Mapping the peptide and protein immune response in the larvae of the fleshfly Sarcophaga bullata.
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 beta-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.
Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Praha 6, Czech Republic.
Alice
A
Ciencialová
Tereza
T
Neubauerová
Miloslav
M
Sanda
Radek
R
Sindelka
Josef
J
Cvacka
Zdenek
Z
Voburka
Milos
M
Budesínský
Václav
V
Kasicka
Petra
P
Sázelová
Veronika
V
Solínová
Martina
M
Macková
Bohumír
B
Koutek
Jirí
J
Jirácek
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004175:Diptera / Q000254:growth & development / Q000276:immunology*; D004591:Electrophoresis, Polyacrylamide Gel; D019476:Insect Proteins / Q000737:chemistry / Q000276:immunology*; D007814:Larva / Q000276:immunology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010449:Peptide Mapping; D021241:Spectrometry, Mass, Electrospray Ionization
D019476:Insect Proteins