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Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, Hyas araneus.

Abstract：

:Antimicrobial peptides (AMPs) are considered to play an important role as host-defense molecules in both vertebrates and invertebrates. This work was undertaken to characterize AMPs from hemocyte extracts of the small spider crab, Hyas araneus. A novel proline-arginine-rich AMP of 37 amino acids was isolated and characterized. The peptide, named arasin 1, has a chimeric structure with an N-terminal domain rich in proline and arginine and a C-terminal domain containing two disulfide linkages. The peptide precursor of 64 amino acids, deduced from a cDNA library, contained a hydrophobic pre-region of 25 amino acids, directly followed by the mature peptide. C-terminally, this precursor had two additional amino acids, which seem to be cleaved off post-translationally. Synthetic arasin 1 showed antibacterial activity. A putative isoform of arasin 1, named arasin 2, was found at the genetic level, and both transcripts were shown by real-time RT-PCR to be expressed mainly in hemocytes.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Stensvåg K,Haug T,Sperstad SV,Rekdal O,Indrevoll B,Styrvold OB

doi

10.1016/j.dci.2007.06.002

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

275-85

issue

3

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(07)00088-2

journal_volume

32

pub_type

杂志文章

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