

confidence: 97%

Susceptibility difference between methicillin‐susceptible and methicillin‐resistant Staphylococcus aureus to a bovine myeloid antimicrobial peptide (BMAP‐28)

Takagi

Nishimura

Bai

et al. 2013

Animal Science Journal

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A bovine myeloid antimicrobial peptide antimicrobial peptide (BMAP-28) is a member of the cathelicidin family and acts as a component of innate immunity. There are few reports of susceptibility difference of methicillin-resistant Staphylococcus aureus (MRSA) and susceptible strains (MSSA) against BMAP-28. This study aims to clarify how a few amino acid substitutions of BMAP-28 are related to its antimicrobial activity using four analog peptides of BMAP-28. We also compared cellular fatty acid components of MSSA and MRSA using gas chromatography. We found that a few amino acid substitutions of BMAP-28 do not change antimicrobial activity. It was also revealed that the percentage of cis-11-eicosenoic acid in total detected fatty acids of MRSA was significantly higher than that of MSSA. In addition, the percentage of palmitic acid in total detected fatty acids of MRSA tended to be lower than that of MSSA. Our results will provide new information to deal with the question of differences in bacterial susceptibility against BMAP-28.

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Antimicrobial activity of a bovine myeloid antimicrobial peptide (BMAP‐28) against methicillin‐susceptible and methicillin‐resistant Staphylococcus aureus

Cited by 19 publications

References 17 publications

Evaluation of free or anchored antimicrobial peptides as candidates for the prevention of orthopaedic device‐related infections

Evaluation of free or anchored antimicrobial peptides as candidates for the prevention of orthopaedic device‐related infections

Activity of tick antimicrobial peptide from Ixodes persulcatus (persulcatusin) against cell membranes of drug-resistant Staphylococcus aureus

Susceptibility difference between methicillin‐susceptible and methicillin‐resistant Staphylococcus aureus to a bovine myeloid antimicrobial peptide (BMAP‐28)

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