Category: News

 

Albert J.R. Heck, Professor Biomolecular Mass Spectrometry and Proteomics at the Science Faculty of Utrecht University, has been elected EMBO member. In total 106 outstanding researchers in the life sciences were newly elected in this special year for EMBO on the occasion of its 50^th anniversary. The EMBO Membership currently comprises of more than 1600 life scientists.

“For the 50th anniversary of EMBO we are extremely pleased to welcome significantly more researchers to our membership than in previous years,” EMBO Director Maria Leptin said. “In the past decades, many of the concepts, techniques and insights of molecular biology have been applied to fundamental questions in other disciplines of the life sciences. Molecular explanations are now emerging for the origins and functions of complex systems like the brain and the living world around us. We wanted to reflect more of these exciting developments in our membership.”

EMBO Members make invaluable contributions to the organization by providing suggestions and feedback on the activities of EMBO. They serve on selection committees for EMBO programmes and mentor young scientists. Their input has helped to promote excellence in life sciences since 1964.

The other newly elected members from the Netherlands are:

• Ineke Braakman – Utrecht University
• Thijn Brummelkamp – Netherlands Cancer Institute
• Mike Jetten – Radboud University Nijmegen
• Rene Ketting – IMB Mainz, Germany

 

Dr Shabaz Mohammed (Oxford University and Biomolecular Mass Spectrometry and Proteomics Group of Utrecht University) has been awarded the Joseph Black Award 2014 by the Royal Society of Chemistry.

The Joseph Black Award is for a young scientist in any field covering the practice and teaching of analytical science and is sponsored by the Analytical Chemistry Trust Fund.

Previous winners are:

• 2013 – Dr Karen Faulds
• 2012 – Aaron Wheeler
• 2011 – Christy Haynes
• 2010 – Andre Simpson
• 2009 – Perdita Barran

AbLab provides state of the art Native MS services and is a service unit within the Heck lab. Due to this unique position AbLab has access to the latest insights, innovations, methodology and instrumentation for providing mass spectrometry services.

Native MS is emerging as a powerful technique for the characterization of antibodies, especially antibody mixtures, and in principle all therapeutic proteins. It provides the identity and accurate relative quantitative data of species in a mixture and complements, in many cases supersedes, conventional techniques such as cation exchange chromatography (CEX).

AbLab offers the following standardized services:

• Qualitative analysis
  Antibodies and half-bodies in a mixture are identified base on their (theoretical and experimental) mass, according to a standard and documented procedure. It provides the identity of each species by mass determination and  a graphical presentation of the spectrum.
• Semi-quantitative analysis
  Antibodies and half-bodies in a mixture are identified base on their (theoretical and experimental) mass and their relative abundance is determined according to a standard and documented procedure. It provides both the identity of each species in a mixture by mass determination, the relative abundance through comparison of relative ion signal intensities and  a graphical presentation of the spectrum. A semi-quantitative analysis is performed in triplicate.
• Services available in the near future
  Analysis of drug antibody ratios and analysis of antibody derived proteins.

We are able to offer this service and produce an analytical report within 5-10 business days.

For more information and the services please click here

Researchers of Utrecht University, Intravacc and the National Institute for Public Health and the Environment used a new method to identify hitherto unknown peptide antigens. This type of antigen had long been searched for, as they may be the starting points for new vaccines and cancer immunotherapy.  The results were published in Proceedings of the National Academy of Sciences (PNAS) on March 10, 2014.

“With this new method, we can identify more than twelve thousand peptide antigens, whereas before, we could only see the tip of the iceberg,” explains immunologist Dr Cécile van Els of the National Institute for Public Health and the Environment (RIVM). The new method, developed by the Biomolecular Mass Spectrometry and Proteomics group of Albert Heck, is not only much more sensitive, but also makes more routine research possible.

Complete picture
It is of vital importance for the development of vaccines and cancer immunotherapy to know which antigens alert the immune system. Up till now, it was not possible to get a complete picture of this process. In the best case, only a few hundreds of peptide antigens could be identified. But now, the researchers detecetd 12,000 of them, close to what is expected to be the maximum.

