Gene organization of a novel defensin of Ixodes ricinus: first annotation of an intron/exon structure in a hard tick defensin gene and first evidence of the occurrence of two isoforms of one member of the arthropod defensin family
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17651239
DOI
10.1111/j.1365-2583.2007.00745.x
PII: IMB745
Knihovny.cz E-resources
- MeSH
- Defensins chemistry genetics metabolism MeSH
- Exons genetics MeSH
- Gastrointestinal Tract MeSH
- Introns genetics MeSH
- Ixodes genetics metabolism MeSH
- Molecular Sequence Data MeSH
- Protein Isoforms genetics MeSH
- Gene Expression Regulation MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Defensins MeSH
- Protein Isoforms MeSH
Antimicrobial peptides (defensins) are effectors of the immune system. Herein, we describe a novel Ixodes ricinus defensin gene(s), analyse its structure and compare it with other known antimicrobial peptides from different tick species. For the first time, an intron/exon structure is discovered in a hard-tick defensin gene. The intron/exon genomic organization of the gene is similar to the organization in Ornithodoros moubata, but not to that of the intronless defensins of Dermacentor variabilis and Ixodes scapularis. The analysis of the deduced amino acid sequences of different recombinants from the I. ricinus cDNA library reveals the presence of two defensin isoforms with three amino acid substitutions. Whether or not these substitutions affect the biological properties of the peptides is currently unknown. The expression of the defensin gene is strongly induced in the tick midgut after infection with Borrelia burgdorferi.
References provided by Crossref.org
Insect Antimicrobial Peptides, a Mini Review
Functional characterization of two defensin isoforms of the hard tick Ixodes ricinus
