Antimicrobial activity of three tick defensins and four mammalian cathelicidin-derived synthetic peptides against Lyme disease spirochetes and bacteria isolated from the midgut

Isogai, Emiko; Isogai, Hiroshi; Takahashi, Koichi; Kobayashi-Sakamoto, Michiko; Okumura, Katsuhiko

doi:10.1007/s10493-009-9251-5

Cited by 27 publications

(37 citation statements)

References 13 publications

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“…However, potential mechanisms employed by the spirochete to evade the innate host response are not well understood yet. It has been demonstrated that unlike many other bacterial pathogens, B. burgdorferi is highly resistant to cathelicidin-derived peptides (27,39), consistent with the spirochete's ability to persistently colonize the skin, where CRAMP is present. Sambri et al (39) suggest that the resistance of B. burgdorferi to antimicrobial peptides may derive from the spirochete's lack of lipopolysaccharide, a negatively charged membrane component to which cationic peptides typically bind (25,43).…”

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confidence: 93%

Borrelia burgdorferi Resistance to a Major Skin Antimicrobial Peptide Is Independent of Outer Surface Lipoprotein Content

Sarkar

Tilly

Stewart

et al. 2009

Antimicrob Agents Chemother

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We hypothesize a potential role for Borrelia burgdorferi OspC in innate immune evasion at the initial stage of mammalian infection. We demonstrate that B. burgdorferi is resistant to high levels (>200 g/ml) of cathelicidin and that this antimicrobial peptide exhibits limited binding to the spirochetal outer membrane, irrespective of OspC or other abundant surface lipoproteins. We conclude that the essential role of OspC is unrelated to resistance to this component of innate immunity.

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mentioning

confidence: 93%

Borrelia burgdorferi Resistance to a Major Skin Antimicrobial Peptide Is Independent of Outer Surface Lipoprotein Content

Sarkar

Tilly

Stewart

et al. 2009

Antimicrob Agents Chemother

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“…Their mode of action involves electrostatic interaction with the bacterial membrane, leading to permeability changes or pore formation (Sonehshine and Hynes 2008). Our previous work demonstrated that tick defensins with disulfide bridges showed strong killing activity within 1 h against S. aureus but not isolates from the midgut of I. persulcatus (Isogai et al 2009). However, we did not compare the activity between the peptide with tertiary structure and that with primary linear structure.…”

Section: Introductionmentioning

confidence: 99%

Tertiary structure-related activity of tick defensin (persulcatusin) in the taiga tick, Ixodes persulcatus

Isogai

Okumura

et al. 2010

Exp Appl Acarol

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Defensins are small cysteine-rich cationic proteins found in both vertebrates and invertebrates constituting the front line of host innate immunity. To examine the importance of the tertiary structure of tick defensin in its antimicrobial activity, we synthesized two types of the peptides with tertiary structure or primary one on basis of the information of the sequence in the defensin originated from the taiga tick, Ixodes persulcatus. Chemically synthesized peptides were used to investigate the activity spectrum against Staphylococcus aureus, Borrelia garinii and flora-associated bacteria. Both synthetic peptides showed antimicrobial activity against S. aureus in short-time killing within 1 h, but they do not show the activity against B. garinii, Stenotrophomonas maltophila and Bacillus spp., which were frequently isolated from the midgut of I. persulcatus. The teriary structure brought more potent activity to S. aureus than primary one in short-time killing. We also examined its antimicrobial activity by evaluation of growth inhibition in the presence of the synthetic peptides. Minimum inhibitory concentration (MIC) was ranged from 1.2 to 5.0 μg/ml in tertiary peptide and from 10 to 40 μg/ml in primary peptide, when 10 strains of S. aureus were used. From the curve of cumulative inhibition rates, MIC50 (MIC which half of the strains showed) to S. aureus is about 1.2 μg/ml in the peptide with tertiary structure and about 10 μg/ml in the linear one. Corynebacterium renale is 10 times or more sensitive to tertiary peptide than primary one. In conclusion, the presence of 3 disulfide bridges, which stabilize the molecule and maintain the tertiary structure, is considered to have an effect on their antimicrobial activities against Gram-positive bacteria such as S. aureus.

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“…Our results suggest that Gram-negative bacteria are more sensitive to treatment with cationic antimicrobial peptides. The antimicrobial activities of tick defensins and DefDM are generally known to function against species of Gram-positive bacteria at very low concentrations (Isogai et al 2009;Chrudimská et al 2011Chrudimská et al , 2014. It has been shown that anionic AMPs bind to the St. aureus membrane via interaction with a receptor (Steffen et al 2006) or that AMPs might proteins extracted from normal uninfected Sf9 cells.…”

Section: Discussionmentioning

confidence: 99%

Functional analysis of a novel cysteine-rich antimicrobial peptide from the salivary glands of the tick Rhipicephalus haemaphysaloides

et al. 2015

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Ticks encounter various microbes while sucking blood from an infected host and carrying these pathogens in themselves. Ticks can then transmit these pathogens to vertebrate hosts. The immune system of ticks can be stimulated to produce many bioactive molecules during feeding and pathogen invasion. Antimicrobial peptides (AMPs) are key effector molecules of a tick's immune response, as they can kill invading pathogenic microorganisms. In this study, we identified a novel cysteine-rich AMP, designated Rhamp1, in the salivary glands of unfed and fed female ticks (Rhipicephalus haemaphysaloides). Rhamp1 is encoded by a gene with an open reading frame of 333 bp, which in turn encodes a peptide of 12 kDa with a 22 amino acid residue signal peptide. The Rhamp1 protein had a pI of 8.6 and contained six conserved cysteine residues at the C-terminus. Rhamp1 shared 43% amino acid identity with a secreted cysteine-rich protein of another tick species, Ixodes scapularis. We cloned the Rhamp1 gene and attempted to express a recombinant protein using prokaryotic and eukaryotic systems, to determine its biological significance. Recombinant Rhamp1 was successfully expressed in both systems, yielding a glutathione S-transferase (GST)-tagged protein (36 kDa) from the prokaryotic system, and a polyhistidine-tagged Rhamp1 protein (14 kDa) from the eukaryotic system. Rhamp1 inhibited the activities of chymotrypsin (16%) and elastase (22%) and exerted low hemolytic activity. It also inhibited the growth of Gram-negative bacteria, including Pseudomonas aeruginosa (49%), Salmonella typhimurium (50%), and Escherichia coli (52%). Our findings suggest that Rhamp1 is a novel AMP in R. haemaphysaloides with the ability to inhibit proteinase activity.

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Antimicrobial activity of three tick defensins and four mammalian cathelicidin-derived synthetic peptides against Lyme disease spirochetes and bacteria isolated from the midgut

Cited by 27 publications

References 13 publications

Borrelia burgdorferi Resistance to a Major Skin Antimicrobial Peptide Is Independent of Outer Surface Lipoprotein Content

Borrelia burgdorferi Resistance to a Major Skin Antimicrobial Peptide Is Independent of Outer Surface Lipoprotein Content

Tertiary structure-related activity of tick defensin (persulcatusin) in the taiga tick, Ixodes persulcatus

Functional analysis of a novel cysteine-rich antimicrobial peptide from the salivary glands of the tick Rhipicephalus haemaphysaloides

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