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Microbiology Research
Special Issues
Current Progress in Prion Research
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Current Progress in Prion Research

A special issue of Microbiology Research (ISSN 2036-7481).

Deadline for manuscript submissions: closed (29 February 2024) | Viewed by 5633

Special Issue Editor

Dr. Kefeng Qin

E-Mail Website
Guest Editor
Department of Neurology, University of Chicago, Chicago, IL, USA
Interests: prion; protein structure; copper; Alzheimer’s disease

Special Issue Information

Dear Colleagues,

Although accumulating but conflicting reports have discussed the possible roles of prion protein (PrP) in Alzheimer’s disease (AD), whether and how prion interacts with β-amyloid precursor protein (APP) and/or microtubule-associated protein tau (Mapt) remains elusive. This Special Issue collects evidence regarding the interaction of prion with APP, β-amyloid (Aβ) and/or tau. PrPC may influence APP amyloidogenic pathways and exosome-related Aβ secretion. Prion may also affect autophagy by regulating levels of dephosphorylated Tau. Therefore, prion may be important in the development of AD.

Dr. Kefeng Qin
Guest Editor

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Microbiology Research is an international peer-reviewed open access monthly journal published by MDPI.

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Keywords

  • prion
  • prion diseases
  • protein structure
  • Alzheimer’s disease

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Published Papers (3 papers)

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Research

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17 pages, 21389 KiB  
Article
Transcription Factors Mcm1 and Sfp1 May Affect [PSI+] Prion Phenotype by Altering the Expression of the SUP35 Gene
by Andrew G. Matveenko, Anastasiia S. Mikhailichenko, Polina B. Drozdova and Galina A. Zhouravleva
Microbiol. Res. 2024, 15(2), 508-524; https://doi.org/10.3390/microbiolres15020034 - 8 Apr 2024
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Abstract
Mcm1 is an essential Q/N-rich transcription factor. Q/N-rich proteins interact with each other, and many affect the [PSI+] prion formed by the translation termination factor Sup35 (eRF3). We found that transient MCM1 overexpression increased nonsense suppression in [PSI+ [...] Read more.
Mcm1 is an essential Q/N-rich transcription factor. Q/N-rich proteins interact with each other, and many affect the [PSI+] prion formed by the translation termination factor Sup35 (eRF3). We found that transient MCM1 overexpression increased nonsense suppression in [PSI+] strains and SUP35 transcription. As we had discovered similar effects of another Q/N-rich transcription factor, Sfp1, here we focus on the roles of Mcm1 and Sfp1 in SUP35 expression, as well as on the effects of Sfp1 on the expression of the gene encoding another release factor, Sup45 (eRF1). Mutations in the SUP35 promoter showed that none of the potential Mcm1 binding sites affected the Sup35 protein level or nonsense suppression, even during MCM1 overexpression. Mcm1 itself neither formed aggregates in vivo nor affected Sup35 aggregation. In contrast, a mutation in the Sfp1-binding site decreased Sup35 production and [PSI+] toxicity of excess Sfp1. Mutation of the Sfp1 binding site in the SUP45 promoter lowered SUP45 expression and increased nonsense suppression even more drastically. Our data indicate that the mechanisms of Mcm1 and Sfp1 action differ. While Mcm1 seems unlikely to directly regulate SUP35 expression, Sfp1 appears to act through its binding sites and to directly activate SUP35 expression, which in turn may influence the [PSI+] prion phenotype and toxicity. Full article
(This article belongs to the Special Issue Current Progress in Prion Research)
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Review

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14 pages, 971 KiB  
Review
Are Gastrointestinal Microorganisms Involved in the Onset and Development of Amyloid Neurodegenerative Diseases?
by Vladimir I. Muronetz, Lidia P. Kurochkina, Evgeniia V. Leisi and Sofia S. Kudryavtseva
Microbiol. Res. 2023, 14(4), 1942-1955; https://doi.org/10.3390/microbiolres14040131 - 20 Nov 2023
Cited by 1 | Viewed by 1339
Abstract
This review discusses a few examples of specific mechanisms mediating the contribution of the GIT microbiota to the development of amyloid neurodegenerative diseases caused by the pathologic transformation of prion protein, or alpha-synuclein. The effect of the bacterial GroE chaperonin system and phage [...] Read more.
This review discusses a few examples of specific mechanisms mediating the contribution of the GIT microbiota to the development of amyloid neurodegenerative diseases caused by the pathologic transformation of prion protein, or alpha-synuclein. The effect of the bacterial GroE chaperonin system and phage chaperonins (single-ring OBP and double-ring EL) on prion protein transformation has been described. A number of studies have shown that chaperonins stimulate the formation of cytotoxic amyloid forms of prion protein in an ATP-dependent manner. Moreover, it was found that E. coli cell lysates have a similar effect on prion protein, and the efficiency of amyloid transformation correlates with the content of GroE in cells. Data on the influence of some metabolites synthesized by gut microorganisms on the onset of synucleinopathies, such as Parkinson’s disease, is provided. In particular, the induction of amyloid transformation of alpha-synuclein from intestinal epithelial cells with subsequent prion-like formation of its pathologic forms in nervous tissues featuring microbiota metabolites is described. Possible mechanisms of microbiota influence on the occurrence and development of amyloid neurodegenerative diseases are considered. Full article
(This article belongs to the Special Issue Current Progress in Prion Research)
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22 pages, 1445 KiB  
Review
Clustering Disease of Clostridioides Difficile Infection: Implication for the Management in Internal Medicine
by Pietro Crispino
Microbiol. Res. 2023, 14(3), 1376-1397; https://doi.org/10.3390/microbiolres14030094 - 15 Sep 2023
Viewed by 2361
Abstract
Clostridioides difficile is a bacterium responsible for a healthcare-associated gastrointestinal infection, primarily affecting people who have undergone prolonged antibiotic treatment or who have compromised immune systems. The CD is of particular concern due to its high recurrence rates and the potential for serious [...] Read more.
Clostridioides difficile is a bacterium responsible for a healthcare-associated gastrointestinal infection, primarily affecting people who have undergone prolonged antibiotic treatment or who have compromised immune systems. The CD is of particular concern due to its high recurrence rates and the potential for serious outcomes, including life-threatening conditions such as pseudomembranous colitis, septic shock, and all associated conditions. Since this infection is a disease associated with other health conditions, a general vision of the problems is necessary which aims to obtain a general overview of the manifestations that generally correlate with care. Clinical reasoning following the disease-clustering method is able to produce a categorization process by grouping the possible correlations of the various conditions or factors underlying diseases on the basis of certain similarities or common models. The clustering process is performed using data analysis techniques which, by statically correlating each other, give an exact dimension of all the information related to a particular disease. In the case of CD, reasoning based on disease clustering has better clarified the practices, appropriateness in infection control, judicious use of antibiotics, and research into therapeutic and preventive strategies. This review, taking advantage of the clustering strategy, aimed to analyze the contingent conditions of the infection under examination, to reduce the incidence and impact of CD, having as its mission the improvement of the results deriving from the contrast of all those correlated pathological conditions to healthcare for the improvement of public health. Full article
(This article belongs to the Special Issue Current Progress in Prion Research)
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