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. 2004 Apr 26;101(19):7363–7368. doi: 10.1073/pnas.0401567101

Table 2. Recognition of diverse classes of antimicrobial peptides by the enantiomeric sequence formulae.

Sequence isoform, no. found
Antimicrobial peptide class Phylogeny Dextro Levo-1 Levo-2 Total % of total
α-Defensin Chordata 24 42 6 72 15.3
β-Defensin Chordata 52 65 31 148 31.4
θ-Defensin Chordata 1 1 0 2 0.4
Insect defensin/CS-αβ Insectae 21 23 12 56 11.9
Plant defensin/CS-αβ Plantae 51 67 20 138 29.3
Invertebrate defensin/CS-αβ Mollusca 3 4 4 11 2.3
Protegrins/gomesins Chordata/Arthropoda 0 0 6 6 1.3
Tachyplesins/Polyphemusins Arthropoda 6 5 2 13 2.8
Thanatin Arthropoda 0 1 0 1 0.2
Mytilins/Big Defensin Mollusca 3 3 2 8 1.7
AFP-1 Ascomycota 1 0 0 1 0.2
Lantibiotics/microcins Proteobacteria 3 3 9 15 3.2
Total 165 214 92 471

Forward or reverse Swiss-Prot databases (release 42.4; November 14, 2003; 138,347 entries) were probed with formulae containing the dextromeric or levomeric motifs of the antimicrobial peptide signature by using prosite (14). Data indicate the proportionate distribution of a nonredundant cohort of retrieval sets; in some cases, peptides were retrieved by more than one formula isoform. Note that search results include members of the lantibiotic superfamily of antimicrobial peptides, which lack conventional disulfide bridges but have thioether stabilization.