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Animal Antimicrobial Peptides: an Overview

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Animal Antimicrobial Peptides: an Overview David Andreu1 Luis Rivas2 1 Universitat de Barcelona, Animal Antimicrobial Barcelona, Spain Peptides: An Overview 2 Centro de Investigaciones Biolo´ gicas (CSIC), Madrid, Spain Abstract: Antibiotic peptides are a key component of the innate immune systems of most multi- cellular organisms. Despite broad divergences in sequence and taxonomy, most antibiotic peptides share a common mechanism of action, i.e., membrane permeabilization of the pathogen. This review provides a general introduction to the subject, with emphasis on aspects such as structural types, post-translational modifications, mode of action or mechanisms of resistance. Some of these questions are treated in depth in other reviews in this issue. The review also discusses the role of antimicrobial peptides in nature, including several pathological conditions, as well as recent accounts of their application at the preclinical level. © 1999 John Wiley & Sons, Inc. Biopoly 47: 415–433, 1998 Keywords: peptide antibiotics; structures; mode of action; biological roles INTRODUCTION ber of peptides, either inducible or constitutive, and with activity against different types of microorgan- Despite their structural and functional diversity, mul- isms, have been found in almost all groups of animals. ticellular organisms have certain common features in These discoveries were preceded by the finding of their defense-and-surveillance systems against patho- thionins in plants,7 the earliest example of antimicro- gens. Early concepts of nonspecific and specific de- bial peptides related to host defense. At the moment fense systems for plants and animals, respectively, are being reevaluated and expanded in the light of grow- of this writing, several hundreds of structures with ing evidence that plants are endowed with certain some type of antimicrobial activity have been de- specific defense systems, while on the other hand scribed. A quite comprehensive, periodically updated innate (nonadaptive) immunity in animals largely de- data base can be found on the Internet at http:// pends on nonspecific effectors.1–6 In particular, gene- www.bbcm.univ.tries.it/;tossi. The present chapter is encoded antimicrobial peptides are now clearly estab- meant to provide a general overview of the main lished as key players in both plant and animal defense families of animal host defense peptides, as well as systems. In the last two decades, a considerable num- selected details on their biological action, including Correspondence to: David Andreu, Department of Organic Chemistry, Universitat de Barcelona, Martı´ i Franque`s 1-11, E-08028 Barcelona, Spain; email: [email protected] Contract grant sponsor: Comunidad Auto´noma de Madrid (CAM), European Union (EU), Fondo de Investigaciones Sanitarias (FIS), Generalitat de Catalunya (CERBA), and Spanish Ministry of Education and Science (SMES) Contract grant number: 08.2/0029.1/98 (CAM), IC18-CT97- 0213 (EU), SAF95-0019 (FIS), and PB94-0845 (SMES) Biopolymers (Peptide Science), Vol. 47, 415–433 (1998) © 1999 John Wiley & Sons, Inc. CCC 0006-3525/99/060415-19 415 416 Andreu and Rivas also relevant synthetic analogues. A number of sig- Glycosylation nificant aspects of this emerging field have been cov- ered by recent reviews8–23 and by the accompanying Glycosylation has been described in five antimicrobial articles in this issue. peptides from insects, all of them belonging to the proline-rich structural subgroup: diptericin,50 droso- cin,51 formaecin,53 lebocin,56 and pyrrhocorricin.60 Occurrence of glycosylation is probably underesti- STRUCTURAL ASPECTS mated; for instance, a diptericin-like peptide from Sarcophaga peregrina117 reported before the first re- 51 A considerable variety of peptide sizes and structures port on drosocin glycosylation has not been further are associated to antimicrobial activity in eukaryotic investigated in this respect. Only O-glycosylation has hosts. The early classification of antimicrobial pep- been described to date in insects, with the oligosac- tides on a taxonomical basis has been increasingly charide chain linked to the peptide backbone through found inadequate, in view of the fact that very similar a threonine residue. Although a common requirement structural patterns are shared by peptides from widely for O-glycosylation seems to be the presence of 2 different organisms. In contrast, the alternative clas- nearby proline residues, especially in positions 1 1 118 sification based on chemical-structural criteria1 is still and 3 from the glycosylated threonine, one of the oligosaccharide chains of diptericin occurs in a gly- quite useful for cataloging the different families of 50 antimicrobial peptides. This classification defines two cine-rich region. O-oligosaccharide chains