Hernandez L D, Hoffman L R, Wolfsberg T G, White J M
Department of Cell Biology, University of Virginia, Charlottesville 22908, USA.
Annu Rev Cell Dev Biol. 1996;12:627-61. doi: 10.1146/annurev.cellbio.12.1.627.
Significant progress has been made in elucidating the mechanisms of viral membrane fusion proteins; both those that function at low, as well as those that function at neutral, pH. For many viral fusion proteins evidence now suggests that a triggered conformational change that exposes a previously cryptic fusion peptide, along with a rearrangement of the fusion protein oligomer, allows the fusion peptide to gain access to the target bilayer and thus initiate the fusion reaction. Although the topologically equivalent process of cell-cell fusion is less well understood, several cell surface proteins, including members of the newly described ADAM gene family, have emerged as candidate adhesion/fusion proteins.
在阐明病毒膜融合蛋白的机制方面已取得重大进展；无论是在低pH值下起作用的，还是在中性pH值下起作用的。现在有证据表明，对于许多病毒融合蛋白来说，一种引发的构象变化会暴露出先前隐藏的融合肽，同时融合蛋白寡聚体发生重排，使融合肽能够接触到靶膜双层，从而启动融合反应。尽管细胞-细胞融合在拓扑学上等效的过程了解较少，但几种细胞表面蛋白，包括新描述的ADAM基因家族的成员，已成为候选的粘附/融合蛋白。
