Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine

Boman, Hans G.; Agerberth, Birgitta; Boman, Anita

doi:10.1128/iai.61.7.2978-2984.1993

Cited by 478 publications

(228 citation statements)

References 32 publications

(25 reference statements)

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“…4), nevertheless, this peptide is highly active against E. coli and some other Gram-negative bacteria (Agerberth et al, 1991, and Table 1). This is in agreement with the fact that PR-39 does not lyse susceptible bacteria, it being more likely that it affects chromosome replication (Boman et al, 1993). For peptides which rapidly lyse bacteria, like the cecropins, it is impossible by experiment to demonstrate any (Boman et al, 1989), those for PR-39 are from (Agerberth et al, 1991).…”

Section: Discussionsupporting

confidence: 79%

Antibacterial peptides and mitochonrial presequences affect mitochonrial coupling, respiration and protein import

Hugosson

Andreu

Boman

et al. 1994

European Journal of Biochemistry

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Cecropins A and P1, antibacterial peptides from insects and from pig and some related peptides released respiratory control, inhibited protein import and at higher concentrations also inhibited respiration. However, PR-39, an antibacterial peptide from pig intestine, was found to be almost inert towards mitochondria. The concentrations at which the three mitochondrial functions were effected varied for different peptides. Melittin, magainin and Cecropin-A-(1,13) -Melittin(l,l3)-NH2, a hybrid between cecropin A and melittin, were most potent, while the two cecropins acted at higher concentrations. The biosynthesis of cecropin A is known and the intermediates are synthesized. We have used four peptides from this pathway to investigate their effects on coupling, respiration and protein import into mitochondria. Mature cecropin A followed by the preproprotein were most aggressive whereas the intermediates were less active or inert. The efficiency of different derivatives of cecropin A as uncouplers correlates well with their capacity to release membrane potential measured as fluorescence quenching of Rhodamine 123. Inhibition of respiration was found to be dependent on membrane potential and was most pronounced with mature cecropin A, less so with its three precursors. We also found that three peptides derived from mitochondrial presequences showed antibacterial activity. It is concluded that, there are similarities in the functions of antibacterial peptides and mitochondrial presequences, uncoupling activity in mitochondria cannot be correlated with the antibacterial activity (contrary to a previous suggestion), the processing of preprocecropin A may have evolved in such a way that there is a minimum of membrane damage from the intermediates in the pathway, and peptides produced for delivery outside of an animal have evolved to be more aggressive against mitochondria than peptides for delivery inside of the animal.During the last 13 years several classes of broadspectrum antibacterial peptides have been discovered in the animal kingdom, among them cecropins, defensins and magainins (reviewed by Boman, 1991 ;Zasloff, 1992). These three groups of peptides are well characterized, they have been cloned, their three-dimensional structures are known and for cecropins and defensins the gene structures have been determined. All three groups of peptides also form channels in artificial membranes but it is not yet known if channel formation is responsible for the lethal activity on bacteria. There are clear structural similarities between certain antiCorrespondence to E. Glaser,

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Section: Discussionsupporting

confidence: 79%

Antibacterial peptides and mitochonrial presequences affect mitochonrial coupling, respiration and protein import

Hugosson

Andreu

Boman

et al. 1994

European Journal of Biochemistry

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“…Although we do not yet know whether internalization of tenecin 3 over the threshold is required for its fungicidal action, it is evident that the fungicidal action requires some intracellular processes after internalization because the internalization was not a direct cause of the loss of cell viability. The nonlytic internalization and nucleic acid binding properties have been reported for some antimicrobial peptides, such as buforin II isolated from Bufo bufo garagriozans [50], PR-39 from pig intestine [51], and tachyplesin I from Tachypleus tridentatus [52]. Their antimicrobial mechanisms are thought to be related to the inhibition of macromolecular synthesis within the cells.…”

Section: Discussionmentioning

confidence: 99%

Internalization of tenecin 3 by a fungal cellular process is essential for its fungicidal effect onCandida albicans

