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Special Issue "Protein-Based Infection, Inheritance, and Memory"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Microbiology".

Deadline for manuscript submissions: 31 January 2022.

Special Issue Editors

Prof. Dr. Yury O. Chernoff
E-Mail Website
Guest Editor
1. School of Biological Sciences, Georgia Institute of Technology, Krone Engineered Biosystems Building, 950 Atlantic Drive, Atlanta, GA 30332-2000, USA
2. Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg 199034, Russia
Interests: yeast genetics; protein biosynthesis, misfolding and aggregation; protein quality control; amyloids; prions; chaperones and stress response; protein-based inheritance
Dr. Anton Nizhnikov
E-Mail Website
Guest Editor
Institute of Agricultural Microbiology, Russian Academy of Sciences, and St. Petersburg State University, St. Petersburg, Russia
Interests: prion; amyloid; protein structure; proteomics; yeast; bacteria; protein aggregate; chaperone; protein fibril; amyloidogenic region

Special Issue Information

Dear Colleagues,

Overwhelming evidence, mostly accumulated relatively recently, has demonstrated that the templated proliferation of protein isoforms can result in the reproduction and amplification of information encoded in the protein structure. Therefore, self-perpetuating protein isoforms can become carriers of biological information that are not directly encoded in DNA sequences. Transmissible protein isoforms (prions) manifest themselves as infectious agents causing diseases, including some devastating diseases in humans and other mammals. In yeast and other fungi, prions manifest themselves as heritable elements, transmitted via cytoplasm. At the molecular level, many prions are based on fibrous cross-β aggregates (amyloids), although other molecular mechanisms for the transmission of protein-based information are also being uncovered. Self-perpetuating protein isoforms have also been implicated in cellular memory. Such non-heritable molecular memory devices found in yeast have been termed mnemons. The ability of proteins to serve as information templates challenges existing biological paradigms and opens additional pathways for information transfer in biological systems, potentially playing a role in adaptation and evolution. The current issue will cover molecular mechanisms controlling the ability of proteins to serve as information carriers in infection, inheritance, and memory.

Prof. Dr. Yury O. Chernoff
Dr. Anton Nizhnikov
Guest Editors

Manuscript Submission Information

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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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

  • Aggregation
  • amyloid
  • epigenetics
  • mnemon
  • non-Mendelian inheritance
  • prion
  • protein conformation

Published Papers (1 paper)

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Review

Review
β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
Int. J. Mol. Sci. 2021, 22(21), 11316; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms222111316 - 20 Oct 2021
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Abstract
Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation of higher [...] Read more.
Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation of higher order oligomers or even aggregates. In recent years, findings proving that β-barrel proteins can adopt cross-β amyloid folds have emerged. Different β-barrel proteins were shown to form amyloid fibrils in vitro. The formation of functional amyloids in vivo by β-barrel proteins for which the amyloid state is native was also discovered. In particular, several prokaryotic and eukaryotic proteins with β-barrel domains were demonstrated to form amyloids in vivo, where they participate in interspecies interactions and nutrient storage, respectively. According to recent observations, despite the variety of primary structures of amyloid-forming proteins, most of them can adopt a conformational state with the β-barrel topology. This state can be intermediate on the pathway of fibrillogenesis (“on-pathway state”), or can be formed as a result of an alternative assembly of partially unfolded monomers (“off-pathway state”). The β-barrel oligomers formed by amyloid proteins possess toxicity, and are likely to be involved in the development of amyloidoses, thus representing promising targets for potential therapy of these incurable diseases. Considering rapidly growing discoveries of the amyloid-forming β-barrels, we may suggest that their real number and diversity of functions are significantly higher than identified to date, and represent only “the tip of the iceberg”. Here, we summarize the data on the amyloid-forming β-barrel proteins, their physicochemical properties, and their biological functions, and discuss probable means and consequences of the amyloidogenesis of these proteins, along with structural relationships between these two widespread types of β-folds. Full article
(This article belongs to the Special Issue Protein-Based Infection, Inheritance, and Memory)
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