Kilejian A, Rashid M A, Aikawa M, Aji T, Yang Y F
Public Health Research Institute, New York, NY 10016.
Mol Biochem Parasitol. 1991 Feb;44(2):175-81. doi: 10.1016/0166-6851(91)90003-o.
The knob protein of Plasmodium falciparum is essential for the formation of knob-like protrusions on the host erythrocyte membrane. A functional domain of the knob protein was identified. This peptide formed stable complexes with the two major red cell skeletal proteins, spectrin and actin. When introduced into resealed normal erythrocytes, the peptide associated selectively with the cytoplasmic surface of the membrane and formed knob-like electron dense deposits. Knobs are thought to play an important role in the immunopathology of P. falciparum infections. Our findings provide a first step towards understanding the molecular basis for selective membrane changes at knobs.
恶性疟原虫的结节蛋白对于在宿主红细胞膜上形成结节样突起至关重要。已鉴定出结节蛋白的一个功能域。该肽与两种主要的红细胞骨架蛋白血影蛋白和肌动蛋白形成稳定的复合物。当将该肽引入重新封闭的正常红细胞时，它选择性地与膜的细胞质表面结合并形成结节样电子致密沉积物。结节被认为在恶性疟原虫感染的免疫病理学中起重要作用。我们的发现为理解结节处选择性膜变化的分子基础迈出了第一步。
