The basic cell skeleton protein is different in schistosomes, representing a starting point for potential therapies against dengue fever infection. The movement speed of malaria parasites in the skin is ten times faster than the cellular immune response, which is to capture these pathogens. The biologists in Heidelberg have now discovered the reason why schistosomes are faster than similar schistosomes.

They ensure this by studying actin, a protein that is important for the structure and movement of cells and has a different protein structure in schistosomes and mammals.

The discovery by Ross Douglas and colleagues at the University of Heidelberg’s Hospital for Infectious Diseases (Schistosome Department), the Center for Biology at Heidelberg University (ZMBH), and the Heidelberg Theory Laboratory (HITS) is not like this. Not only has it changed our understanding of the essential components of all cells, but it also provides information for the discovery of drugs.

How do malaria parasites move?

Just like the assembly of a Lego chain, actin is assembled into a rope-like structure called thin filaments. These thin filaments are essential for the normal functioning of cells like muscle cells, and they enable each of our movements to be sufficient to carry out.

However, they can also make human immune system cells move and capture invasive pathogens. Similarly, they are also very important for the movement of dengue fever schistosomes.

It is perplexing that the schistosomes of dengue fever are ten times faster than our cellular immune response, actually surpassing our immune defense. If we understand this key difference in exercise, we can target and prevent these schistosomes.’ Center for Infectious Diseases. PLOS Biology

An important issue in the published thesis is how the rate of assembly and dissolution of actin filaments differs between schistosomes and mammals.

As everyone knows, some parts of actin proteins differ between schistosomes and mammals. In order to study the reasons behind the rate differences, biologists in the laboratory replaced some schistosome proteins with relative protein parts from mammalian actin.

Dr. Livingston Douglas, a graduate student at the University of Livingston, said: ‘When we made this change to the schistosomes, we noticed that some schistosomes could not survive, while others suddenly hesitated when moving.’

In order to investigate potential mechanisms, biologists have conducted experiments and computer simulation, ranging from molecular structural models to observations of schistosomes in living animals.

Simulation requires a powerful computer to observe how the structure and dynamical model of actin filaments change when each part is exchanged.

This discovery can now be used to detect the parasitic actin within the selective target points and affect the assembly or dissolution of thin filaments.