Anthropogenic particles and legacy pollutants combined with transcriptomic and multi-biomarker responses for an integrated assessment of the health status of mussels Mytilus galloprovincialis in two locations of the Bay of Biscay
Abstract
Aberrant aggregation of the transactive response DNA-binding protein (TDP-43) is associated with several lethal neurodegenerative diseases, including amyotrophic lateral sclerosis and frontotemporal dementia. Cytoplasmic neuronal inclusions of TDP-43 are enriched in various fragments of the low-complexity C-terminal domain and are associated with different neurotoxicity. Here we dissect the structural basis of TDP-43 polymorphism using magic-angle spinning solid-state NMR spectroscopy in combination with electron microscopy and Fourier-transform infrared spectroscopy. We demonstrate that various low-complexity C-terminal fragments, namely TDP-13 (TDP-43 300–414 ), TDP-11 (TDP-43 300–399 ), and TDP-10 (TDP-43 314–414 ), adopt distinct polymorphic structures in their amyloid fibrillar state. Our work demonstrates that the removal of less than 10% of the low-complexity sequence at N- and C-termini generates amyloid fibrils with comparable macroscopic features but different local structural arrangement. It highlights that the assembly mechanism of TDP-43, in addition to the aggregation of the hydrophobic region, is also driven by complex interactions involving low-complexity aggregation-prone segments that are a potential source of structural polymorphism.
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BibTeX
@article{landro2026anthropogenic,
title = {{Anthropogenic particles and legacy pollutants combined with transcriptomic and multi-biomarker responses for an integrated assessment of the health status of mussels Mytilus galloprovincialis in two locations of the Bay of Biscay}},
author = {Sonia Landro and Ransford Parry and Isabella Gutiérrez-Zabala and Nagore González-Soto and Sophie Lecomte and Eider Bilbao and Florencia Arrighetti and Miren Cajaraville},
journal = {Marine Pollution Bulletin},
year = {2026},
month = oct,
doi = {10.1016/j.marpolbul.2026.119615},
url = {https://hal.science/hal-05842086v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Anthropogenic particles and legacy pollutants combined with transcriptomic and multi-biomarker responses for an integrated assessment of the health status of mussels Mytilus galloprovincialis in two locations of the Bay of Biscay
AU - Sonia Landro
AU - Ransford Parry
AU - Isabella Gutiérrez-Zabala
AU - Nagore González-Soto
AU - Sophie Lecomte
AU - Eider Bilbao
AU - Florencia Arrighetti
AU - Miren Cajaraville
PY - 2026
DA - 2026/10/29
JO - Marine Pollution Bulletin
DO - 10.1016/j.marpolbul.2026.119615
UR - https://hal.science/hal-05842086v1
AB - Aberrant aggregation of the transactive response DNA-binding protein (TDP-43) is associated with several lethal neurodegenerative diseases, including amyotrophic lateral sclerosis and frontotemporal dementia. Cytoplasmic neuronal inclusions of TDP-43 are enriched in various fragments of the low-complexity C-terminal domain and are associated with different neurotoxicity. Here we dissect the structural basis of TDP-43 polymorphism using magic-angle spinning solid-state NMR spectroscopy in combination with electron microscopy and Fourier-transform infrared spectroscopy. We demonstrate that various low-complexity C-terminal fragments, namely TDP-13 (TDP-43 300–414 ), TDP-11 (TDP-43 300–399 ), and TDP-10 (TDP-43 314–414 ), adopt distinct polymorphic structures in their amyloid fibrillar state. Our work demonstrates that the removal of less than 10% of the low-complexity sequence at N- and C-termini generates amyloid fibrils with comparable macroscopic features but different local structural arrangement. It highlights that the assembly mechanism of TDP-43, in addition to the aggregation of the hydrophobic region, is also driven by complex interactions involving low-complexity aggregation-prone segments that are a potential source of structural polymorphism.
SN - 0025-326X
SN - 1879-3363
ER -