The accumulation of rotavirus NSP3 dimers does not correlate with the extent of host cell translation inhibition

Edgar Reyna-Rosas; Hugo I Contreras-Treviño; Renato León-Rodríguez; Leticia Rocha-Zavaleta; Tzvetanka D Dinkova; Luis Padilla-Noriega

doi:10.2217/fvl-2020-0259

The accumulation of rotavirus NSP3 dimers does not correlate with the extent of host cell translation inhibition

Future Virology ◽

10.2217/fvl-2020-0259 ◽

2020 ◽

Vol 15 (9) ◽

pp. 565-576

Author(s):

Edgar Reyna-Rosas ◽

Hugo I Contreras-Treviño ◽

Renato León-Rodríguez ◽

Leticia Rocha-Zavaleta ◽

Tzvetanka D Dinkova ◽

...

Keyword(s):

Host Cell ◽

Dimer Formation ◽

Translation Inhibition ◽

Linear Kinetics ◽

Kinetics Of

Aim: We aimed to determine the functionality of rotavirus NSP3 dimers. Materials & methods: We expressed rhesus rotavirus NSP3 and determined the kinetics of host cell translation inhibition and the levels of accumulated dimerization intermediates and dimers. Results: We observed a linear kinetics of host cell translation inhibition, which correlated well with the sum of the dimerization intermediates and dimers. Treatment with 17-dimethylaminoethylamino-17-demethoxygeldanamycin reduced the accumulation of NSP3 dimers and potentiated host cell translation inhibition. Conclusion: Our results show that NSP3 dimer formation does not correlate with host cell translation inhibition and suggest that both NSP3 dimers and dimerization intermediates are functional and inhibit host cell translation.

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Modeling the complete kinetics of coxsackievirus B3 reveals human determinants of host-cell feedback

Cell Systems ◽

10.1016/j.cels.2021.02.004 ◽

2021 ◽

Vol 12 (4) ◽

pp. 304-323.e13

Author(s):

Aaron B. Lopacinski ◽

Andrew J. Sweatt ◽

Christian M. Smolko ◽

Elise Gray-Gaillard ◽

Cheryl A. Borgman ◽

...

Keyword(s):

Host Cell ◽

Coxsackievirus B3 ◽

Kinetics Of

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Kinetics of Host Cell Recruitment During Dissemination of Diffuse Malignant Peritoneal Mesothelioma

Cancer Microenvironment ◽

10.1007/s12307-010-0048-1 ◽

2010 ◽

Vol 4 (1) ◽

pp. 39-50 ◽

Cited By ~ 8

Author(s):

Nathan R. Miselis ◽

Bonnie W. Lau ◽

Zhijin Wu ◽

Agnes B. Kane

Keyword(s):

Host Cell ◽

Peritoneal Mesothelioma ◽

Malignant Peritoneal Mesothelioma ◽

Cell Recruitment ◽

Diffuse Malignant Peritoneal Mesothelioma ◽

Kinetics Of

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Non-linear kinetics of glutamyl-tRNA synthesis catalyzed by high molecular weight complexes from rat brain neuronal cells but not from glial cells

Molecular Brain Research ◽

10.1016/0169-328x(86)90016-1 ◽

1986 ◽

Vol 1 (1) ◽

pp. 17-27

Author(s):

Lucille Lacoste ◽

Leif Hertz ◽

Jacques Lapointe

Keyword(s):

Molecular Weight ◽

Rat Brain ◽

High Molecular Weight ◽

Glial Cells ◽

Neuronal Cells ◽

Linear Kinetics ◽

Non Linear ◽

Kinetics Of

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Time kinetics of cyclobutane pyrimidine dimer formation by narrowband and broadband UVB irradiation

Journal of Dermatological Science ◽

10.1016/j.jdermsci.2021.07.009 ◽

2021 ◽

Author(s):

Erika Toriyama ◽

Hideyuki Masuda ◽

Kan Torii ◽

Kyoko Ikumi ◽

Akimichi Morita

Keyword(s):

Pyrimidine Dimer ◽

Cyclobutane Pyrimidine Dimer ◽

Dimer Formation ◽

Uvb Irradiation ◽

Kinetics Of

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Physiological implications of linear kinetics of mitochondrial respiration in vitro

AJP Cell Physiology ◽

10.1152/ajpcell.00264.2008 ◽

2008 ◽

Vol 295 (3) ◽

pp. C844-C846 ◽

Cited By ~ 14

Author(s):

Graham Kemp

Keyword(s):

Mitochondrial Respiration ◽

Linear Kinetics ◽

Kinetics Of

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A Dimerization Site at SCR-17/18 in Factor H Clarifies a New Mechanism for Complement Regulatory Control

Frontiers in Immunology ◽

10.3389/fimmu.2020.601895 ◽

2021 ◽

Vol 11 ◽

Author(s):

Orla M. Dunne ◽

Xin Gao ◽

Ruodan Nan ◽

Jayesh Gor ◽

Penelope J. Adamson ◽

...

Keyword(s):

Host Cell ◽

Analytical Ultracentrifugation ◽

Dissociation Constants ◽

Alternative Pathway ◽

Factor H ◽

Regulatory Control ◽

Size Exclusion ◽

Complement Factor ◽

Dimer Formation ◽

Self Association

Complement Factor H (CFH), with 20 short complement regulator (SCR) domains, regulates the alternative pathway of complement in part through the interaction of its C-terminal SCR-19 and SCR-20 domains with host cell-bound C3b and anionic oligosaccharides. In solution, CFH forms small amounts of oligomers, with one of its self-association sites being in the SCR-16/20 domains. In order to correlate CFH function with dimer formation and the occurrence of rare disease-associated variants in SCR-16/20, we identified the dimerization site in SCR-16/20. For this, we expressed, in Pichia pastoris, the five domains in SCR-16/20 and six fragments of this with one-three domains (SCR-19/20, SCR-18/20, SCR-17/18, SCR-16/18, SCR-17 and SCR-18). Size-exclusion chromatography suggested that SCR dimer formation occurred in several fragments. Dimer formation was clarified using analytical ultracentrifugation, where quantitative c(s) size distribution analyses showed that SCR-19/20 was monomeric, SCR-18/20 was slightly dimeric, SCR-16/20, SCR-16/18 and SCR-18 showed more dimer formation, and SCR-17 and SCR-17/18 were primarily dimeric with dissociation constants of ~5 µM. The combination of these results located the SCR-16/20 dimerization site at SCR-17 and SCR-18. X-ray solution scattering experiments and molecular modelling fits confirmed the dimer site to be at SCR-17/18, this dimer being a side-by-side association of the two domains. We propose that the self-association of CFH at SCR-17/18 enables higher concentrations of CFH to be achieved when SCR-19/20 are bound to host cell surfaces in order to protect these better during inflammation. Dimer formation at SCR-17/18 clarified the association of genetic variants throughout SCR-16/20 with renal disease.

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