Kim¹,

Lee²,

Kim³

et al. 2001

European Journal of Biochemistry

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Tenecin 3 is a glycine-rich, antifungal protein of 78 residues isolated from the insect Tenebrio molitor larva. As an initial step towards understanding the antifungal mechanism of tenecin 3, we examined how this protein interacts with the pathogenic fungus Candida albicans to exert its antifungal action. Tenecin 3 did not induce the release of a fluorescent dye trapped in the artificial membrane vesicles and it did not perturb the membrane potential of C. albicans by the initial interaction. Fluorescence confocal microscopy and flow cytometric analysis revealed that tenecin 3 is rapidly internalized into the cytoplasmic space in energy-dependent and temperature-dependent manners. This internalization is also dependent on the ionic environment and cellular metabolic states. These results suggest that the internalization of tenecin 3 into the cytoplasm of C. albicans is mediated by a fungal cellular process. The internalized tenecin 3 is dispersed in the cytoplasm, and the loss of cell viability occurs after this internalization. [14]. These studies have shown that the formation of transmembrane pores or ion channels on the cellular membranes cause the leakage of essential metabolites. The disruption of the microbial cell structure is the major killing mechanism for these cationic, antimicrobial proteins. This mechanism is also generally applicable to the antifungal action mechanism of these proteins, and even to the antiviral mechanism [15]. Other well known antifungal mechanisms of plant antifungal proteins, such as chitinases [16] [19], include the disruption of the cell wall structure and interference in cell wall synthesis. However, some antimicrobial proteins, including the cysteine-rich plant defensin Rs-AFP 2 [20], the insect antifungal protein drosomycin [5], and the glycine-rich insect antifungal protein AFP [21], show no growth inhibition for Gram negative and Gram positive bacteria. It has been proposed that the channel formation through direct protein-lipid interaction is not a probable antifungal mechanism for these proteins although their action mechanisms have not yet been fully elucidated [22]. There is a high sequence homology between Rs-AFP 2 and drosomycin, while AFP has no significant homology with these proteins [21]. We previously isolated tenecin 3 as an antifungal protein from the insect Tenebrio molitor and found that it had no antibacterial activity [23]. As tenecin 3 shares 37.3% identity with AFP from Sarcophaga peregrina, it can be categorized into an antifungal protein group with AFP and another insect antifungal protein, holotricin 3, from Holotricia diomphalia [24]. Tenecin 3 is also a glycine-rich protein, as are AFP and holotricin 3. However, little is known about the action mechanism of AFP and its homologs. The binding of AFP to Candia albicans was thought to be the cause of some damage to the cells even though this binding is weak and dependent on ionic environments [21]. Tenecin 3 consists of 78 amino acids and has distinctive features in its primary Abbreviations: AFP, ant...

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“…While majority of agents that perturb the outer membrane of Gram-negative bacteria makes them susceptible to lysis by lysozyme, treatment of E. coli with indolicidin does not make it susceptible to lysis by lysozyme [7]. Thus, it is conceivable that indolicidin uses its membrane a¤nity property for entering the cytoplasm and exerts its antibacterial activity by attacking other targets, like PR-rich peptides PR-39, bac-5 and bac-7 [10,11]. All these peptides are known to inhibit macromolecular synthesis in bacteria.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of antimicrobial action of indolicidin

Subbalakshmi¹

1998

FEMS Microbiology Letters

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Indolicidin, a 13-residue antimicrobial peptide isolated from cytoplasmic granules of bovine neutrophils, exhibits activity against Gram-positive and Gram-negative bacteria as well as fungi. Although indolicidin is bactericidal and permeabilizes the bacterial membranes, it does not lyse the bacterial cells. We examined the effect of bactericidal concentrations of indolicidin on the morphology of Escherichia coli cells and found that it induces filamentation. Further investigations showed that indolicidin inhibits DNA synthesis in E. coli cells at concentrations at which RNA and protein synthesis are either partially affected or not affected at all. Since inhibition of DNA synthesis is also known to induce filamentation in E. coli, it appears to contribute to the antimicrobial activity of indolicidin. z 1998 Published by Elsevier Science B.V.

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Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine

Abstract: Cecropin P1 and PR-39 are two antibacterial peptides isolated from the upper part of the small intestine of the pig. They have been sequenced, and their antibacterial spectra have been investigated (J.-Y. Lee, A.

Cited by 478 publications

References 32 publications

Antibacterial peptides and mitochonrial presequences affect mitochonrial coupling, respiration and protein import

Antibacterial peptides and mitochonrial presequences affect mitochonrial coupling, respiration and protein import

Internalization of tenecin 3 by a fungal cellular process is essential for its fungicidal effect onCandida albicans

Mechanism of antimicrobial action of indolicidin

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