The structure of mouse cytomegalovirus m04 protein determined from sparse NMR data reveals a new fold of the m02-m06 family of viral immune modulators
By Nikolaos G. Sgourakis, K. Natarajan, Jinfa Ying, B. Vogeli, L. Boyd, D. Margulies, A. Bax. 2014
24 citations recorded by the source corpus.
Summary Immunoevasins are key proteins employed by viruses to subvert host immune responses. Determining their high-resolution structures is key to understanding virus-host interactions towards the design of vaccines and other antiviral therapies. Mouse cytomegalovirus (MCMV) encodes a unique set of immunoevasins, the m02-m06 family, that modulates major histocompatibility complex class I (MHC-I) antigen presentation to CD8+ T cells and natural killer (NK) cells. Notwithstanding the large number of genetic and functional studies, the structural biology of immunoevasins remains incompletely understood, due largely to crystallization bottlenecks. Here we implement a new technology employing sparse NMR data and integrative Rosetta modeling to determine the structure of the m04/gp34 immunoevasin extracellular domain. The structure reveals a new β fold that is representative of the m02-m06 family of viral proteins, several of which are known to bind MHC-I molecules and interfere with antigen presentation, suggesting its role as a diversified immune regulation module.
Subfields: Endocrinology, Epidemiology, Parasitology
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Citations in the corpus
- Critical Assessment of Methods of Protein Structure Prediction (CASP) – Progress and New directions in Round XI (2016, methodology): “28,29,32 In CASP11 we conducted an initial experiment to objectively assess the extent to which current modeling meth-ods can improve the accuracy of structures based on such data.”
- Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data (2016, unknown): “…be quite useful, and we previously applied this method to the structural study of the 196-residue extracellular domain of the cytomegalovirus m04 protein (Sgourakis et al. 2014), which had proven recalcitrant to conventional structural analysis due to its limited stability and tendency to dimerize.”
- Chemical shift-based methods in NMR structure determination (2018, methodology): “complementary NOE and RDC measurements [94].”