are short broad groups, corresponding to linear and cyclic and often microheterogeneous. Glycosylations with 3 3 3 structures, respectively. Within the first group, two only one (GalNAc Thr), two (Gal GalNAc Thr), or three (Glc 3 Gal 3 GalNAc 3 Thr) glycan subgroups can be distinguished (a) linear peptides 50,51,53,56,60 tending to adopt a-helical amphipathic conformation residues have been described. As a general (Table I); and (b) linear peptides of unusual compo- rule, integrity of the oligosaccharide chain is neces- sition, rich in amino acids such as Pro, Arg, or (oc- sary for optimal antimicrobial activity. Thus, treat- casionally) Trp (Table II). The second group, encom- ment of diptericin with O-glycosydase abolished the antibacterial activity of diptericin against most bacte- passing all cystine-containing peptides, can also be 50 divided into two subgroups corresponding to single or ria tested and the antibacterial activity of a nongly- cosylated synthetic drosocin is several times lower multiple disulfide structures (Tables III and IV), re- 56 spectively. Tables I–IV include sequences of some the than the native compound. earliest reported antimicrobial structures, as well as Aside from its important role in antimicrobial ac- recent noteworthy additions, with no pretense to be tivity, little is known about other roles of glycosyla- exhaustive. Readers looking for additional structures tion in the lethal mechanisms of the corresponding are directed to the above Internet address and other peptides, though some ideas have been advanced, general reviews of this field.1–23 such as protection against proteinases, modification of A number of secondary structures of antimicrobial secondary structure inhibition of enzymes involved in peptidoglycan biosynthesis or specific recognition be- peptides, broadly representative of the above struc- 50,51,53,119 tural groups, have been determined by two-dimen- tween pathogen and peptide. It is notewor- sional nmr, either in solution or in model membrane thy that glycosylated peptides do not seem to have environments. They include cecropins,89–92 magain- membrane permeabilization as their main mechanism ins,93–95 PGLa,96 sarcotoxin,97 buforin,98 caerin,99 of action. Evidence for nonmembrane mechanisms bactenecins,100 enkelytin,101 histatin,102 ranalexin,103 are as follows: (a) Deglycosylated all-D-diptericin is 104 105 106 much less active than the deglycosylated natural thanatin, protegrin, tachyplesin, different 120 types of defensins,107–115 and drosomycin.116 form. (b) Kinetics of the lethal process is usually quite slow for membrane permeabilization; long con- tact periods (usually hours) between peptide and mi- croorganism are required for pyrrhocoricin, drosocin, POSTTRANSLATIONAL and formaecins to produce a bactericidal effect.50,51,53 MODIFICATIONS Disulfide Bonds Antimicrobial peptides display different types of post- translational modifications that can modify their ac- Intramolecular disulfide bonds are relatively common tivity in a significant way. The following are among in antimicrobial peptides. Structures ranging from one the most frequent. to five disulfides have been reported (Tables III and Table I Linear Antimicrobial Peptides with Helical Conformation Peptide Sequence Source Reference Andropin VFIDILDKVNAIHNAAQVGIGFAKPFEKLINPK Fruit fly (Drosophila melanogaster)24 BLP-1 GIGASILSAGKSALKGLAKGLAEHFANa Asian toad (Bombina orientalis)25 Bombinin GIGALSAKGALKGLAKGLAEHFANa Yellow-bellied toad (Bombina variegata)26 Bombolitin IKITTMLAKLGKVLAHVa Bumblebee (Megabombus pennsylvanicus)27 Cecropin A KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAKa Silk moth (Hyalophora cecropia)28 Cecropin RWKIFKKIEKMGRNIRDGIVKAGPAIEVIGSAKAIa Silk moth (Bombyx mori)29 Cecropin WNPFKELERAGQRVRDAVISAAPAVATVGQAAAIARGa Tobacco moth (Manduca sexta)30 Cecropin C GWLKKLGKRIERIGQHTRDATIQGLGIAQQAANVAATARGa Fruit fly (Drosophila melanogaster)31 Cecropin P1 SWLSKTAKKLENSAKKRISEGIAIAIQGGPRa Pig (Sus scrofa)32 Ceratotoxin A SIGSALKKALPVAKKIGKIALPIAKAALP Mediterranean fruit fly (Ceratitis capitata)33 Clavanin A VFQFLGKIIHHVGNFVHGFSHVFa Tunicate (Styela clava)34 CRAMP ISRLAGLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE Mouse (Mus musculus)35 Dermaseptin 1 ALWKTMLKKLGTMALHAGKAALGAAANTISQGTQ Arboreal frog (Phyllomedusa sauvageii)36 Enbocin WNYFKEIERAVARTRDAVISAGPAVATVAAATSVASa Silk moth (Bombyx mori)37 FALL-39 FALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Man (Homo sapiens)38 Lycotoxin I IWLTALKFLGKHAAKHLAKQQLSKLa Wolf spider (Lycosa carolinensis)39 Magainin 1 GIGKFLHSAGKFGKAFVGEIMKS South African clawed frog (Xenopus laevis)40 Melittin GIGAVLKVLTTGLPALISWIKRKRQQa Honeybee (Apis mellifera)41 Animal Antimicrobial Peptides Misgurin RQRVEELSKFSKKGAAARRRK Mudfish (Misgurnus anguillicaudatus)42 PGLa GMASKAGAIAGKIAKVALKALa South African clawed frog (Xenopus laevis)43 Pleurocidin
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