PeerJ Award Winner: 4th European Conference on Natural Products

by | Sep 22, 2021 | Award Winner Interviews, Awards, Community, Conferences

The 4th European Conference on Natural Products (ECNP) was held virtually between the 6th and the 8th of September 2021. The conference features recent advances from all fields in secondary metabolite research: biosynthesis, synthetic biology, organic syntheses, targets and MoA/ chemical biology, chemical communication, and the advanced methods in NP discovery and characterization.

Jacqueline Luque-Hornero (organiser): At the 4th European Conference on Natural Products a large number of scientific posters and exciting talks presented the latest advances in secondary metabolite research with a special focus on networking opportunities and the interaction of academic and industrial research.

PeerJ sponsored an award for the Best Poster presented by an Early Career Researcher, which was won by Hui Tao from the University of Tokyo.

If you are organising a conference and would like to consider a PeerJ Award, please get in contact via communities@peerj.com

 

*****

Hui Tao Post doctoral researcher at the University of Tokyo. 

Can you tell us a bit about yourself and your research interests?

I obtained my Ph.D under the supervision of Profs. Zixin Deng and Tiangang Liu at Wuhan University in China. I was working on metabolic engineering of microbes to produce fine chemicals and biofues. After graduation,  I joined in Prof. Abe’s group as a JSPS fellow, and now my research is focused on natural products biosynthesis.

 

What first interested you in this field of research?

I’m pretty interested in research to uncover the biosynthesis of natural products, especially for polyketide and terpenoids. Whilst in Prof. Abe’s lab, I’m also working on structural based enzyme mechanism studies, including 2OG-dependent oxygenase and terpene synthase.

 

You won the Best ECR Poster award at ECNP 2021, can you explain the research you presented?

This work is a collaboration with Prof. Yudai Matsuda from the City University of Hong Kong, China. Calbistrins are fungal metabolites originally isolated from Penicillium restrictum and reportedly exhibit antifungal activity. Calbistrins feature the decalin and polyene portions and is seemingly biosynthesized by the fusion of two distinct polyketide products, as seen in the biosynthesis of lovastatin. Intriguingly, the cal cluster encodes only one PKS, despite the apparent requirement of two PKSs to afford the two distinct polyketide moieties.  In this study, we investigated the mechanism by which the backbone structures of calbistrins are formed, by heterologous and in vitro reconstitution of the biosynthesis and a structural biological study. Intriguingly, our analyses revealed that the decalin and polyene portions of calbistrins are synthesized by the single polyketide synthase (PKS) CalA, with the aid of the trans-acting enoylreductase CalK and the trans-acting C-methyltransferase CalH, respectively. We also determined that the esterification of the two polyketide parts is catalyzed by the acyltransferase CalD. Our study has uncovered a novel dual-functional PKS and thus broadened our understanding of how fungi synthesize diverse polyketide natural products.

How did you find the virtual conference experience?

It’s much better than I expected, and I really enjoyed this conference.

What are your next steps?

The next step could be investigating the mechanism about how the PKS interact with two trans-acting enyzmes.

 

 

Get PeerJ Article Alerts