• Andrew Webb

Caught in the act: new CryoEM protein structure reveals the potential to drug antibiotic resistance

How bacteria resistance can be spread between species of bacteria is understood to occur via a couple mechanisms. One of these such mechanisms involves cell surface proteins that can bind and transport exogenous DNA through the outer membrane. Future drugs developed to block this process could be incredibly important as combined therapies in preventing the development and spread of resistance during treatment with antibiotics, which is one of the major global medical health challenges we face.

Here Weaver et al, solve the structure of VcPilQ purified from native V. cholerae cells using cryoEM and IonOpticks Aurora columns to confirm its sequence. In solving the structure of a natively purified complex, their work suggests that these proteins may be amenable as druggable targets and provide new insights into how DNA transfer may promote antibiotic resistance.

CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae. Nature Communications 11, 5080 (2020).


Weaver SJ, Ortega DR, Sazinsky MH, Dalia TN, Dalia AB, Jensen GJ