Integrative Parasitology, Center for Infectious Diseases, University of Heidelberg Medical School , Im Neuenheimer Feld 324, 69120 Heidelberg, Germany.
University of Heidelberg , Department of Biophysical Chemistry and Max Planck Institute for Intelligent Systems, Department of New Materials and Biosystems, Heisenbergstr. 3, 70569 Stuttgart, Germany.
ACS Nano. 2016 Feb 23;10(2):2091-102. doi: 10.1021/acsnano.5b06417. Epub 2016 Jan 27.
Migration of malaria parasites is powered by a myosin motor that moves actin filaments, which in turn link to adhesive proteins spanning the plasma membrane. The retrograde flow of these adhesins appears to be coupled to forward locomotion. However, the contact dynamics between the parasite and the substrate as well as the generation of forces are complex and their relation to retrograde flow is unclear. Using optical tweezers we found retrograde flow rates up to 15 μm/s contrasting with parasite average speeds of 1-2 μm/s. We found that a surface protein, TLP, functions in reducing retrograde flow for the buildup of adhesive force and that actin dynamics appear optimized for the generation of force but not for maximizing the speed of retrograde flow. These data uncover that TLP acts by modulating actin dynamics or actin filament organization and couples retrograde flow to force production in malaria parasites.
疟原虫的迁移是由一种肌球蛋白马达驱动的,该马达带动肌动蛋白丝运动,而肌动蛋白丝又与横跨质膜的黏附蛋白相连。这些黏附蛋白的逆行流动似乎与向前运动相耦合。然而,寄生虫与基质之间的接触动力学以及力的产生是复杂的,它们与逆行流动的关系尚不清楚。我们使用光学镊子发现,逆行流动速度高达 15 μm/s,而寄生虫的平均速度为 1-2 μm/s。我们发现一种表面蛋白 TLP 通过减少逆行流动来增强黏附力,并且肌动蛋白动力学似乎优化了力的产生,但不是最大程度地提高逆行流动速度。这些数据表明,TLP 通过调节肌动蛋白动力学或肌动蛋白丝组织来发挥作用,并将逆行流动与疟原虫的力产生相耦合。