Next Article in Journal
Lab-Based Retrospective 10-Year Analysis Shows Seasonal Variation of Vaginal Candida Infection Rates in Belgium
Next Article in Special Issue
Dynamic Features of Herd Immunity: Similarities in Age-Specific Anti-Measles Seroprevalence Data between Two Countries of Different Epidemiological History
Previous Article in Journal
Is Long COVID a State of Systemic Pericyte Disarray?
Previous Article in Special Issue
Freshwater Clam Extract Mitigates Neuroinflammation and Amplifies Neurotrophic Activity of Glia: Insights from In Vitro Model of Neurodegenerative Pathomechanism
Article

A Microplate-Based Approach to Map Interactions between TDP-43 and α-Synuclein

Department of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Korea
*
Author to whom correspondence should be addressed.
Academic Editors: Muh-Shi Lin and Andrew Chih Wei Huang
J. Clin. Med. 2022, 11(3), 573; https://doi.org/10.3390/jcm11030573
Received: 27 December 2021 / Revised: 15 January 2022 / Accepted: 18 January 2022 / Published: 24 January 2022
(This article belongs to the Special Issue Role of Enzyme-Linked Immunosorbent Assay (ELISA))
Trans-active response DNA-binding protein (TDP-43) is a multifunctional regulatory protein, whose abnormal deposition in neurons was linked to debilitating neurodegenerative diseases, such as amyotrophic lateral sclerosis, frontotemporal lobar degeneration, Limbic-predominant age-related TDP-43 encephalopathy, and Alzheimer’s disease with a secondary pathology. Several reports showed that TDP-43 proteinopathy as a comorbidity can form aggregates with other pathological proteins. The co-deposition of alpha synuclein and TDP-43 inclusions was previously reported in glial cells and by observing TDP-43 proteinopathy in Lewy body disease. In this study, it was hypothesized that alpha synuclein and TDP-43 may co-aggregate, resulting in comorbid synucleinopathy and TDP-43 proteinopathy. A solid-phase microplate-based immunoassay was used to map out the epitopes of anti-TDP-43 antibodies and locate the interaction of TDP-43 with α-synuclein. A region of the low complexity domain of TDP-43 (aa 311–314) was shown to interact with full-length α-synuclein. Conversely, full-length TDP-43 was shown to bind to the non-amyloid beta component of α-synuclein. Using in silico sequence-based prediction, the affinity and dissociation constant of full-length TDP-43 and α-synuclein were calculated to be −10.83 kcal/mol and 1.13 × 10−8, respectively. Taken together, this microplate-based method is convenient, economical, and rapid in locating antibody epitopes as well as interaction sites of two proteins. View Full-Text
Keywords: epitope mapping; TDP-43; alpha synuclein; ELISA; comorbidity; proteinopathy; aggregation epitope mapping; TDP-43; alpha synuclein; ELISA; comorbidity; proteinopathy; aggregation
Show Figures

Figure 1

MDPI and ACS Style

Jamerlan, A.M.; An, S.S.A. A Microplate-Based Approach to Map Interactions between TDP-43 and α-Synuclein. J. Clin. Med. 2022, 11, 573. https://doi.org/10.3390/jcm11030573

AMA Style

Jamerlan AM, An SSA. A Microplate-Based Approach to Map Interactions between TDP-43 and α-Synuclein. Journal of Clinical Medicine. 2022; 11(3):573. https://doi.org/10.3390/jcm11030573

Chicago/Turabian Style

Jamerlan, Angelo M., and Seong S.A. An. 2022. "A Microplate-Based Approach to Map Interactions between TDP-43 and α-Synuclein" Journal of Clinical Medicine 11, no. 3: 573. https://doi.org/10.3390/jcm11030573

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop