Following the success of this Research Topic, we are happy to launch a second edition of the project in which we extend the scope of the issue to the study of the phenomenon of protein aggregation in other microorganisms, in addition to bacteria.
Typically, only folded and soluble proteins are functional. Protein folding and solubility are controlled genetically, transcriptionally, and at the protein sequence and structural level. In addition, a well-conserved cellular machinery assists the folding of polypeptides and preserves proteostasis. When these redundant protective strategies are overcome, misfolded proteins are recruited into aggregates.
Recombinant protein production is an essential tool for the biotechnology industry and also supports expanding areas of basic and biomedical research, including structural genomics and proteomics. Many recombinant polypeptides produced in microbial hosts undergo irregular or incomplete folding processes that usually result in their accumulation as insoluble aggregates. The solubility of microbially produced proteins is of major concern in the production of life-saving protein therapeutics and strategies aimed to improve it are needed.
The presence of a fraction of molecules in a native-like structure in microbial aggregates endorses them with a degree of biological activity, a property that in recent years that can be exploited for applied purposes.
The protein embedded in microbial deposits resembles the amyloid fibrils characteristic of several human neurodegenerative diseases. This makes microbial cells simple, but biologically relevant model systems to address the mechanisms behind the amyloid formation and for the rapid screening of therapeutic drugs. Interestingly, microbial organisms also exploit the structural principles behind amyloid formation for functional purposes such as adhesion or cytotoxicity.
Since the first edition of this Research Topic was published, new approaches for recombinant protein production in microbial hosts have been designed, a number of structures of pathogenic and non-pathogenic protein aggregates have been determined, bacterial prions have been discovered, therapeutically active protein aggregates have been developed and new computational tools to predict aggregation have been evolved, making a second edition necessary to cover these advances.
In this Research Topic we encourage submissions of original research articles, reviews, mini-reviews, methods articles, hypothesis and theory articles and technology reports that make a substantial and updated contribution to our understanding of protein aggregation in microbial cells. We, therefore, welcome work on, but not limited, to the following topics:
- Protein aggregation in microbial protein production.
- Microbial proteostasis.
- Conformational and functional properties of microbial protein aggregates.
- Use of microbial protein aggregates for applied purposes.
- Microbial amyloids and prions, function and structure.
- Microbes to identify anti-aggregational drugs.
- Computational and biophysics studies on microbial protein aggregation.
Following the success of this Research Topic, we are happy to launch a second edition of the project in which we extend the scope of the issue to the study of the phenomenon of protein aggregation in other microorganisms, in addition to bacteria.
Typically, only folded and soluble proteins are functional. Protein folding and solubility are controlled genetically, transcriptionally, and at the protein sequence and structural level. In addition, a well-conserved cellular machinery assists the folding of polypeptides and preserves proteostasis. When these redundant protective strategies are overcome, misfolded proteins are recruited into aggregates.
Recombinant protein production is an essential tool for the biotechnology industry and also supports expanding areas of basic and biomedical research, including structural genomics and proteomics. Many recombinant polypeptides produced in microbial hosts undergo irregular or incomplete folding processes that usually result in their accumulation as insoluble aggregates. The solubility of microbially produced proteins is of major concern in the production of life-saving protein therapeutics and strategies aimed to improve it are needed.
The presence of a fraction of molecules in a native-like structure in microbial aggregates endorses them with a degree of biological activity, a property that in recent years that can be exploited for applied purposes.
The protein embedded in microbial deposits resembles the amyloid fibrils characteristic of several human neurodegenerative diseases. This makes microbial cells simple, but biologically relevant model systems to address the mechanisms behind the amyloid formation and for the rapid screening of therapeutic drugs. Interestingly, microbial organisms also exploit the structural principles behind amyloid formation for functional purposes such as adhesion or cytotoxicity.
Since the first edition of this Research Topic was published, new approaches for recombinant protein production in microbial hosts have been designed, a number of structures of pathogenic and non-pathogenic protein aggregates have been determined, bacterial prions have been discovered, therapeutically active protein aggregates have been developed and new computational tools to predict aggregation have been evolved, making a second edition necessary to cover these advances.
In this Research Topic we encourage submissions of original research articles, reviews, mini-reviews, methods articles, hypothesis and theory articles and technology reports that make a substantial and updated contribution to our understanding of protein aggregation in microbial cells. We, therefore, welcome work on, but not limited, to the following topics:
- Protein aggregation in microbial protein production.
- Microbial proteostasis.
- Conformational and functional properties of microbial protein aggregates.
- Use of microbial protein aggregates for applied purposes.
- Microbial amyloids and prions, function and structure.
- Microbes to identify anti-aggregational drugs.
- Computational and biophysics studies on microbial protein aggregation.
