Meine Ramakers

Correction for Konstantoulea et al., Phagocytes as plaque catalysts: Human macrophages generate seeding-competent Aβ42 fibrils with cross-seeding activity

Katerina Konstantoulea, Meine Ramakers, Sarah C. Borrie, Dries T’Syen et autres

status: Published

Phagocytes as plaque catalysts: Human macrophages generate seeding-competent Aβ42 fibrils with cross-seeding activity

Katerina Konstantoulea, Meine Ramakers, Sarah Catherine Borrie, Dries T’Syen et autres

The prevailing view frames microglia and macrophages as guardians against amyloid beta (Aβ) accumulation in Alzheimer's disease (AD). Here, we overturn this paradigm by demonstrating that human phagocytic cells, including differentiated THP-1 macrophages and hESC-derived microglia, are not merely passive responders but …

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Phagocytes as Plaque Catalysts: Human Macrophages Actively Generate Pathogenic Aβ42 Fibrils with Seeding and Cross-Seeding Potency

Katerina Konstantoulea, Meine Ramakers, Sarah Catherine Borrie, Dries T’Syen et autres

Abstract The prevailing view frames microglia and macrophages as guardians against amyloid beta (Aβ) accumulation in Alzheimer’s disease (AD). Here, we overturn this paradigm by demonstrating that human phagocytic cells—including differentiated THP-1 macrophages and iPSC-derived microglia—are not merely passive responders but active …

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TDP-43 seeding induces cytoplasmic aggregation heterogeneity and nuclear loss of function of TDP-43

JL Rummens, Bilal Khalil, Günseli Yıldırım, Pedro Silva et autres

Cytoplasmic aggregation and nuclear depletion of TAR DNA-binding protein 43 (TDP-43) are hallmarks of several neurodegenerative disorders. Yet, recapitulating both features in cellular systems has been challenging. Here, we produced amyloid-like fibrils from recombinant TDP-43 low-complexity domain and demonstrate that sonicated fibrils …

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Local structural preferences in shaping tau amyloid polymorphism

Nikolaos N. Louros, Martin Wilkinson, Grigoria Tsaka, Meine Ramakers et autres

Tauopathies encompass a group of neurodegenerative disorders characterised by diverse tau amyloid fibril structures. The persistence of polymorphism across tauopathies suggests that distinct pathological conditions dictate the adopted polymorph for each disease. However, the extent to which intrinsic structural tendencies of tau …

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Exploiting the aggregation propensity of beta-lactamases to design inhibitors that induce enzyme misfolding

Ladan Khodaparast, Laleh Khodaparast, Guiqin Wu, Emiel Michiels et autres

There is an arms race between beta-lactam antibiotics development and co-evolving beta-lactamases, which provide resistance by breaking down beta-lactam rings. We have observed that certain beta-lactamases tend to aggregate, which persists throughout their evolution under the selective pressure of antibiotics on their …

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Author Correction: Reverse engineering synthetic antiviral amyloids

Emiel Michiels, Kenny Roose, Rodrigo U. Gallardo, Ladan Khodaparast et autres

In this article the grant number G045920N relating to Funds for Scientific Research Flanders was omitted. The original article has been corrected.

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Exploiting the intrinsic misfolding propensity of the KRAS oncoprotein

Kobe Janssen, Filip F. Claes, Dido Van de Velde, Vanessa L. Wehbi et autres

Mutant KRAS is a major driver of oncogenesis in a multitude of cancers but remains a challenging target for classical small molecule drugs, motivating the exploration of alternative approaches. Here, we show that aggregation-prone regions (APRs) in the primary sequence of the …

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Tau amyloid polymorphism is shaped by local structural propensities of its protein sequence

Nikolaos N. Louros, Martin Wilkinson, Grigoria Tsaka, Meine Ramakers et autres

Abstract Different tauopathies are characterized by specific amyloid filament folds that are conserved between patients. Disease-specific tau filament folds probably reflect the specific pathological contexts leading to their formation including isoforms or post-translational modifications. Little is known, however, as to whether and …

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Seeding, maturation and propagation of amyloid β-peptide aggregates in Alzheimer’s disease

Xiaohang Li, Simona Ospitalieri, Tessa Robberechts, Linda Hofmann et autres

Alzheimer's disease is neuropathologically characterized by the deposition of the amyloid β-peptide (Aβ) as amyloid plaques. Aβ plaque pathology starts in the neocortex before it propagates into further brain regions. Moreover, Aβ aggregates undergo maturation indicated by the occurrence of post-translational modifications. …

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Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers

Nikolaos N. Louros, Meine Ramakers, Emiel Michiels, Katerina Konstantoulea et autres

Heterotypic amyloid interactions between related protein sequences have been observed in functional and disease amyloids. While sequence homology seems to favour heterotypic amyloid interactions, we have no systematic understanding of the structural rules determining such interactions nor whether they inhibit or facilitate …

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Heterotypic Amyloid β interactions facilitate amyloid assembly and modify amyloid structure

Katerina Konstantoulea, Patrícia Silva Guerreiro, Meine Ramakers, Nikolaos N. Louros et autres

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