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Published on: November 5, 2012
Trichoplusia ni lebocin, an inducible immune gene with a downstream insertion element
1Department of Microbiology, Stockholm University, Stockholm, 10609, Sweden.
Insights
Researchers identified a novel lebocin-like protein in the cabbage looper (Trichoplusia ni) that is inducible by bacterial challenge. This immune-related protein is primarily expressed in the fat body and hemocytes.
Area of Science:
- Insect immunology
- Molecular biology
- Biochemistry
Background:
- The cabbage looper (Trichoplusia ni) is a significant agricultural pest.
- Understanding insect immune responses is crucial for pest control strategies.
- Lebocin and metchnikowin are known antimicrobial peptides in other insects.
Purpose of the Study:
- To identify and characterize novel immune-responsive genes in Trichoplusia ni.
- To investigate the expression patterns of a newly discovered lebocin-like protein.
- To analyze the structural and evolutionary features of the identified protein.
Main Methods:
- Differential display PCR was used to identify genes with altered expression.
- Northern blot analysis was performed to confirm gene expression patterns.
- Bioinformatic tools were used for protein sequence analysis and comparison.
Main Results:
- A cDNA clone encoding a 143-amino acid lebocin-like protein was isolated.
- Gene expression was inducible by bacterial challenge, peaking at 20 hours post-injection.
- Transcripts were detected in fat body and hemocytes, with sequence homology to Bombyx mori lebocin and Drosophila metchnikowin.
Conclusions:
- A novel inducible immune protein, similar to known antimicrobial peptides, has been identified in Trichoplusia ni.
- The protein's expression pattern suggests a role in the insect's innate immune response.
- Further research is warranted to elucidate the specific antimicrobial functions of this lebocin-like protein.
Abstract:
A cDNA clone encoding a lebocin-like protein was obtained from the cabbage looper Trichoplusia ni by using differential display PCR. Northern blot analysis showed that lebocin gene expression was inducible upon bacterial challenge. Transcripts were mainly found in fat body but were also observed in hemocytes. Expression reached its highest level at 20 h and continued at least until 60 h after bacterial injection. The deduced protein is proline-rich and contains 143 amino acid residues. At position 128, a possible O-glycosylation site is observed. The whole protein shows 35% identity to Bombyx mori lebocin. The mature peptide displays an N-terminus similar to that of lebocin and a C-terminus to that of Drosophila metchnikowin. A 39-bp repetitive element is located downstream of the coding region.
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