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One of the most widely used methods to detect an acute viral infection in clinical specimens is diagnostic real-time polymerase chain reaction. However, because of the COVID-19 pandemic, mass-spectrometry-based proteomics is currently being discussed as a potential diagnostic method for viral infections. Because proteomics is not yet applied in routine virus diagnostics, here we discuss its potential to detect viral infections. Apart from theoretical considerations, the current status and technical limitations are considered. Finally, the challenges that have to be overcome to establish proteomics in routine virus diagnostics are highlighted.
Global supply chains rely on the compliance and safety of their products, processes, and facilities. These vital services (often referred to as ‘quality assurance’ or ‘conformity assessment’ services) are provided by Conformity Assessment Bodies (CABs). This empirical study explores the impact of the COVID-19 pandemic on CABs as well as their response to the resulting challenges. Data was gathered through an online survey among all accredited CABs in Germany, which resulted in 555 valid responses. Taking a resilience perspective, we reveal that CABs were hit hard by the disruptions caused by the pandemic, albeit to different degrees, in part due to their type of services, size, and sectors served. Furthermore, we find that contingency plans do not directly cushion order declines (as the main indicator of the economic impact of the pandemic) but rather indirectly through helping CABs respond more quickly, which in turn mitigates their order declines. However, our results show that contingency plans can also have adverse effects if they hinder flexible reaction to the crisis. The findings of our study help managers and policymakers learn from the COVID-19 pandemic and improve the resilience of the conformity assessment sector and quality assurance in the event of future crises.
MALDI-TOF-MS-Based Identification of Monoclonal Murine Anti-SARS-CoV-2 Antibodies within One Hour
(2022)
During the SARS-CoV-2 pandemic, many virus-binding monoclonal antibodies have been developed for clinical and diagnostic purposes. This underlines the importance of antibodies as universal bioanalytical reagents. However, little attention is given to the reproducibility crisis that scientific studies are still facing to date. In a recent study, not even half of all research antibodies mentioned in publications could be identified at all. This should spark more efforts in the search for practical solutions for the traceability of antibodies. For this purpose, we used 35 monoclonal antibodies against SARS-CoV-2 to demonstrate how sequence-independent antibody identification can be achieved by simple means applied to the protein. First, we examined the intact and light chain masses of the antibodies relative to the reference material NIST-mAb 8671. Already half of the antibodies could be identified based solely on these two parameters. In addition, we developed two complementary peptide mass fingerprinting methods with MALDI-TOF-MS that can be performed in 60 min and had a combined sequence coverage of over 80%. One method is based on the partial acidic hydrolysis of the protein by 5 mM of sulfuric acid at 99 degrees C. Furthermore, we established a fast way for a tryptic digest without an alkylation step. We were able to show that the distinction of clones is possible simply by a brief visual comparison of the mass spectra. In this work, two clones originating from the same immunization gave the same fingerprints. Later, a hybridoma sequencing confirmed the sequence identity of these sister clones. In order to automate the spectral comparison for larger libraries of antibodies, we developed the online software ABID 2.0. This open-source software determines the number of matching peptides in the fingerprint spectra. We propose that publications and other documents critically relying on monoclonal antibodies with unknown amino acid sequences should include at least one antibody fingerprint. By fingerprinting an antibody in question, its identity can be confirmed by comparison with a library spectrum at any time and context.