Abstract
To combat nutritional immunity, N. gonorrhoeae has evolved systems to hijack zinc and other metals directly from host metal-binding proteins such as calprotectin (CP). Here, we report the 6.1 Å cryoEM structure of the gonococcal surface receptor TdfH in complex with a zinc-bound CP tetramer. We further show that TdfH can also interact with CP in the presence of copper and manganese, but not with cobalt.
Highlights
To combat nutritional immunity, N. gonorrhoeae has evolved systems to hijack zinc and other metals directly from host metal-binding proteins such as calprotectin (CP)
Neisseria gonorrhoeae causes the sexually transmitted infection gonorrhea, which can lead to more serious conditions including bacteremia, increased risk of HIV/ AIDS, and infertility[1,2]
No binding was observed with just calcium or zinc alone, or in the presence of ethylenediaminetetraacetic acid (EDTA) (Fig. 1b; lanes 9–11)
Summary
N. gonorrhoeae has evolved systems to hijack zinc and other metals directly from host metal-binding proteins such as calprotectin (CP). TdfH was bound to Streptavidin MagneSphere Paramagnetic Particles and assayed for binding under various CP buffer conditions. Experiments reported here demonstrate that both calcium and zinc are required for the stable interaction between CP and TdfH and that the order of calcium or zinc addition to CP has no effect on the complex formation (Fig. 1b; lanes 12–14).
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
