Structure of S. agalactiae toxin identified
JIN Tengchuan
By utilizing X-ray diffraction technique, researchers reported the structural fold of S. agalactiae CAMP factor is composed of 5+3 helix bundles, where the N-terminal 5 helix bundle is believed to be responsible for membrane permeabilization and the C-terminal 3 helix bundle is likely responsible for host receptor binding. Besides, the C-terminal domain is revealed to inhibit the activity of both full-length toxin and its N-terminal domain.
The researchers also observed that the linker region has a conserved DLxxxDxAT sequence motif, which is required for CAMP factor's co-hemolytic activity. The results helped clarify the molecular mechanism of S. agalactiae's co-hemolytic activity.
What the researchers illustrated may assist in the screening of anti-CAMP virulent factor drugs and inspire more to reveal the nature of the interaction between proteins and biofilms.
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