Detail Structure of the Immature Dengue Virus at Low pH Primes Proteolytic Maturation   Oleh:  I-Mei, Yu ; Wei, Zhang ; Holdaway, Heather A. ; Long, Li Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 319 no. 5871 (Mar. 2008), page 1834-1837. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2008.03 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel Intracellular cleavage of immature flaviviruses is a critical step in assembly that generates the membrane fusion potential of the E glycoprotein. With cryo–electron microscopy we show that the immature dengue particles undergo a reversible conformational change at low pH that renders them accessible to furin cleavage. At a pH of 6.0, the E proteins are arranged in a herringbone pattern with the pr peptides docked onto the fusion loops, a configuration similar to that of the mature virion. After cleavage, the dissociation of pr is pH-dependent, suggesting that in the acidic environment of the trans-Golgi network pr is retained on the virion to prevent membrane fusion. These results suggest a mechanism by which flaviviruses are processed and stabilized in the host cell secretory pathway. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

Copyright © 2006, 2007 Unika Atma Jaya, all rights reserved