Phototemtide A, a Cyclic Lipopeptide Heterologously Expressed from Photorhabdus temperata Meg1, Shows Selective Antiprotozoal Activity.

Lei Zhao,Marcel Kaiser,Tien Duy Vo,Helge B Bode

doi:10.1002/cbic.201900665

Abstract

A new cyclic lipopeptide, phototemtide A (1), was isolated from Escherichia coli expressing the biosynthetic gene cluster pttABC from Photorhabdus temperata Meg1. The structure of 1 was elucidated by HR‐ESI‐MS and NMR experiments. The absolute configurations of amino acids and 3‐hydroxyoctanoic acid in 1 were determined by using the advanced Marfey's method and comparison after total synthesis of 1, respectively. Additionally, three new minor derivatives, phototemtides B–D (2–4), were identified by detailed HPLC–MS analysis. Phototemtide A (1) showed weak antiprotozoal activity against Plasmodium falciparum, with an IC50 value of 9.8 μm. The biosynthesis of phototemtides A–D (1–4) was also proposed.

Highlights

A new cyclic lipopeptide, phototemtide A (1), was isolated from Escherichia coli expressing the biosynthetic gene cluster pttABC from Photorhabdus temperata Meg1
Cyclic lipopeptides (CLPs) are a class of structurally diverse natural products mainly produced by a wide variety of microorganisms, including cyanobacteria,[1] bacteria,[2] actinobacteria,[3] and fungi.[4]
During our further investigation on new natural products from Photorhabdus and Xenorhabdus strains, we found a new family of CLPs, named phototemtides (Scheme 1), after their biosynthetic gene cluster (BGC) pttABC from Photorhabdus temperata Meg1 was heterologously expressed in Escherichia coli

Summary

Introduction

A new cyclic lipopeptide, phototemtide A (1), was isolated from Escherichia coli expressing the biosynthetic gene cluster pttABC from Photorhabdus temperata Meg1. During our further investigation on new natural products from Photorhabdus and Xenorhabdus strains, we found a new family of CLPs, named phototemtides (Scheme 1), after their biosynthetic gene cluster (BGC) pttABC from Photorhabdus temperata Meg1 was heterologously expressed in Escherichia coli.

Results

Conclusion