Antibacterial peptides: basic facts and emerging concepts

Boman, Hans G.

doi:10.1046/j.1365-2796.2003.01228.x

Cited by 1,004 publications

(850 citation statements)

References 129 publications

(155 reference statements)

Supporting

Mentioning

822

Contrasting

Unclassified

Order By: Relevance

“…Invertebrate animals, living without adaptive immunity in a microbe laden environment, produce AMPs as important evolutionary conserved component of their innate immune system, which play a key role in the host defense against bacterial, fungal, and viral invasion. 1,2 In marine invertebrates, a battery of AMPs were found in Spongia, Cnidaria, Annelida, Mollusca, Chelicerata, Crustacea, and Tunicata, for example, aurelin from jellyfish, 3 myticin from mussels, 4 tachyplesins and polyphemusins from horseshoe crabs, 5,6 penaeidins from shrimp, 7 clavanins and styelins from ascidians. [8][9][10] Earlier we discovered two novel 21-residue AMPs, termed arenicins, from coelomocytes of marine polychaeta lugworm Arenicola marina.…”

Section: Introductionmentioning

confidence: 99%

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

et al. 2007

View full text Add to dashboard Cite

Arenicins are 21‐residue cationic antimicrobial peptides isolated from marine polychaeta Arenicola marina. The peptides exhibit potent broad‐spectrum antimicrobial activity. In water solution arenicin‐2 adopts a β‐hairpin conformation, stabilized by one disulfide and nine hydrogen bonds. To determine the propensity for the peptide oligomerization in membrane mimetic systems, the recombinant arenicin‐2 was overexpressed as a fused form in Escherichia coli. The arenicin‐2 oligomerization and intermolecular packing in membrane mimicking environment were investigated using high‐resolution NMR spectroscopy. The present studies show that arenicin‐2 preserves a β‐hairpin structure and forms asymmetric dimers upon incorporation into the dodecylphosphocholine micelle. Two monomers of arenicin‐2 are aligned parallel to each other by the N‐terminal strands of the β‐hairpin (CN↑↑NC type of association). Polyacrylamide gel electrophoresis analysis indicated that in environment of anionic SDS micelles the arenicin‐2 might undergo further oligomerization and form tetramers. Our results afford further molecular insight into possible mechanism of antimicrobial action of arenicins. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 455–464, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

show abstract

Section: Introductionmentioning

confidence: 99%

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

et al. 2007

View full text Add to dashboard Cite

show abstract

“…Antimicrobial peptides (AMP) are an important component of the innate immune system present in all phyla of the living kingdom and provide immunity against infection caused by pathogens [1,2]. AMPs have been identified and characterized in many vertebrates [3], invertebrates [1] and plants [4].…”

Section: Introductionmentioning

confidence: 99%

Adaptive evolution after duplication of penaeidin antimicrobial peptides

Padhi

Verghese

Otta

et al. 2007

Fish & Shellfish Immunology

View full text Add to dashboard Cite

Penaeidin antimicrobial peptides in penaeid shrimps are an important component of their innate immune system that provides immunity against infection caused by several gram-positive bacteria and filamentous fungal species. Despite the knowledge on the identification and characterization of these peptides in penaeid shrimps, little is known about the evolutionary pattern of these peptides and the underlying genetic mechanisms that maintain high sequence diversities in the penaeidin gene family. Based on the phylogenetic analyses and maximum likelihood-based codon substitution analyses, here we present the convincing evidence that multiple copies of penaeidins have evolved by gene duplication, and positive Darwinian selection (adaptive evolution) is the likely cause of accelerated rate of amino acid substitutions among these duplicated genes.While the average ratio of non-synonymous to synonymous substitutions (u) for the entire coding region of both active domains is 0.9805, few codon sites showed significantly higher u (3.73). The likelihood ratio tests that compare models incorporating positive selection (u > 1) at certain codon sites with models not incorporating positive selection (u < 1), failed to reject (p ¼ 0) the evidence of positive Darwinian selection. The rapid adaptive evolution of this gene family might be directed by the pathogens and the faster rate of amino acid substitutions in the N-terminal proline-rich and C-terminal cysteine-rich domains could be due to their direct involvement in the protection against pathogens. When the host expose to different habitats/environment an accelerated rate of amino acid substitutions in both the active domains may also be expected.

show abstract

“…5 Cecropin A (CA) and melittin (M) provided the first examples of EAP sequence hybridization. [6][7][8] CA(1-8)M (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18), one of the most successful examples of the hybridization concept, showed improved antimicrobial activity relative to parent cecropin A and greatly reduced the hemolytic properties of melittin. Taking CA(1-8)M(1-18) as lead, a subsequent approach was to further reduce the size of the hybrid CA-M peptides while retaining antimicrobial activity.…”

Section: Introductionmentioning

confidence: 99%

Interaction and Lipid-Induced Conformation of Two Cecropin−Melittin Hybrid Peptides Depend on Peptide and Membrane Composition

et al. 2005

View full text Add to dashboard Cite

The interaction of two hybrid peptides of cecropin A and melittin [CA(1-8)M(1-18) and CA(1-7)M(2-9)] with liposomes was studied by differential scanning calorimetry (DSC), circular dichroism (CD), and quasi-elastic light scattering (QELS). The study was carried out with large unilamellar vesicles (LUVs) of three different lipid compositions: 1,2-dimyristoil-sn-glycero-3-phosphocholine (DMPC), 1,2-dimyristoylsn-glycero-3-phospho-rac-(1-glycerol) (DMPG) and a binary mixture of DMPC/DMPG, in a wide range of peptide-to-lipid (P:L) molar ratios (0 to 1:7). DSC results indicate that, for both peptides, the interaction depends on membrane composition, with very different behavior for zwitterionic and anionic membranes. CD data show that, although the two peptides have different secondary structures in buffer (random coil for CA(1-7)M(2-9) and predominantly -sheet for CA(1-8)M(1-18)), they both adopt an R-helical structure in the presence of the membranes. Overall, results are compatible with a model involving a strong electrostatic surface interaction between the peptides and the negatively charged liposomes, which gives place to aggregation in the gel phase and precipitation after a threshold peptide concentration. In the case of zwitterionic membranes, a progressive surface coverage with peptide molecules destabilizes the membrane, eventually leading to membrane disruption. Moreover, delicate modulations in behavior were observed depending on the peptide.

show abstract

Antibacterial peptides: basic facts and emerging concepts

Cited by 1,004 publications

References 129 publications

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

Adaptive evolution after duplication of penaeidin antimicrobial peptides

Interaction and Lipid-Induced Conformation of Two Cecropin−Melittin Hybrid Peptides Depend on Peptide and Membrane Composition

Contact Info

Product

Resources

About