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Insect antimicrobial peptides and their applications
#MMPMID24811407
Yi HY
; Chowdhury M
; Huang YD
; Yu XQ
Appl Microbiol Biotechnol
2014[Jul]; 98
(13
): 5807-22
PMID24811407
show ga
Insects are one of the major sources of antimicrobial peptides/proteins (AMPs).
Since observation of antimicrobial activity in the hemolymph of pupae from the
giant silk moths Samia Cynthia and Hyalophora cecropia in 1974 and purification
of first insect AMP (cecropin) from H. cecropia pupae in 1980, over 150 insect
AMPs have been purified or identified. Most insect AMPs are small and cationic,
and they show activities against bacteria and/or fungi, as well as some parasites
and viruses. Insect AMPs can be classified into four families based on their
structures or unique sequences: the ?-helical peptides (cecropin and moricin),
cysteine-rich peptides (insect defensin and drosomycin), proline-rich peptides
(apidaecin, drosocin, and lebocin), and glycine-rich peptides/proteins (attacin
and gloverin). Among insect AMPs, defensins, cecropins, proline-rich peptides,
and attacins are common, while gloverins and moricins have been identified only
in Lepidoptera. Most active AMPs are small peptides of 20-50 residues, which are
generated from larger inactive precursor proteins or pro-proteins, but gloverins
(~14 kDa) and attacins (~20 kDa) are large antimicrobial proteins. In this
mini-review, we will discuss current knowledge and recent progress in several
classes of insect AMPs, including insect defensins, cecropins, attacins, lebocins
and other proline-rich peptides, gloverins, and moricins, with a focus on
structural-functional relationships and their potential applications.
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