Mechanistic insights into staphylopine-mediated metal acquisition

Research Highlight

The metal uptake mechanism that keeps bacteria harmful

© Callista Images/Cultura/Getty

© Callista Images/Cultura/Getty

Researchers in China have uncovered the structural details of a protein necessary to sustain bacterial virulence. 

Living organisms need transition metals, like nickel, iron, and zinc, for their biological processes. During an infection, some bacteria produce a molecule, called staphylopine, which competes with human cells to bind to these metals. Another protein, called CntA, recognizes the staphylopine-metal complex and initiates its transportation across the bacterial membrane. The molecular mechanisms of this process have been unclear. 

A ShanghaiTech University-led team crystallized CntA to study its structure and conducted experiments to understand its interaction with complexes formed between staphylopine and the metals cobalt, nickel and zinc. They also induced mutations to uncover the roles played by distinct parts of CntA in its overall function.

The investigations clarified the protein’s sophisticated recognition mechanism. Binding of the staphylopine-metal complex to CntA changed its shape, initiating metal transportation across the bacterial membrane. Targeting this mechanism could be a potent antibacterial strategy.

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  1. PNAS 115, 3942–3947 (2018). doi: 10.1073/pnas.1718382115
Institutions FC
School of Physical Science and Technology, ShanghaiTech, China 0.83
School of Chemistry and Chemical Engineering (SCCE), SJTU, China 0.17

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