NR AWQB
AU Vitale,M.; Vitale,F.; Glorioso,N.S.; D'Andrea,A.; Rea,S.; Reale,S.; Caracappa,S.
TI Sequence analysis of prion gene in Sicilian autochthon bovine breeds
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions GEN-30
PT Konferenz-Poster
AB A project for a characterization and biodiversity conservation on Sicilian autochthon breeds of different animal species had been started which includes two bovine breeds of Sicily: Modicana and Cinisara. The two bovine breeds are particularly adapted to climatic and geographic environment of the island and are particularly good milk producers. Cinisara is a breed confined essentially in the province of Palermo and produces a milk with high percentage of fat and protein; Modicana cows are present not only in all Sicilian territory but also In Abruzzo region. With the aim of polymorphism analysis at nucleotide and aminoacids levels a sequencing studies on prion gene (Prnp) had been started on group of animals of this two breeds coming from different herds in comparison with bovine of different not pure breeds present also in Sicilian territory, but coming from different geographical area such as Italian Red Spotted. A Charolais cow and an African cow had also been included in the studies. Blood samples in EDTA had been taken from the animals. DNA had been extracted by magnetic particle purification (King Fisher system). Genomic region corresponding to different part of the gene and to the coding sequence had been amplified and purified by agarose gel with the DNA gel extraction Kit (Genomics Millipore) following manufacture's instructions. Sequencing had been performed by the Kit BigDye Terminator v1.1 Cycle Sequencing and by ABI prism 310 genetic analyzer (Applied Biosystem). Comparison analysis on coding sequence showed that Modicana breed as all other cows have few conservative aminoacids replacements. Interestingly Cinisara breed is the only one that, on the contrary, showed a replacement involving the substitution of a Serine (aromates) in Asparagin (large polar) residue. The asparagin residues in the Prion protein can be glycosylated and so this can be a potential new site for glycosilation. Considering the importance that glycosilation pattern has in distinguishing different prion strains and its role in the susceptibility of cellular PrP (PrPc) to conversion to the disease-associated conformation, PrPsc further studies will be performed by western blot analysis to evaluate if glycosylation pattern in Cinisara cows are different compare to the other bovine breeds.
AD M. Vitale, F. Vitale, A. D'Andrea, S. Rea, S. Reale, S. Caracappa: Area Biologia Molecolare, Istituto Zooprofilattico Sperimentale della Sicilia "A. Mirri", Palermo, Italy; N.S. Glorioso: 1Servizio Veterinario A.S.L. 6 Palermo, Italy. E-mail: mvitale@pa.izs.it
SP englisch
PO Italien