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Naegleria fowleri, is the causative agent of Primary Amoebic Meningoencephalitis (PAM), a lethal acute brain inflammation with high mortality. The virulent and reproductively active trophozoite stage of N. fowleri migrates to central nervous system (CNS) by entering through nasal passage and causes severe neural infection, brain disease and inflammation with high mortality.

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Analysis of virulence factors in extracellular vesicles secreted by Naegleria fowleri.

Parasitol Res

October 2024

Universidad Nacional Autónoma de México, Grupo CyMA, UIICSE, FES Iztacala, Laboratorio de Microbiología Ambiental, Estado de México, Tlalnepantla de Baz, Mexico.

Article Synopsis
  • Naegleria fowleri causes primary amebic meningoencephalitis (PAM), a deadly infection with over 95% mortality, especially in young individuals, and its symptoms resemble other types of meningitis, complicating timely diagnosis.
  • Researchers aimed to analyze the virulence factors in extracellular vesicles (EVs) secreted by N. fowleri, employing techniques like SDS-PAGE and RT-PCR for molecular identification.
  • The study found that N. fowleri secretes various sized vesicles containing key proteins, including ones recognized by specific antibodies and markers, suggesting these vesicles may play a role in the amoeba’s communication and pathogenicity.
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Article Synopsis
  • Free-living amoeba, though rarely harmful to humans, can cause severe central nervous system infections, as evidenced by two case reports of rapid illness progression.
  • The first case involved a 36-year-old male whose disease was linked to contaminated water, leading to fatal complications despite positive identification of the infection in cerebrospinal fluid (CSF).
  • The second case featured a 4-year-old boy with similar symptoms; despite treatment attempts, he also succumbed to cardiac arrest, highlighting the urgent need for awareness and early diagnosis of such parasitic infections.
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Among sequenced organisms, the genome of is unique in that it encodes for a massive amount of repeat-rich sequences in the coding region of genes. This results in the proteome encoding for thousands of repeat-rich proteins, with nearly 24% of the proteome encoding Q/N-rich regions that are predicted to be prion like in nature. To begin investigating the role of prion-like proteins in , we decided to investigate ERF3, the ortholog of the well-characterized yeast prion protein Sup35.

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() infection the upper respiratory tract causes a fatal CNS disease known as primary amoebic meningoencephalitis (PAM). The robust immune response to underlies the immunopathology that characterizes the disease. However, little is known about why this pathogen evades immune control.

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