Research

Scientists from the IQFR, the Norwegian University of Life Sciences and the Univ. Of Bloomington Indiana have characterized the structure of the extracellular domain of FtsX, an essential protein in the bacterial division.

Structure of the large extracellular loop of FtsX and its interaction with the essential peptidoglycan hydrolase PcsB in Streptococcus pneumoniae

Streptococcus pneumoniae is a leading killer of children and immunocompromised individuals. S. pneumoniae has become increasingly resistant to major antibiotics, and therefore the development of new antibiotic strategies is desperately needed. Targeting bacterial cell division is one such strategy, specifically targeting essential proteins for the synthesis and breakdown of peptidoglycan. Across multiple species of bacteria, the protein FtsX is a cell division protein involved in the regulation of peptidoglycan hydrolases. FtsX represents a large group of ABC-transporter like proteins that function as ‘mechanotransmitters’, proteins that relay signals from inside the cell to the outside. In a collaborative international (Spain, Norway and USA) effort leaded by IQFR and University Indiana Bloomington we present the first structural characterization of the large extracellular loop of FtsX from the human opportunistic pathogen Streptococcus pneumoniae. We show the direct interaction between the peptidoglycan hydrolase PcsB and FtsX, and that this interaction is essential for cell viability. As such, FtsX represents an attractive, conserved target for the development of new classes of antibiotics.

Reference:

Britta E. Rued, Martín Alcorlo, Katherine A. Edmonds, Siseth Martínez-Caballero, Daniel Straume, Yue Fu, Kevin E. Bruce, Hongwei Wu, Leiv Sigve Håvarstein, Juan A. Hermoso*, Malcolm E. Winkler* and David P. Giedroc*. Structure of the large extracellular loop of FtsX and its interaction with the essential peptidoglycan hydrolase PcsB in Streptococcus pneumoniae.

MBio(2019) DOI: 10.1128/mBio.02622-18

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