Biomolecular NMR Research
Jordan Chill

The pathogenic bacterium Bordetella pertussis, the cause of whooping cough, delivers the effector protein BteA into host cells during infection. In collaboration with Dr. Raz Zarivach, Life Sciences, BGU, we have characterized the helical N-terminal domain of BteA and studied the molecular basis of the interaction with its cognate chaperone BtcA as well as its binding of phosphatidylinositol headgroups in the host membrane. By following changes in the NMR fingerprint spectrum of BteA131 we have identified the protein surfaces utilized for each of these interactions and gained insight into how the effector progresses along the type-III secretion system pathway en route to host infection.  

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Publications:

Guttman, C.; Davidov, G.; Shaked, H.; Ganguly, A.; Miller, J.F.; Chill, J.H.*.; Zarivach, R.* Characterization of the N-terminal domain of BteA: a Bordatella Type III secreted cytotoxic effector. PLoS One, 2013, 8(1):e55650. (*Corresponding authors).

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Guttman, C.; Davidov, G.; Yahalom, A.; Shaked, H.; Kolusheva, S.; Bitton, R.; Chill, J.H.*; Zarivach, R.* BtcA, a class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism. PLoS One, 2013, 8(12), e81557. (*Corresponding authors)

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Yahalom, A.; Davidov, G.; Kolusheva, S.; Shaked, H.; Barber-Zucker, S.; Zarivach, R.† Chill, J.H.† Structure and membrane-targeting of a Bordetella pertussis effector N-terminal domain. BBA-Biomembranes, 2019, 1861(12):183054 (†Co-corresponding author).