Different mechanisms of insensitivity to the staphylococcin-like peptide pep 5

Sahl, Hans‐Georg; Ersfeld-Dressen, Hildegard; Bierbaum, Gabriele; Josten, Michaele; Kordel, Marianne; Reis, Michaela; Schüller, Friederike

doi:10.1016/s0176-6724(87)80002-0

Cited by 7 publications

(2 citation statements)

References 13 publications

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“…We discovered that lipoteichoic acid from S.epidermidis substantially attenuated keratinocyte response to skin injury through a TLR2-dependent inhibition of the TLR3 signaling via TNF receptor-associated factor 1 (TRAF1), thus suppressing unwanted inflammatory cytokine production [1]. Besides the regulation of inflammation in skin injury, other groups showed that S.epidermidis produced some antimicrobial molecules including Staphylococcin 1580 [2], Pep5 [3], PSMs [4] to benefit cutaneous immune defense by selectively inhibiting the survival of skin pathogens. We have also demonstrated that less than 10 kDa molecules from S.epidermidis culture media induced the production of β-defensins to enable the skin to mount an enhanced response to pathogens [5].…”

Section: Introductionmentioning

confidence: 99%

A Novel Lipopeptide from Skin Commensal Activates TLR2/CD36-p38 MAPK Signaling to Increase Antibacterial Defense against Bacterial Infection

et al. 2013

PLoS ONE

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Staphylococcus epidermidis (S.epidermidis) plays important protective roles by directly producing or by stimulating hosts to produce antimicrobial peptides (AMPs) against pathogenic infections. Although several AMPs from S.epidermidis have been identified, molecules that stimulate hosts to produce AMPs remain largly unknown. Here we demonstrate that a new lipopeptide (named LP01) purified from S.epidermidis culture media has a unique structure with heneicosanoic acid (21 carbons) binding to lysine11 of a peptide chain. In vitro LP01 increased the expression of β-defensin 2(hBD2) and hBD3 in neonatal human epidermal keratinocytes(NHEK), leading to increased capacity of cell lysates to inhibit the growth of S.aureus. In vivo LP01 induced the expression of mouse β-defensin 4(mBD4) to decrease the survival of local S.aureus in skin and systemic S.aureus survival in liver. The induction of beta-defensins by LP01 was dependent on TLR2 as Tlr2-deficient mice had decreased mBD4. Furthermore, knockdown of CD36 decreased the expression of hBD2 and hBD3, and p38 MAPK inhibitor significantly inhibited the expression of hBDs induced by LP01.Taken together, these findings demonstrate that lipopeptide LP01 from normal commensal S.epidermidis increases antimicrobial peptide hBD2 and hBD3 expression via the activation of TLR2/CD36-p38 MAPK, thus enhancing antimicrobial defense against pathogenic infections.

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Section: Introductionmentioning

confidence: 99%

A Novel Lipopeptide from Skin Commensal Activates TLR2/CD36-p38 MAPK Signaling to Increase Antibacterial Defense against Bacterial Infection

et al. 2013

PLoS ONE

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“…Its affinity for lipid membranes is sensitive to the lipid composition and increases for negatively charged lipids ( − ). The presence of a transmembrane potential of sufficient height (inside negative) increases the level of perturbation of the membrane permeability induced by nisin ( , ). At sufficiently high concentrations, nisin affects the overall organization of lipid bilayers by promoting the inverse hexagonal phase (H II ) structure ().…”

mentioning

confidence: 99%

Binding of Nisin Z to Bilayer Vesicles As Determined with Isothermal Titration Calorimetry

et al. 2000

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Nisin Z, a 34-residue lantibiotic, is secreted by some lactic acid bacteria and exerts its antibacterial activity against various Gram-positive bacteria by permeabilizing the cell membrane. It is a cationic amphiphilic peptide with several unusual dehydro residues and thioether-bridged lanthionines. Isothermal titration calorimetry was used to provide a quantitative thermodynamic description for nisin Z adsorption to and penetration into negatively charged and neutral lipid bilayers. The binding of the cationic peptide (electric charge z approximately 3.8) to anionic membranes was found to be dominated by electrostatic forces which could be described with the Gouy-Chapman theory. For biologically relevant conditions with a membrane surface potential of -40 mV, the peptide concentration near the membrane surface increases by about 2-3 orders of magnitude compared to the bulk concentration. The binding step proper, i.e., the transition from the lipid-water interface into the membrane, is almost exclusively driven by the high surface concentration. Binding can be described by a partition equilibrium of the form X(b) = KC(M) = KC(p,f) exp(-z(p)psi(0)F(0)/RT), where C(M) is the peptide surface concentration, C(p,f) the bulk concentration, and psi(0) the membrane surface potential. The intrinsic partition coefficient (K = 1.8 M(-)(1)) is remarkably small, indicating a correspondingly small hydrophobic energy contribution to the binding process. The electrostatic model was confirmed with nisin Z mutants in which valine-32 was replaced with either lysine (V32K) or glutamate (V32E), increasing or decreasing the electric charge by 1 unit. The extent of peptide binding increased for V32K and decreased for V32E as predicted by the electrostatic theory. In contrast, electrostatic effects were almost negligible for the binding of nisin Z to neutral membranes. However, the binding isotherms were characterized by a distinctly larger intrinsic binding constant K(0) of approximately 540 M(-)(1) and an enhanced hydrophobic free energy of binding. The binding of nisin Z to sonicated lipid vesicles is exothermic with a DeltaH degrees of ca. -9 and -3.4 kcal/mol for charged and neutral membranes, respectively.

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Potential Therapeutic Applications of Magainins and other Antimicrobial Agents of Animal Origin

Jacob¹,

Zasloff²

2007

Novartis Foundation Symposia

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Different mechanisms of insensitivity to the staphylococcin-like peptide pep 5

Cited by 7 publications

References 13 publications

A Novel Lipopeptide from Skin Commensal Activates TLR2/CD36-p38 MAPK Signaling to Increase Antibacterial Defense against Bacterial Infection

A Novel Lipopeptide from Skin Commensal Activates TLR2/CD36-p38 MAPK Signaling to Increase Antibacterial Defense against Bacterial Infection

Binding of Nisin Z to Bilayer Vesicles As Determined with Isothermal Titration Calorimetry

Potential Therapeutic Applications of Magainins and other Antimicrobial Agents of Animal Origin

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