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
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
17651239
DOI
10.1111/j.1365-2583.2007.00745.x
PII: IMB745
Knihovny.cz E-zdroje
- MeSH
- defensiny chemie genetika metabolismus MeSH
- exony genetika MeSH
- gastrointestinální trakt MeSH
- introny genetika MeSH
- klíště genetika metabolismus MeSH
- molekulární sekvence - údaje MeSH
- protein - isoformy genetika MeSH
- regulace genové exprese MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- defensiny MeSH
- protein - isoformy 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.
Citace poskytuje Crossref.org
Insect Antimicrobial Peptides, a Mini Review
Functional characterization of two defensin isoforms of the hard tick Ixodes ricinus
