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 Series 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.

Read the full paper
CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.
Nature Communications 11, 5080 (2020). doi:
Weaver SJ, Ortega DR, Sazinsky MH, Dalia TN, Dalia AB, Jensen GJ

Commentary by Andrew Webb, PhD.

About the author
Andrew has over 15 years’ experience in the field of chromatography and mass spectrometry. He is the lead innovator and inventor at IonOpticks, working closely with the team to test, refine and develop cutting edge techniques to support higher quality outputs and analytics from MS instruments. Andrew is also the Lab Head of the Walter and Eliza Hall Institute of Medical Research’s Proteomics Research Laboratory.