A community-wide effort to formulate recommendations and guidelines for HDX-MS experiments was published in Nature Methods. The paper offers detailed recommendations on experiment design and reporting of HDX-MS experiments.
The Veesler lab at University of Washington published a new study in Cell revealing the mechanism of neutralization of two antibodies against SARS and MERS coronavirus spikes.
The team used cryo electron microscopy and mass spectrometry to study the antibodies in complex with spike proteins at near-atomic resolution and profile the composition of the viral glycan shields. The reconstructions revealed that the antibodies interact with the receptor binding domains of the spike proteins. The antibody that targets the SARS spike protein functionally mimics receptor binding by triggering a premature transition to the post-fusion conformation.
Glycoproteomics experiments revealed a very complex and heterogeneous pattern of glycosylation of the viral spikes. Some glycans are in direct contact with the neutralizing antibodies. Such a high degree of variability in glycosylation is thought to complicate antigen recognition by the host immune system.
In February of 2019 Joost Snijder will start his own research group in the Hecklab at Utrecht University. His appointment is part of the Institute for Chemical Immunology. His work will focus on glycosylation of viral antigens and its role in antibody interactions, as well as the development of new mass spectrometry based antibody sequencing tools.
The Veesler lab at University of Washington published a study in eLife describing how N-linked glycans of HIV Envelope spikes interact with a broadly neutralizing antibody.
Using a combination of cryo electron microscopy and mass spectrometry, it was shown that glycans in and around the CD4 receptor binding site modulate interactions with the germline precursor to a class of broadly neutralizing antibodies. It was demonstrated that the VRC01 germline precursor can accommodate glycans in the epitope, even though it binds stronger when the glycans are shorter or completely absent.
The findings have important implications for HIV vaccine design. With the right choice of expression platform, immunogens can be produced with carefully tuned N-linked glycosylation in and around the CD4 receptor binding site. The aim is to find a perfect balance between the strength of interaction with VRC01 antibodies and the ability to accommodate glycans that are present in the Envelope spikes of the virus.
The Heineken Prizes for Science and Art were awarded during an official ceremony on September 27th 2018 in Amsterdam. Read the news item from The Royal Netherlands Academy of Arts and Sciences (KNAW), who selected the winners, here. The Heineken Young Scientist Awards were also awarded on the same night. Joost Snijder won in the category Medical/Biomedical Science.
Jop de Vrieze recently interviewed Joost Snijder for the Dutch magazine De Groene Amsterdammer about his work on viruses and his decision to start Snijder Bioscience. Read the article (in Dutch) here.
Alinda Wolthuis recently interviewed Joost Snijder for Dutch Chemistry magazine C2W. They talked about his scientific work, starting a research consultancy, and his recent Heineken Young Scientist Award. Follow this link to read the article (closed access for KNCV members only).
Esther Thole of NEMO Kennislink recently sat down with Joost Snijder for an interview about his work and the Heineken Young Scientists Award 2018. They discuss the benefits of combining different analytical techniques to study viruses on the molecular level, and talk about the trade-off between developing new analytical methods and learning new biology. Follow this link to read the full interview (in Dutch).
The Royal Netherlands Academy of Arts and Sciences (KNAW) has awarded Joost Snijder the biennial Heineken Young Scientists Award for Medical/Biomedical Sciences. More information about the award can be found in the news items below:
The award ceremony will be held on September 27th in Amsterdam.
Encapsulins are virus-like metabolic compartments from bacteria. Sigmund et al. demonstrated the versatile nanotechnological applications of encapsulins in a recent report in Nature Communications. They demonstrate how encapsulins can be expressed as functional nanocompartments in mammalian cells. The encapsulins are capable of targeted cargo encapsulation, allowing for the in situ construction of synthetic metabolic compartments, protective storage capsules and imaging labels.
Working with the Heck lab at Utrecht University, Snijder Bioscience contributed to the report by estimating the cargo load of encapsulins with native mass spectrometry, revealing that the nanocompartments can package between 60 and 100 copies of their cargo protein.