Fachbereich Veterinärmedizin

Service-Navigation

Feedback | Startseite
Fachbereich Veterinärmedizin/

Veterinärmedizinische Bibliothek

Mikronavigation

    Publikationsdatenbank

    Beta-tubulin complementary DNA sequence variations observed between cyathostomins from benzimidazole-susceptible and -resistant populations (2004)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Drogemuller, M
    Schnieder, T
    von Samson-Himmelstjerna, G (WE 13)
    Quelle
    Journal of parasitology : the journal of the American Society of Parasitologists; 90(4) — S. 868–870
    ISSN: 0022-3395
    Sprache
    Englisch
    Verweise
    Pubmed: 15357086
    Kontakt
    Institut für Parasitologie und Tropenveterinärmedizin

    Robert-von-Ostertag-Str. 7-13
    Gebäude 35, 22, 23
    14163 Berlin
    +49 30 838 62310
    parasitologie@vetmed.fu-berlin.de

    Abstract / Zusammenfassung

    The molecular mechanism of benzimidazole (BZ) resistance in cyathostomins of horses is still unclear. Previous studies revealed that the TTC or TAC polymorphism in codon 200 of the beta-tubulin isotype 1 gene is not as strictly correlated with BZ resistance as in trichostrongyles in sheep. To identify further sites of polymorphism within the beta-tubulin gene related to BZ resistance, complete complementary DNAs (cDNAs) encoding beta-tubulin of adult worms of Cylicocyclus nassatus, Cyathostomum pateratum, Cyathostomum coronatum, Cyathostomum catinatum, Cylicostephanus longibursatus, and Cylicostephanus goldi of a BZ-resistant cyathostomin population were characterized using specific primers. The cDNA sequence of each species spans 1,429 bp, encoding a protein of 448 amino acids. The interspecific identities are 95.2-99.6% at the nucleotide and 98.7-100.0% at the peptide level. The comparison of the amino acid sequences of individuals isolated from the BZ-resistant cyathostomin population with those from individuals of Cc. nassatus, Cy. coronatum, Cy. pateratum, and Cy. catinatum of a BZ-susceptible one showed differing amino acids in 11 positions. The commonness of a phenylalanine to tyrosine mutation at position 167 in all the 6 cyathostomin species isolated from a BZ-resistant population suggests its involvement in the molecular mechanism in BZ resistance.