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Instruments / Technical Area	Publication Details	Published
	Metabolic reprogramming in colon cancer cells persistently infected with Newcastle disease virus Tong Yu , Archana Chandrabhan Jadhav , Jiabao Xu , Adrian L. Harris , Venugopal Nair , Wei E. Huang Cancers 15 DOI: 10.3390/cancers15030811 Open Access Show Abstract ▼ Abstract: Newcastle disease virus (NDV) is an oncolytic agent against various types of mammalian cancers. As with all cancer therapies, the development of cancer resistance, both innate and acquired, is becoming a challenge. In this study, we investigated persistently NDV-infected Caco-2 colon cancer cells, designated as virus-resistant (VR) Caco-2 cells, which were then able to resist NDV-mediated oncolysis. We applied single-cell Raman spectroscopy, combined with deuterium isotope probing (Raman-DIP) techniques, to investigate the metabolic adaptations and dynamics in VR Caco-2 cells. A linear discriminant analysis (LDA) model demonstrated excellent performance in differentiating VR Caco-2 from Caco-2 cells at single-cell level. By comparing the metabolic profiles in a time-resolved manner, the de novo synthesis of proteins and lipids was found upregulated, along with decreased DNA synthesis in VR Caco-2. The results suggest that VR Caco-2 cells might reprogram their metabolism and divert energy from proliferation to protein synthesis and lipidic modulation. The ability to identify and characterise single resistant cells among a population of cancer cells would help develop a deeper understanding of the resistance mechanisms and better tactics for developing effective cancer treatment.	Jan 2023
B22-Multimode InfraRed imaging And Microspectroscopy	Interrogation of IDH1 status in gliomas by fourier transform infrared spectroscopy James M. Cameron , Justin J. A. Conn , Christopher Rinaldi , Alexandra Sala , Paul M. Brennan , Michael D. Jenkinson , Helen Caldwell , Gianfelice Cinque , Khaja Syed , Holly J. Butler , Mark G. Hegarty , David S. Palmer , Matthew J. Baker Cancers 12 DOI: 10.3390/cancers12123682 Diamond Proposal Number(s): [23417] Open Access Show Abstract ▼ Abstract: Mutations in the isocitrate dehydrogenase 1 (IDH1) gene are found in a high proportion of diffuse gliomas. The presence of the IDH1 mutation is a valuable diagnostic, prognostic and predictive biomarker for the management of patients with glial tumours. Techniques involving vibrational spectroscopy, e.g., Fourier transform infrared (FTIR) spectroscopy, have previously demonstrated analytical capabilities for cancer detection, and have the potential to contribute to diagnostics. The implementation of FTIR microspectroscopy during surgical biopsy could present a fast, label-free method for molecular genetic classification. For example, the rapid determination of IDH1 status in a patient with a glioma diagnosis could inform intra-operative decision-making between alternative surgical strategies. In this study, we utilized synchrotron-based FTIR microanalysis to probe tissue microarray sections from 79 glioma patients, and distinguished the positive class (IDH1-mutated) from the IDH1-wildtype glioma, with a sensitivity and specificity of 82.4% and 83.4%, respectively. We also examined the ability of attenuated total reflection (ATR)-FTIR spectroscopy in detecting the biomolecular events and global epigenetic and metabolic changes associated with mutations in the IDH1 enzyme, in blood serum samples collected from an additional 72 brain tumour patients. Centrifugal filtration enhanced the diagnostic ability of the classification models, with balanced accuracies up to ~69%. Identification of the molecular status from blood serum prior to biopsy could further direct some patients to alternative treatment strategies.	Dec 2020
B21-High Throughput SAXS I02-Macromolecular Crystallography	Natural killer cell activation receptor NKP30 oligomerization depends on its n-glycosylation Ondřej Skořepa , Samuel Pazicky , Barbora Kalousková , Jan Bláha , Celeste Abreu , Tomáš Ječmen , Michal Rosůlek , Alexander Fish , Arthur Sedivy , Karl Harlos , Jan Dohnalek , Tereza Skálová , Ondřej Vaněk Cancers 12 DOI: 10.3390/cancers12071998 Diamond Proposal Number(s): [10627] Open Access Show Abstract ▼ Abstract: NKp30 is one of the main human natural killer (NK) cell activating receptors used in directed immunotherapy. The oligomerization of the NKp30 ligand binding domain depends on the length of the C-terminal stalk region, but our structural knowledge of NKp30 oligomerization and its role in signal transduction remains limited. Moreover, ligand binding of NKp30 is affected by the presence and type of N-glycosylation. In this study, we assessed whether NKp30 oligomerization depends on its N-glycosylation. Our results show that NKp30 forms oligomers when expressed in HEK293S GnTI− cell lines with simple N-glycans. However, NKp30 was detected only as monomers after enzymatic deglycosylation. Furthermore, we characterized the interaction between NKp30 and its best-studied cognate ligand, B7-H6, with respect to glycosylation and oligomerization, and we solved the crystal structure of this complex with glycosylated NKp30, revealing a new glycosylation-induced mode of NKp30 dimerization. Overall, this study provides new insights into the structural basis of NKp30 oligomerization and explains how the stalk region and glycosylation of NKp30 affect its ligand affinity. This furthers our understanding of the molecular mechanisms involved in NK cell activation, which is crucial for the successful design of novel NK cell-based targeted immunotherapeutics.	Jul 2020

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