亨德拉病毒融合蛋白的N-连接糖基化作用
Role of N-linked glycosylation of the Hendra virus fusion protein.
作者信息
Carter James Richard, Pager Cara Theresia, Fowler Stephen Derrick, Dutch Rebecca Ellis
机构信息
Department of Molecular and Cellular Biochemistry University of Kentucky, 800 Rose Street, UKMC MN606 Lexington, KY 40536-0298, USA.
出版信息
J Virol. 2005 Jun;79(12):7922-5. doi: 10.1128/JVI.79.12.7922-7925.2005.
Abstract
The Hendra virus fusion (F) protein contains five potential sites for N-linked glycosylation in the ectodomain. Examination of F protein mutants with single asparagine-to-alanine mutations indicated that two sites in the F(2) subunit (N67 and N99) and two sites in the F(1) subunit (N414 and N464) normally undergo N-linked glycosylation. While N-linked modification at N414 is critical for protein folding and transport, F proteins lacking carbohydrates at N67, N99, or N464 remained fusogenically active. As N464 lies within heptad repeat B, these results contrast with those seen for several paramyxovirus F proteins.
摘要
亨德拉病毒融合（F）蛋白的胞外区域含有5个潜在的N-糖基化位点。对具有单个天冬酰胺到丙氨酸突变的F蛋白突变体进行检测表明，F(2)亚基中的两个位点（N67和N99）以及F(1)亚基中的两个位点（N414和N464）通常会发生N-糖基化。虽然N414位点的N-连接修饰对于蛋白质折叠和转运至关重要，但在N67、N99或N464处缺乏碳水化合物的F蛋白仍具有融合活性。由于N464位于七肽重复序列B内，这些结果与几种副粘病毒F蛋白的情况形成对比。
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