A thioredoxin-like protein (txl) gene was cloned from the bumblebee, Bombus ignitus. The B. ignitus txl (Bitxl) gene spans 1777 bp and consists of three introns and four exons coding for 285 amino acid residues with a conserved active site (CGPC). The deduced amino acid sequence of the Bitxl cDNA was 65% similar to the Drosophila melanogaster txl. Northern blot analysis revealed the presence of Bitxl transcripts in all tissues examined. When H2O2 was injected into the body cavity of B. ignitus workers, Bitxl mRNA expression was up-regulated in the fat body tissue. In addition, the expression levels of Bitxl mRNA in the fat body greatly increased when B. ignitus workers were exposed to low (4°C) or high (37°C) temperatures, or injected with lipopolysaccharide (LPS), which suggests that the Bitxl possibly protects against oxidative stress caused by extreme temperatures and bacterial infection.
A serine protease gene was cloned from the bumblebee, Bombus ignitus. The B. ignitus serine protease (BiSP) gene spans 1702 bp and consists of four introns and five exons coding for 250 amino acid residues. Southern blot analysis of genomic DNA suggested that BiSP gene is a single copy gene. The cDNA encoding BiSP was expressed as a 28-kDa polypeptide in baculovirus-infected insect cells and the recombinant BiSP showed activity in a protease enzyme assay. BiSP was specifically expressed in the midgut of B. ignitus queens, males, and workers, suggesting that the BiSP is a gut enzyme involved in the digestion of dietary proteins.