Use of the Cell Wall Precursor Lipid II by a Pore-Forming Peptide Antibiotic

Breukink, Eefjan; Wiedemann, Imke; Kraaij, Cindy van; Kuipers, Oscar P.; Sahl, Hans‐Georg; Kruijff, Ben de

doi:10.1126/science.286.5448.2361

Cited by 702 publications

(619 citation statements)

References 16 publications

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“…Their data support a model in which membrane patches containing sphingolipids act as specific binding sites for defensins or, alternatively, are required to anchor membrane-or cell wall-associated proteins, which themselves interact with defensins (Thevissen et al, 2000a). Similarly, the protein antibiotic nisin Z from Lactococcus lactis binds with high affinity to the membrane-anchored cell wall precursor lipid II of Gram-positive bacteria (Breukink et al, 1999). Like harpin Psph (Lee et al, 2001), nisin Z is an amphipathic, highly charged protein.…”

Section: A Harpin Binding Site Involved In Pr Gene Expression In Tobaccomentioning

confidence: 63%

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A Harpin Binding Site in Tobacco Plasma Membranes Mediates Activation of the Pathogenesis-Related Gene HIN1 Independent of Extracellular Calcium but Dependent on Mitogen-Activated Protein Kinase Activity

Lee¹,

Klessig²,

Nürnberger³

2001

The Plant Cell

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Harpin from the bean halo-blight pathogen Pseudomonas syringae pv phaseolicola (harpin Psph ) elicits the hypersensitive response and the accumulation of pathogenesis-related gene transcripts in the nonhost plant tobacco. Here, we report the characterization of a nonproteinaceous binding site for harpin Psph in tobacco plasma membranes, which is assumed to mediate the activation of plant defense responses in a receptor-like manner. Binding of 125 I-harpin Psph to tobacco microsomal membranes (dissociation constant ‫؍‬ 425 nM) and protoplasts (dissociation constant ‫؍‬ 380 nM) was specific, reversible, and saturable. A close correlation was found between the abilities of harpin Psph fragments to elicit the transcript accumulation of the pathogenesis-related tobacco gene HIN1 and to compete for binding of 125 Iharpin Psph to its binding site. Another elicitor of the hypersensitive response and HIN1 induction in tobacco, the Phytophthora megasperma -derived ␤ -elicitin ␤ -megaspermin, failed to bind to the putative harpin Psph receptor. In contrast to activation by ␤ -megaspermin, harpin Psph -induced activation of the 48-kD salicylic acid-responsive mitogen-activated protein kinase (MAPK) and HIN1 transcript accumulation were independent of extracellular calcium. Moreover, use of the MAPK kinase inhibitor U0126 revealed that MAPK activity was essential for pathogenesis-related gene expression in harpin Psph -treated tobacco cells. Thus, a receptor-mediated MAPK-dependent signaling pathway may mediate the activation of plant defense responses induced by harpin Psph .

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Section: A Harpin Binding Site Involved In Pr Gene Expression In Tobaccomentioning

confidence: 63%

“…Like harpin Psph (Lee et al, 2001), nisin Z is an amphipathic, highly charged protein. Remarkably, nisin Z exerted its biological function through high affinity binding to lipid II and subsequent formation of an ion-conducting pore (Breukink et al, 1999).…”

Section: A Harpin Binding Site Involved In Pr Gene Expression In Tobaccomentioning

confidence: 99%

A Harpin Binding Site in Tobacco Plasma Membranes Mediates Activation of the Pathogenesis-Related Gene HIN1 Independent of Extracellular Calcium but Dependent on Mitogen-Activated Protein Kinase Activity

Lee¹,

Klessig²,

Nürnberger³

2001

The Plant Cell

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“…Compounds 2a-d were purified using reversed-phase HPLC according to modified literature procedure 13 and characterized by high field 1 H NMR spectroscopy and mass spectrometry (MS). The attachment of the ligands to the C-terminal of Van 4 ] 10+ , the activity of the mixture of 2d and Zn-(OAc) 2 (4:1, at pH ) 7) against VRE is the same as that of 2d, suggesting that there is no multivalent Van formed by metal complexation when 2d and Zn(OAc) 2 react at the condition of the in vitro experiment. We also did not observe the formation of [Zn(2d) n ] (2n+2)+ (n ) 1-4) by ESI-MS, which is consistent with the observed activity.…”

Section: Resultsmentioning

confidence: 88%

Multivalent Antibiotics via Metal Complexes: Potent Divalent Vancomycins against Vancomycin-Resistant Enterococci

Xing

et al. 2003

J. Med. Chem.

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“…Studies have also suggested that more specific interactions within bacterial cell walls or membranes help to define antimicrobial peptide activity (38). For example, binding of the antimicrobial peptide nisin can be mediated by peptidoglycan-associated lipid II (39), and salivary histatins bind a 67-kDa surface protein of Candida albicans (40). Specific cell wall/membrane targeting may explain some of the differences in the spectrum of K6A-derived peptide activity, e.g., the 19-mer is effective against S. pyogenes but not S. aureus or E. coli, both of which are highly susceptible to the 14-mer.…”

Section: Discussionmentioning

confidence: 99%

Cytokeratins mediate epithelial innate defense through their antimicrobial properties

Tam

Mun²,

Evans³

et al. 2012

J. Clin. Invest.

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Epithelial cells express antimicrobial proteins in response to invading pathogens, although little is known regarding epithelial defense mechanisms during healthy conditions. Here we report that epithelial cytokeratins have innate defense properties because they constitutively produce cytoprotective antimicrobial peptides. Glycine-rich C-terminal fragments derived from human cytokeratin 6A were identified in bactericidal lysate fractions of human corneal epithelial cells. Structural analysis revealed that these keratin-derived antimicrobial peptides (KDAMPs) exhibited coil structures with low α-helical content. Synthetic analogs of these KDAMPS showed rapid bactericidal activity against multiple pathogens and protected epithelial cells against bacterial virulence mechanisms, while a scrambled peptide showed no bactericidal activity. However, the bactericidal activity of a specific KDAMP was somewhat reduced by glycine-alanine substitutions. KDAMP activity involved bacterial binding and permeabilization, but the activity was unaffected by peptide charge or physiological salt concentration. Knockdown of cytokeratin 6A markedly reduced the bactericidal activity of epithelial cell lysates in vitro and increased the susceptibility of murine corneas to bacterial adherence in vivo. These data suggest that epithelial cytokeratins function as endogenous antimicrobial peptides in the host defense against infection and that keratin-derived antimicrobials may serve as effective therapeutic agents.

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Use of the Cell Wall Precursor Lipid II by a Pore-Forming Peptide Antibiotic

Cited by 702 publications

References 16 publications

A Harpin Binding Site in Tobacco Plasma Membranes Mediates Activation of the Pathogenesis-Related Gene HIN1 Independent of Extracellular Calcium but Dependent on Mitogen-Activated Protein Kinase Activity

A Harpin Binding Site in Tobacco Plasma Membranes Mediates Activation of the Pathogenesis-Related Gene HIN1 Independent of Extracellular Calcium but Dependent on Mitogen-Activated Protein Kinase Activity

Multivalent Antibiotics via Metal Complexes: Potent Divalent Vancomycins against Vancomycin-Resistant Enterococci

Cytokeratins mediate epithelial innate defense through their antimicrobial properties

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