By comparing the structures of the extended and contracted states, the researchers were able to model how the T6SS works in detail. “During the sheath contraction, ring after ring turns and gets closer to the previous ring, while the ring diameter expands and thus releases the spear,” explains Basler. “This combination of sheath shrinking and turning results in drilling a hole into the target cells. Within less than two milliseconds, the T6SS sheath contracts to half of its length and at the same time the toxic spear spirals out like a screw. Therefore, the bacteria have an extremely powerful drill.”

Only contracted T6SS sheaths are disassembled

Furthermore, the researchers also addressed another question. After firing T6SS, bacteria re-use the individual components of the sheath to assemble a new speargun. “For a long time, it was not clear why only the contracted, but not the extended sheath is disassembled,” says Basler. “Now, we could see that a certain protein domain is exposed on the surface of the sheath during contraction and can be recognized by a specific protein responsible for dismantling the sheath. In the extended sheath state, this domain is hidden and the T6SS sheath is therefore protected from disassembly.”

The bacterial speargun will continue to be the subject of future research. “One of our projects is dedicated to the question of how the T6SS is embedded in the bacterial cell envelope. As the speargun is fired with such a high force, it must be firmly anchored, otherwise firing would not work properly or could be also fatal for the weapon-carrying bacteria themselves.”