Looking at proteins from different angles: The unusual behavior of phospholipase PlaB from Legionella pneumophila


Legionella pneumophila, the causative agent of Legionnaires’ Disease, uses contaminated freshwater to trigger potentially fatal pneumonia. It enters lung macrophages and establishes itself in a protected niche by secreting a plethora of proteins into the host cell. Among these factors is a significant number of phospholipases that damage host cell membranes, manipulate signal transduction by interfering with second messengers and provide nutrients to the bacterium. One of these phospholipases is PlaB, a PLA2-type phospholipase that inserts into the outer membrane of L. pneumophila after being secreted via an unknown pathway. Interestingly, PlaB shows lowest specific activity at high protein concentrations, which is the consequence of tetramer formation and may represent a means of self-protection that prevents harmful activity while PlaB is synthesized within the L. pneumophila cell.

A surprising mechanism that controls the tetramerization of PlaB was discovered by employing different analytical methods, including SEC-MALS and protein crystallography in prominent roles. These findings demonstrate the synergy of looking at proteins from different angles.

When: Tuesday, Feb. 22nd
Time: 10-11 AM CET
Register at the link below at no cost.

Key learning objectives:
  • Understanding the pathomechanism of Legionella pneumophila
  • Analysis of protein oligomerization using biophysical means and protein crystallography
  • How the oligomeric state and absolute molar mass of proteins can be assessed by SEC-MALS
Who should attend:
  • Structural Biologists and Biochemists who want to understand protein behavior better
  • Researchers working with purified recombinant proteins
  • Managers of academic labs and protein production/characterization core facilities who want to broaden the analytical methodology

Pricing: Registration is FREE.



Presented by: Prof. Wulf Blankenfeldt, Helmholtz-Zentrum für Infektionsforschung
Prof. Blankenfeldt studied chemistry at the Technische Universität Braunschweig (Germany) and the National Taiwan Normal University (Republic of China). After a doctorate in structural biology and a postdoctoral stay at the University of St. Andrews (United Kingdom), he started his own research group at the Max Planck Institute of Molecular Physiology in Dortmund (Germany). He served as an associate professor of biochemistry at the University of Bayreuth (Germany) before returning to Braunschweig as a head of department at the Helmholtz Centre for Infection Research. At the same time, he is a full professor at the Technische Universität Braunschweig.