Antimicrobial peptides fromMirabilis jalapa andAmaranthus caudatus: expression, processing, localization and biological activity in transgenic tobacco

Bolle, Miguel F.C. De; Osborn, Rupert W.; Goderis, Inge J.W.M.; Noé, Lydie; Acland, David P.; Hart, Cliff A.; Torrekens, Sophie; Leuven, Fred Van; Broekaert, Willem F.

doi:10.1007/bf00040718

Cited by 116 publications

(61 citation statements)

References 60 publications

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“…Ac-AMP2, a 30-residue peptide found in Amaranthus caudatus seeds (79,80), has potent antifungal activity and binds specifically to chitin, a polymer of ␤-1,4-Nacetyl-D-glucosamine (81). Mj-AMP2 (82) is a 36-residue, cationic peptide from the seeds of Mirabilis jalapa and hevein is a 43-residue, multivalent, chitin-binding antifungal peptide found in the rubber tree (Hevea brasiliensis) (83)(84)(85).…”

Section: Discussionmentioning

confidence: 99%

Multivalent Binding of Carbohydrates by the Human α-Defensin, HD5

Lehrer

Jung

Ruchala

et al. 2009

The Journal of Immunology

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Four of the six human α-defensins (human neutrophil peptides 1–3 and human α-defensin 5; HD5) have a lectin-like ability to bind glycosylated proteins. Using HD5 as a model, we applied surface plasmon resonance techniques to gain insights into this property. HD5 bound natural glycoproteins > neoglycoproteins based on BSA > nonglycosylated BSA ≫ free sugars. The affinity of HD5 for simple sugars covalently bound to BSA was orders of magnitude greater than its affinity for the same sugars in solution. The affinity of HD5 for protein-bound carbohydrates resulted from multivalent interactions which may also involve noncarbohydrate residues of the proteins. HD5 showed concentration-dependent self-association that began at submicromolar concentrations and proceeded to dimer and tetramer formation at concentrations below 5 μM. The (R9A, R28A) and (R13A, R32A) analogs of HD5 showed greatly reduced self-association as well as minimal binding to BSA and to BSA-affixed sugars. From this and other evidence, we conclude that the extensive binding of HD5 to (neo)glycoproteins results from multivalent nonspecific interactions of individual HD5 molecules with carbohydrate and noncarbohydrate moieties of the target molecule and that the primary binding events are magnified and enhanced by subsequent in situ assembly and oligomerization of HD5. Self-association and multivalent binding may play integral roles in the ability of HD5 to protect against infections caused by viruses and other infectious agents.

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Section: Discussionmentioning

confidence: 99%

Multivalent Binding of Carbohydrates by the Human α-Defensin, HD5

Lehrer

Jung

Ruchala

et al. 2009

The Journal of Immunology

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“…Automated chemical synthesis to produce antimicrobial peptides remains very costly (Hancock & Lehrer, 1998;Hancock & Sahl, 2006;Marr et al, 2006), while use of transgenic organisms for the production of antimicrobial peptides, either directly (De Bolle et al, 1996;François et al, 2002;Yarus et al, 1996) or as fusion proteins (Lee et al, 2000;Li, 2011;Moon et al, 2007), is limited to ribosomally produced antimicrobial peptides. Our attention has turned to a group of nonribosomal antimicrobial peptides, the tyrocidines, which in the tyrothricin complex were the first antibiotics in clinical use (Dubos & Cattaneo, 1939;Dubos, 1939), although their use was limited to topical applications due to observed haemolytic toxicity (Rammelkamp & Weinstein, 1942;Rankin, 1944;Robinson & Molitor, 1942).…”

Section: Introductionmentioning

confidence: 99%

Manipulation of the tyrothricin production profile of Bacillus aneurinolyticus

et al. 2013

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A group of non-ribosomally produced antimicrobial peptides, the tyrocidines from the tyrothricin complex, have potential as antimicrobial agents in both medicine and industry. Previous work by our group illustrated that the more polar tyrocidines rich in Trp residues in their structure were more active toward Gram-positive bacteria, while the more non-polar tyrocidines rich in Phe residues had greater activity toward Plasmodium falciparum, one of the major causative pathogens of malaria in humans. Our group also found that the tyrocidines have pronounced antifungal activity, dictated by the primary sequence of the tyrocidine. By simply manipulating the Phe or Trp concentration in the culture medium of the tyrothricin producer, Bacillus aneurinolyticus ATCC 10068, we were able to modulate the production of subsets of tyrocidines, thereby tailoring the tyrothricin complex to target specific pathogens. We optimized the tailored tyrothricin production using a novel, small-scale, high-throughput deep 96-well plate culturing method followed by analyses of the peptide mixtures using ultra-performance liquid chromatography linked to mass spectrometry. We were able to gradually shift the production profile of the tyrocidines and analogues, as well as the gramicidins between two extremes in terms of peptide subsets and peptide hydrophobicity. This study demonstrated that tyrothricin peptide subsets with targeted activity can be efficiently produced by simple manipulation of the aromatic amino acid profile of the culture medium. INTRODUCTIONSince the advent of antimicrobial use, there has been a progressive increase in drug resistance toward conventional antibiotics. This has instigated the search for an alternative class of antimicrobial agents with novel mechanisms of action and rare resistance (Brown & Wright, 2005). Antimicrobial peptides are potential candidates with membrane-linked mechanisms of action as well as possible cellular targets (Brown & Wright, 2005). Their rapid membranolytic activity reduces the likelihood of resistant mutants developing. Furthermore, reduced toxicities of the antimicrobial peptides through greater selectivity toward the more negatively charged bacterial cell membrane allow them to discriminate between pathogen targets and the neutral membranes of plants and animals (Javadpour et al., 1996;Matsuzaki et al., 1991Matsuzaki et al., , 1995Qin et al., 2003). Consequently, antimicrobial peptides show potential in the development of therapeutic agents to treat resistant strains of pathogenic microorganisms or to serve as bio-pesticides and preservatives (Brul & Coote, 1999;Cleveland et al., 2001;Keymanesh et al., 2009).A major limitation to the large-scale use of antimicrobial peptides has been the cost and efficiency of their production (Bradshaw, 2003;Gordon et al., 2005;Marr et al., 2006;Yeaman & Yount, 2003). Automated chemical synthesis to produce antimicrobial peptides remains very costly (Hancock & Lehrer, 1998;Hancock & Sahl, 2006;Marr et al., 2006), while use of transgenic organisms fo...

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“…Erzler in 1986 reported that lectins in higher plants defend against pathogenic bacteria and fungi by recognizing and immobilizing the infecting microorganisms via binding, thereby preventing their subsequent growth and multiplication. The role of lectins as those of the herbaceous Amaranthus in inhibiting bacteria and fungi has long been known (Bolle et al, 1996). Microbes have lectins that help in recognition and the blocking of these can prevent the infection has been established in mouse models.…”

Section: Introductionmentioning

confidence: 99%