Cancer immunotherapy
The new method is also a very powerful technique for demonstrating the subtle differences between healthy cells and damaged cells, according to Geert Mommen of Intravacc. Of the twelve thousand peptide antigens, there are maybe a few dozen damaged ones that actually deviate from or are completely different from healthy cells. Researchers have found more proof that these deviating or unique peptide antigens are best equipped to prepare our immune system for the fight against cancer.

“Currently, a lot of research is being conducted into cancer immunotherapy,” adds Heck. “Science has even called this the break-through of the year 2013, but in actual fact, the therapy is still in its infancy. The good thing about immunotherapy is that it does not destroy or damage healthy cells. With our new method, researchers will obtain significantly more information about our immune system. We hope that this information will help them with the further development of cancer treatment.”

Read the full article:
Expanding the detectable HLA peptide repertoire using electron-transfer/higher-energy collision dissociation (EThcD)

Geert P. M. Mommen, Christian K. Frese, Hugo D. Meiring, Jacqueline van Gaans-van den Brink, Ad P. J. M. de Jong, Cécile A. C. M. van Els, Albert J. R. Heck
PNAS, Monday 10 March, doi 10.1073

This research is co-funded by the Netherlands Proteomics Centre (NPC), which performs high-quality research and transfer of knowledge in proteomics. The RIVM was part of this project as strategic research partner.

On Saturday March 15th the Dutch newspaper NRC Handelsblad published an article on the Science publication Complement Is Activated by IgG Hexamers Assembled at the Cell Surface. Prof. Albert Heck and PhD student Sara Rosati contributed to this Science publication.

Check it out!

 

 

Almost all living things have adapted to earth’s day and night rhythm by keeping time with a biological clock. The biological clock of cyanobacteria, known as the Kai system, is one of the simplest known to date, and is therefore intensively studied by theoretical biologists and systems biologists in the hope to learn about biological time keeping. The Kai system is so robust, that it can even be reconstituted in the lab, simply by mixing the three Kai proteins (KaiA, KaiB and KaiC) in a test-tube. This test-tube oscillator still produces the same 24 hour rhythm that it does in the context of a living cell, and it can do so for weeks on end. The three Kai proteins interact with each other to produce these 24 hour rhythms, forming large protein complexes whose structure and composition changes depending on the time of day. The interactions between KaiC and KaiB marks a defining moment in the 24 hour cycle of the clock, but structural details of this interaction have not been well understood.

In the Proceedings of the National Academy of Sciences USA, Joost Snijder, Rebecca Burnley and Albert Heck, from the Biomolecular Mass Spectrometry and Proteomics Group (Utrecht University), have used structural mass spectrometry (native MS, ion mobility MS and HDX-MS) to shed light on the interaction between KaiB and KaiC. Their experiments revealed the composition of the KaiC-KaiB complex and showed which regions of the proteins are important for their interaction. Understanding these aspects of the KaiB-KaiC interaction explains many of the known features of the biological clock and helps us understand how such a simple system by biological standards is able to constitute a complex time keeping device in cyanobacteria.

The work was performed in collaboration with the groups of Alexandre Bonvin (Computational Structural Biology, Bijvoet Centre, Utrecht University) and Ilka Axmann (Institute for Theoretical Biology, Universitätsmedizin Berlin)

Link to the full article:

http://www.pnas.org/content/111/4/1379.long

As of January 2014 Simone Lemeer started as Assistant Professor at the at the Biomolecular Mass Spectrometry and Proteomics group (Utrecht University). Before joining the group, Simone was group leader Mass Spectrometry at the Technical University of Munich in Germany.

Her future work will focus on the elucidation of the mechanisms of action of small molecule inhibitors in cancer cells, as well as identification of the intrinsic resistance mechanisms that are present in those cells. Constitutive acitivity of kinases is known to be crucial for a tumor to maintain its malignant phenotype. Small molecule inhibitors are therefore attractive therapeutics as they target these kinases that are critical for tumor cell survival and proliferation. Several small molecule inhibitors have been proven successful in the clinic, but despite initial success most cancers eventually develop resistance against these drugs. Resistance to the drugs, both intrinsic and acquired is a major problem and is believed to be the major cause of failure of drug treatment. Simone will use state state of the art, high sensitive, chemical proteomics and phosphoproteomics technology to study the dynamic changes of the kinome and phosphoproteome in response to small molecule inhibitor treatment, revealing mechanisms of action and resistance pathways in cancer cells in response to drug treatment.