Human-disease associated amyloidogenic proteins are not unique in their ability to form amyloid fibrillar structures. Numerous microbes produce amyloidogenic proteins that have distinct functions for their physiology in their amyloid form, rather than solely detrimental. Emerging data indicate associations between various microbial organisms, including those which produce functional amyloids, with neurodegenerative diseases. Here, we review some of the evidence suggesting that microbial amyloids impact amyloid disease in host organisms. Experimental data are building a foundation for continued lines of enquiry and suggest that that direct or indirect interactions between microbial and host amyloids may be a contributor to amyloid pathologies. Inhibiting microbial amyloids or their interactions with the host may therefore represent a tangible target to limit various amyloid pathologies.
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http://dx.doi.org/10.1111/febs.17023 | DOI Listing |
Nanoscale
January 2025
Department of Engineering Mechanics, Hohai University, Nanjing 211100, P.R. China.
The aberrant aggregation of the human islet amyloid polypeptide (hIAPP) is a hallmark of type II diabetes. LL37, the only cathelicidin host-defense peptide in humans, plays essential roles in antimicrobial and immunomodulatory activities. Mounting evidence indicates that LL37 can inhibit the amyloid aggregation of hIAPP, suggesting possible interplays between infections and amyloid diseases while the mechanism remains unclear.
View Article and Find Full Text PDFAlzheimers Dement
January 2025
Center for Motor Neuron Biology and Disease, Columbia University Medical Center, New York, New York, USA.
This proceedings article summarizes the inaugural "T Cells in the Brain" symposium held at Columbia University. Experts gathered to explore the role of T cells in neurodegenerative diseases. Key topics included characterization of antigen-specific immune responses, T cell receptor (TCR) repertoire, microbial etiology in Alzheimer's disease (AD), and microglia-T cell crosstalk, with a focus on how T cells affect neuroinflammation and AD biomarkers like amyloid beta and tau.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
State Key Laboratory of Animal Nutrition, Beijing Engineering Technology Research Centre of Raw Milk Quality and Safety Control, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China; College of Animal Science and Technology, Ningxia University, Yinchuan 750021, China. Electronic address:
This study investigated the effects of rumen-degradable starch (RDS) on lactation performance, gastrointestinal fermentation, and plasma metabolomics in dairy cows. Six mid-lactation cows, fitted with rumen, duodenum, and ileum cannulas, were used in a duplicated 3 × 3 Latin square design with 28-day periods. The cows were fed a low RDS (LRDS; 62.
View Article and Find Full Text PDFMicroorganisms
January 2025
Translational Neuropharmacology Laboratory, Department of Psychology, University of Cyprus, 75 Kallipoleos Avenue, 1678 Nicosia, Cyprus.
For decades, Alzheimer's Disease (AD) research has focused on the amyloid cascade hypothesis, which identifies amyloid-beta (Aβ) as the primary driver of the disease. However, the consistent failure of Aβ-targeted therapies to demonstrate efficacy, coupled with significant safety concerns, underscores the need to rethink our approach to AD treatment. Emerging evidence points to microbial infections as environmental factors in AD pathoetiology.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Department of Chemistry, North-Eastern Hill University, Shillong 793 022, India.
The interaction of protein with nanoparticles (NPs) of varying shape and/or size boosts our understanding on their bioreactivity and establishes a comprehensive database for use in medicine, diagnosis, and therapeutic applications. The present study explores the interaction between lysozyme (LYZ) and different NPs like graphene oxide (GO) and zinc oxide (ZnO) having various shapes (spherical, 's', and rod-shaped, 'r') and sizes, focusing on their binding dynamics and subsequent effects on both the protein fibrillation and antimicrobial properties. Typically, GO is considered a promising medium due to its apparent inhibition and prolonged lag phase for LYZ fibrillation.
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