Bert Houben

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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Native Fold Delay and its implications for co-translational chaperone binding and protein aggregation

Ramon Duran‐Romaña, Bert Houben, Paula Fernández Migens, Ying Zhang et autres

Because of vectorial protein translation, residues that interact in the native protein structure but are distantly separated in the primary sequence are unavailable simultaneously. Instead, there is a temporal delay during which the N-terminal interaction partner is unsatisfied and potentially vulnerable to …

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Co-translational protein aggregation and ribosome stalling as a broad-spectrum antibacterial mechanism

Laleh Khodaparast, Ladan Khodaparast, Ramon Duran‐Romaña, Guiqin Wu et autres

Drug-resistant bacteria pose an urgent global health threat, necessitating the development of antibacterial compounds with novel modes of action. Protein biosynthesis accounts for up to half of the energy expenditure of bacterial cells, and consequently inhibiting the efficiency or fidelity of the …

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N-glycosylation as a eukaryotic protective mechanism against protein aggregation

Ramon Duran‐Romaña, Bert Houben, Matthias De Vleeschouwer, Nikolaos N. Louros et autres

The tendency for proteins to form aggregates is an inherent part of every proteome and arises from the self-assembly of short protein segments called aggregation-prone regions (APRs). While posttranslational modifications (PTMs) have been implicated in modulating protein aggregation, their direct role in …

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Analyzing the implications of protein folding delay caused by translation

Bert Houben, Ramon Duran‐Romaña, Paula Fernández Migens, Frédéric Rousseau et autres

ABSTRACT Because of vectorial protein production, residues that interact in the native protein structure but are distantly separated in the primary sequence are unavailable simultaneously. Instead, there is a temporal delay during which the N-terminal interaction partner is vulnerable to off-pathway, non-native …

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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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N-glycosylation as a eukaryotic protective mechanism against protein aggregation

Ramon Duran‐Romaña, Bert Houben, Matthias De Vleeschouwer, Nikolaos N. Louros et autres

ABSTRACT The tendency for proteins to form aggregates is an inherent part of every proteome and arises from the self-assembly of short protein segments called aggregation-prone regions (APRs). While post-translational modifications (PTMs) have been implicated in modulating protein aggregation, their direct role …

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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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Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study

Joëlle A.J. Housmans, Bert Houben, Margarita Monge‐Morera, Diego Asvestas et autres

Highly ordered, straight amyloid fibrils readily lend themselves to structure determination techniques and have therefore been extensively characterized. However, the less ordered curly fibrils remain relatively understudied, and the structural organization underlying their specific characteristics remains poorly understood. We found that the …

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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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