Purification, cDNA structure and biological significance of a single insulin-like growth factor-binding domain protein (SIBD-1) identified in the hemocytes of the spider Cupiennius salei

Autor: Tommy Baumann, Sathyan Chandru, Carlo R. Largiadèr, Johann Schaller, Stefan Schürch, Wolfgang Nentwig, Lucia Kuhn-Nentwig, Kathrin Streitberger, Urs Kämpfer
Rok vydání: 2011
Předmět:
Zdroj: Insect Biochemistry and Molecular Biology. 41:891-901
ISSN: 0965-1748
DOI: 10.1016/j.ibmb.2011.08.003
Popis: Cupiennius salei single insulin-like growth factor-binding domain protein (SIBD-1), which exhibits an IGFBP N-terminal domain-like profile, was identified in the hemocytes of the spider C. salei. SIBD-1 was purified by RP-HPLC and the sequence determined by a combination of Edman degradation and 5'-3'- RACE PCR. The peptide (8676.08 Da) is composed of 78 amino acids, contains six intrachain disulphide bridges and carries a modified Thr residue at position 2. SIBD-1 mRNA expression was detected by quantitative real-time PCR mainly in hemocytes, but also in the subesophageal nerve mass and muscle. After infection, the SIBD-1 content in the hemocytes decreases and, simultaneously, the temporal SIBD-1 expression seems to be down-regulated. Two further peptides, SIBD-2 and IGFBP-rP1, also exhibiting IGFBP N-terminal domain variants with unknown functions, were identified on cDNA level in spider hemocytes and venom glands. We conclude that SIBD-1 may play an important role in the immune system of spiders.
Databáze: OpenAIRE