Premium
Mapping the peptide and protein immune response in the larvae of the fleshfly Sarcophaga bullata
Author(s) -
Ciencialová Alice,
Neubauerová Tereza,
Šanda Miloslav,
Šindelka Radek,
Cvačka Josef,
Voburka Zdeněk,
Buděšínský Miloš,
Kašička Václav,
Sázelová Petra,
Šolínová Veronika,
Macková Martina,
Koutek Bohumír,
Jiráček Jiří
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.967
Subject(s) - hemolymph , peptide , antimicrobial , antimicrobial peptides , cecropin , microbiology and biotechnology , biochemistry , biology , escherichia coli , chemistry , gene
We chose the larvae of fleshfly Sarcophaga bullata to map the peptide and protein immune response. The hemolymph of the third‐instar larvae of S. bullata was used for isolation. The larvae were injected with bacterial suspension to induce an antimicrobial response. The hemolymph was separated into crude fractions, which were subdivided by RP‐HPLC, gel electrophoresis, and free‐flow electrophoresis. In several fractions, we determined significant antimicrobial activities against the pathogenic bacteria Escherichia coli, Staphylococcus aureus, or Pseudomonas aeruginosa . Among antimicrobially active compounds we identified dipeptide β‐alanyl‐ L ‐tyrosine, protein transferrin, and two variants of peptide sapecin. We also partially characterized two novel antimicrobially active polypeptides; odorant‐binding protein 99b, and a peptide which remains unidentified. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.