AMP > Introduction > Differentiating
antimicrobial peptides: Memberss of the major groups of antimicrobial peptides have been classified mainly on the basis of their biochemical (net charge) and/or structural features (linear/circular/amino acid composition), looking for common patterns that might help to distinguish them(Tossi and Sandri, 2002; Zasloff, 2002). The resulting most important groups are the following: From Eukaryotes Cationic peptides: This is the largest group and the first to be reported, being widely distributed in animals and plants. So far, more than a thousand of such peptides have been characterized and over 50 % of them have been isolated from insects (Bulet et al. 1999; Andreu and Rivas, 1998). On the basis of their structural features, cationic peptides can be divided as well into three different classes: (1) linear peptides forming-helical structures; (2) cysteine-rich open-ended peptides containing single or several disulfide bridges; and (3) molecules rich in specific amino acids such as proline, glycine, histidine and tryptophan. Important subfamilies of cationic peptides include:
Two other forms of precursor-derived peptides are represented by cathelicidins and thrombocidins. The formers are quite abundant in mammals and generated from precursor proteins bearing an amino-terminal cathepsin L inhibitor domain (cathelin) . The latters are compounds released from platelets and arise from deletions of the CXC chemokines neutrophil-activating peptide 2 and connective tissue-activating III in humans (Krijgsveld et al. 2000). In plants, a
similar picture is slowly emerging. A new family of antimicrobial
peptides has been described from Macadamia integrifolia of which
the first purified member has been termed MiAMP2c . The peptide,
active against a number of plant pathogens in vitro, derives from
a precursor protein similar to vicilins 7S globulin proteins, suspected
of a putative participation in defense during seed germination (Marcus et al. 1997). The novel peptide
is inserted in the highly hydrophilic N-proximal region of the
precursor, where three additional cysteine-containing MiAMP2c-like
patterns exist, suggestive of three additional peptide isoforms, a
pattern already described for fish AMPs . From Prokaryotes: The antimicrobial peptides produced by bacteria have been grouped into different classes based upon the producer organisms, molecular size, chemical structure and mode of action, which resulted in different names for putative compounds which turned out to be identical: (thiolbiotics, lantibiotic microcin, colicin, bacteriocin, to name a few) . The most relevant active-membrane peptides among them are produced by gram-positive bacteria and classified taxonomically as bacteriocins (Oscáriz and Pisabarro, 2001).. Some of them have been the center of attention because of their application as food preservatives . Bacteriocins, cationic,
neutral and anionic in chemical nature, are all in the range of 1.9
(Actagardine) and 5.8 (Lactococcin B) kDa in molecular mass , cationic,
neutral and anionic in chemical nature . The most thoroughly
studied bacteriocins are those produced by lactic-acid bacteria, of
which sakacins seem to be most unique , and the lantibiotics, which
contain modified amino acid residues . Another representative,
pediocins, are usually co-transcribed with a gene encoding a
cognate-immunity protein(Fimland et al. 2002) . The 44-amino acid
pediocin produced by Pediococcus acidilactici strains is encoded
in an 8.9 kb plasmid.
TOSSI, A.
and SANDRI, L. Molecular diversity in gene-encoded, cationic
antimicrobials polypeptides. Current Pharmaceutical Design,
2002, vol. 8, no. 9, p. 743-761. ZASLOFF,
M. Antimicrobial peptides of multicellular organisms. Nature,
2002, vol. 415, no. 6870, p. 389-395. BULET, P.; HETRU, C.; DIMARCQ, J. and HOFFMANN, D. Antimicrobial peptides in insects; structure and function. Developmental Comparative Immunology, 1999, vol. 23, no. 4-5, p. 329-344. ANDREU, D.
