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metadata.dc.type: Artigo de Periódico
Issue Date: 2004
metadata.dc.creator: SCHNEIDER, Igor
SCHNEIDER, Maria Paula Cruz
SILVA, Artur Luiz da Costa da
Title: The prion protein and New World primate phylogeny
Citation: SCHNEIDER, Igor et al. The prion protein and New World primate phylogeny. Genetics and Molecular Biology, São Paulo, v. 27, n. 4, p. 505-510, 2004. Disponível em: <>. Acesso em: 10 maio 2011. <>.
Abstract: The PrPC prion protein contains 250 amino acids with some variation among species and is expressed in several cell types. PrPC is converted to PrPSc by a post-translational process in which it acquires amino acid sequences of three-dimensional conformation of -sheets. Variations in the prion protein gene were observed among 16 genera of New World primates (Platyrrhini), and resulted in amino acid substitutions when compared with the human sequence. Seven substitutions not yet described in the literature were found: W  R at position 31 in Cebuella, T  A at position 95 in Cacajao and Chiropotes, N S at position 100 in Brachyteles, L  Q at position 130 in Leontopithecus (in the sequence responsible for generating the -sheet 1), D  E at position 144 in Lagothrix (in the sequence responsible for the -helix 1), D G at position 147 in Saguinus (also located in the -helix 1 region), and M  I at position 232 in Alouatta. The phylogenetic trees generated by parsimony, neighbor-joining and Bayesian analyses strongly support the monophyletic status of the platyrrhines, but did not resolve relationships among families. However, the results do corroborate previous findings, which indicate that the three platyrrhine families radiated rapidly from an ancient split.
Keywords: Filogenia molecular
Proteína prion
ISSN: 1415-4757
metadata.dc.rights: Acesso Aberto
Appears in Collections:Artigos Científicos - ICB

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