Your browser doesn't support javascript.
loading
Structural analysis reveals an amyloid form of the human papillomavirus type 16 E1--E4 protein and provides a molecular basis for its accumulation.
McIntosh, Pauline B; Martin, Stephen R; Jackson, Deborah J; Khan, Jameela; Isaacson, Erin R; Calder, Lesley; Raj, Kenneth; Griffin, Heather M; Wang, Qian; Laskey, Peter; Eccleston, John F; Doorbar, John.
Afiliação
  • McIntosh PB; Division of Virology, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom.
J Virol ; 82(16): 8196-203, 2008 Aug.
Article em En | MEDLINE | ID: mdl-18562538
The abundant human papillomavirus (HPV) type 16 E4 protein exists as two distinct structural forms in differentiating epithelial cells. Monomeric full-length 16E1--E4 contains a limited tertiary fold constrained by the N and C termini. N-terminal deletions facilitate the assembly of E1--E4 into amyloid-like fibrils, which bind to thioflavin T. The C-terminal region is highly amyloidogenic, and its deletion abolishes amyloid staining and prevents E1--E4 accumulation. Amyloid-imaging probes can detect 16E1--E4 in biopsy material, as well as 18E1--E4 and 33E1--E4 in monolayer cells, indicating structural conservation. Our results suggest a role for fibril formation in facilitating the accumulation of E1--E4 during HPV infection.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Papillomavirus Humano 16 Idioma: En Ano de publicação: 2008 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Papillomavirus Humano 16 Idioma: En Ano de publicação: 2008 Tipo de documento: Article