and RIVAS, L. Animal antimicrobial peptides: an overview. Biopolymers,1998,
vol. 47, no. 6, p. 415-433. ZASLOFF, M. Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation characterization of two active forms, and partial cDNA sequence of a precursor. Proceeding of the National Academy of Sciences USA, 1987, vol. 84, no. 9, p. 5449-5453. BECHINGER,
B.; ZASLOFF, M. and OPELLA, S.J. Structure and orientation of the
antibiotic peptide magainin in membranes by solid-state nuclear
magnetic resonance spectroscopy. Protein Sciences, 1993,
vol. 2, no. 12, p. 2077-2084. SIMMACO, M.; MIGNOGNA,
G. and BARRA, D. Antimicrobial peptide from amphibian
skin: What do they tell us? Biopolymers, 1998,
vol. 47, no. 6, p. 435-450. TANG,
Y.Q.; YUANG, J.; OSAPAY, G.D.; OSAPAY, K.; TRAN, D.; MILLER, C.J.;
OUELLETTE, A.J. and SELSTED, M.E. A cyclic antimicrobial peptide
produces in primate leukocytes by the ligation of two truncated
alpha-defensins. Science, 1999, vol. 286, no. 5439, p. 498-502. LEHRER,
R.I. and GANZ, T. Defensin of vertebrate animals. Current Opinion
in Immunology, 2002, vol. 14, no. 1, p. 96-102. BOHLMANN,
H. The role of thionins in the resistance of plants. In: DATTA,
S.K., MUTHUKRISHNAN, S. eds. Pathogenesis-related proteins in
plants, CRC Press, 1999, p. 207-234. LI ,S.S.;
GULLBO, J.; LINDHOLM, P.; LARSSON, R.; THUNBERG, E.; SAMUELSSON,
G.; BOHLIN, L. and CLAESON, P. Ligatoxin B, a new cytotoxic protein
with a novel helix-turn-helix DNA-binding domain from the mistletoe Phoradendron
liga. Biochemistry Journal, 2002, vol. 366,
no. 2, 405-413. BULET, P.; HETRU, C.; DIMARCQ, J. and HOFFMANN, D. Antimicrobial peptides in insects; structure and function. Developmental Comparative Immunology, 1999, vol. 23, no. 4-5, p. 329-344. OTVOS, L.
Jr. Antibacterial peptides isolated from insects. Journal
of Peptide Sciences, 2000, vol. 6, no. 10, p. 497-511. TOSSI, A.
and SANDRI, L. Molecular diversity in gene-encoded, cationic
antimicrobials polypeptides. Current Pharmaceutical Design,
2002, vol. 8, no. 9, p. 743-761. PARK,
C.B.; KIM MS. and KIM S.C. A novel antimicrobial peptide from Bufo
bufo gargarizans. Biochemical Biophysical Research
Communications, 1996, vol. 218, no. 1, p. 408-413. IWANAGA,
S.; MUTA, T.; SHIGENAGA, T.; MIURA, Y.; SEKI, N.; SAITO, T. and
KAWABATA, S. Role of hemocyte-derived granular components in
invertebrate defense. Annals of the New York Academy of Sciences,
1994, vol. 712, p. 102-116. LEMAITRE,
C.; ORANGE, N.; SAGLIO, P.; SAINT, N.; GAGNON, J. and MOLLE, G.
Characterization and ion channel activities of novel antibacterial
proteins from the skin mucosa of carp (Cyprinus carpio). European
Journal of Biochemistry, 1996, vol. 240, no. 1, p. 143-149. ZHOU,
Q.J.; SHAO, J.Z. and XIANG, L.X. Progress in fish antibacterial
peptide research. Progress in Biochemistry and Biophysics, 2002,
vol. 29, no. 5, p.682-685. MANDARD, N.; SY, D.; MAUFRAIS, C.; BONMATIN J.M.; BULET, P.; HETRU, C. and VOVELLE, F. Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer. Journal of Biomolecular Structure and. Dynamics, 1999, vol. 17, no. 2, p. 367-380. ANDERSEN,
J.; OSBAKK, S.; VORLAND, L.; TRAAVIK, T. and GUTTEBERG, T. Lactoferrin
and cyclic lactoferricin inhibit the entry of human cytomegalovirus
into human fibroblasts. Antiviral Research, 2001, vol. 51,
no. 2, p. 141-149. KRIJGSVELD,
J.; ZAAT, S.A.J.; MEELDIJK, J.; VAN VEELEN, P.A.; FANG, G.; POOLMAN,
B.; BRANDT, E.; EHLERT, J.E.; KUIJPERS, A.J.; ENGBERS, G.H.M.; FEIJEN,
J.; and DANKERT, J. Thrombocidins, microbicidal proteins from human
blood platelets are C-terminal deletion products of CXC chemokines. Journal
of Biological Chemistry, 2000, vol. 275, no. 27, p.
20374-20381. MARCUS,
J.P.; GOULTER, K.C.; GREEN, J.L.; HARRISON, S.J. and MANNERS, J.M.
Purification, characterisation and cDNA cloning of an antimicrobial
peptide from Macadamia integrifolia. European Journal
of Biochemistry, 1997, vol. 244, no. 3, p. 743-749. OSCÁRIZ, J.C. and PISABARRO, A.G. Classification and mode of action of membrane-active bacteriocins produced by gram-positive bacteria. International Microbiology, 2001, vol. 4, no. 1, p. 13-19. FIMLAND, G.; EIJSINK, V.G. and NISSEN-MEYER, J. Comparative studies of immunity proteins of pediocin-like bacteriocins. Microbiology, 2002, vol. 148, p. 3661 - 3670.
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