Cloning and characterization of genes encoding an antifreeze protein from the spruce budworm, Choristoneura fumiferana

1999 ◽  
Vol 77 (4) ◽  
pp. 391
Author(s):  
Daniel Doucet ◽  
Michael G. Tyshenko ◽  
Peter L. Davies ◽  
Virginia K. Walker
Keyword(s):  
Choristoneura Fumiferana ◽  
Spruce Budworm ◽  
Antifreeze Protein ◽  
Genes Encoding

Cloning and characterization of genes encoding an antifreeze protein from the spruce budworm, Choristoneura fumiferana

1999 ◽  
Vol 77 (4) ◽  
pp. 391
Author(s):  
Daniel Doucet ◽  
Michael G Tyshenko ◽  
Peter L Davies ◽  
Virginia K Walker
Keyword(s):  
Choristoneura Fumiferana ◽  
Spruce Budworm ◽  
Antifreeze Protein ◽  
Genes Encoding

scholarly journals Disulfide bond mapping and structural characterization of spruce budworm antifreeze protein

1998 ◽  
Vol 258 (2) ◽  
pp. 445-453 ◽  
Author(s):  
Sherry Y. Gauthier ◽  
Cyril M. Kay ◽  
Brian D. Sykes ◽  
Virginia K. Walker ◽  
Peter L. Davies
Keyword(s):  
Disulfide Bond ◽  
Structural Characterization ◽  
Spruce Budworm ◽  
Antifreeze Protein

Cloning and characterization of two glutathioneS-transferase cDNAs in the spruce budworm,Choristoneura fumiferana

2007 ◽  
Vol 66 (3) ◽  
pp. 146-157 ◽  
Author(s):  
Sichun Zheng ◽  
Huimin Deng ◽  
Tim Ladd ◽  
Bill L. Tomkins ◽  
Peter J. Krell ◽  
...  
Keyword(s):  
Choristoneura Fumiferana ◽  
Spruce Budworm

Characterization of EST-based SSR loci in the spruce budworm, Choristoneura fumiferana (Lepidoptera: Tortricidae)

2013 ◽  
Vol 5 (2) ◽  
pp. 541-544 ◽  
Author(s):  
B. M. T. Brunet ◽  
D. Doucet ◽  
B. R. Sturtevant ◽  
F. A. H. Sperling
Keyword(s):  
Choristoneura Fumiferana ◽  
Spruce Budworm ◽  
Ssr Loci

scholarly journals Novel anionic cecropins from the spruce budworm feature a poly-L-aspartic acid C-terminus

2018 ◽  
Author(s):  
Halim Maaroufi ◽  
Michel Cusson ◽  
Roger C. Levesque
Keyword(s):  
Anticancer Activity ◽  
Aspartic Acid ◽  
Choristoneura Fumiferana ◽  
Antibacterial Properties ◽  
Spruce Budworm ◽  
Duplication Event ◽  
List Type ◽  
C Terminus ◽  
Genes Encoding ◽  
Dynamics Simulations

AbstractCecropins form a family of amphipathic α-helical cationic peptides with broad-spectrum antibacterial properties and potent anticancer activity. The emergence of bacteria and cancer cells showing resistance to cationic antimicrobial peptides (CAMPs) has fostered a search for new, more selective and more effective alternatives to CAMPs. With this goal in mind, we looked for cecropin homologs in the genome and transcriptome of the spruce budworm, Choristoneura fumiferana. Not only did we find paralogs of the conventional cationic cecropins (Cfcec+), our screening also led to the identification of previously uncharacterized anionic cecropins (Cfcec−), featuring a poly-L-aspartic acid C-terminus. Comparative peptide analysis indicated that the C-terminal helix of Cfcec− is amphipathic, unlike that of Cfcec+, which is hydrophobic. Interestingly, molecular dynamics simulations pointed to the lower conformational flexibility of Cfcec− peptides, relative to that of Cfcec+. Phylogenetic analysis suggests that the evolution of distinct Cfcec+ and Cfcec− peptides may have resulted from an ancient duplication event within the Lepidoptera. Our analyses also indicated that Cfcec− shares characteristics with entericidins, which are involved in bacterial programmed cell death, lunasin, a peptide of plant origins with antimitotic effects, and APC15, a subunit of the anaphase-promoting complex. Finally, we found that both anionic and cationic cecropins contain a BH3-like motif (G-[KQR]-[HKQNR]-[IV]-[KQR]) that could interact with Bcl-2, a protein involved in apoptosis; this observation is congruent with previous reports indicating that cecropins induce apoptosis. Altogether, our observations suggest that cecropins may provide templates for the development of new anticancer drugs.Graphical abstractHighlightsGenes encoding novel anionic cecropins (Cfcec−), featuring a C-terminal poly-L-aspartic acid, were found in the genome of the spruce budworm, Choristoneura fumiferana.Divergence between Cfcec+ and Cfcec− could be the result of an ancient duplication event within the Lepidoptera.There is an apparent relationship between motifs observed in cecropin peptides and apoptosis.Anionic cecropins from the spruce budworm display characteristics suggesting they could have anticancer activity

Sign in / Sign up

Export Citation Format

Share Document