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Nonmammalian vertebrate antibiotic peptides

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Abstract

With the exception of cyclostomes, all vertebrates share the common immune strategy of adaptive, highly specific immunity, based on the products of recombination-activating genes and recombined noninherited receptors for antigens. In addition, they have retained ancient vectors of innate immunity, such as antimicrobial peptides, which are widespread in all eukaryotic organisms and show a high degree of structural homology across most animal taxa. Recently, these substances have become the objects of intensive study for their outstanding bioactive properties with the aim to be applied as very efficient antibiotics, antimicrobials, and even cancerostatics in clinical practice.

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Abbreviations

BLP:

bombinin-like peptide

C3:

third component of complement

CHP:

chicken heterophil peptide

CPF:

cerulein precursor fragment

DRP-AA:

dermaseptin-related peptide fromAgalychnis annae

DRP-PD:

dermaseptin-related peptide fromPachymedusa dacnicolor

f.:

family

GAL:

gallinacins

GALT:

gut-associated lymphoid tissue

GlcNAc:

N-acetyl-d-glucosamine

GPV:

gallopavins

HFA:

hagfish antimicrobial peptide

HFIAP:

hagfish intestinal antimicrobial peptide

HIV:

human immunodeficiency virus

HLMP:

hagfish leukocyte-associated membrane protein

IκB:

inhibition factor κB

LAP:

lingual antimicrobial peptide

LCRP:

lamprey corticostatin-related peptide

MHC:

major histocompatibility complex

Myr BP:

million years before present

NF-IL6:

nuclear factor for interleukin-6

NF-κB:

nuclear factor κB

NOS:

nitric-oxide synthase

OTAP:

ovotransferrin antimicrobial peptide

PGLa:

peptide with aminoterminal glycine and carboxyterminal leucine amide

PLA2 :

phospholipases A2

RAG:

recombination-activating genes

sf.:

subfamily

syn.:

synonymum

TAP:

bovine tracheal antimicrobial peptide

TCR:

T cell recptor

THP:

turkey heterophil peptide

vPLA2 :

venom phospholipases A2

XPF:

xenopsin precursor fragment

XT:

Xenopus tropicalis antimicrobial peptide

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Authors and Affiliations

  1. Division of Immunology and Gnotobiology, Academy of Sciences of the Czech Republic, 142 20, Prague, Czechia

    P. Šíma & I. Trebichavský

  2. Laboratory of Cell Biology, Institute of Microbiology, Academy of Sciences of the Czech Republic, 142 20, Prague, Czechia

    K. Sigler

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  3. K. Sigler
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Correspondence to P. Šíma.

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This review is a continuation of a recently published survey of mammalian antimicrobial substances (Šimaet al. 2003); in nonmammalian vertebrates, antimicrobial peptides represent a very effective component of defense.

The work associated with the topic of this review was supported by theGrant Agency of the Czech Republic (grants 524/01/0917 and 301/02/1232), by theGrant Agency of the Academy of Sciences of the Czech Republic (grant S502 0202) and by theInstitutional Research Concept AV 0Z 502 0903.

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Šíma, P., Trebichavský, I. & Sigler, K. Nonmammalian vertebrate antibiotic peptides. Folia Microbiol 48, 709–724 (2003). https://doi.org/10.1007/BF02931504

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