Encapsulins: Structure, Properties, and Biotechnological Applications

Chmelyuk, Nelly S.; Oda, Vera V.; Габашвили, А. Н.; Abakumov, Maxim A.

doi:10.1134/s0006297923010042

Cited by 10 publications

(4 citation statements)

References 106 publications

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“…Based on sequence analyses, four families (Families 1-4) of encapsulins have been identified and the cargos they encapsulate are known in at least 11 archaea and eubacteria species. The cargos include ferritin-like proteins (Flp), DyP-type peroxidases (DyP), iron-mineralizing encapsulin-associated Firmicute (IMEF), and FolB that is involved in biosynthesis of folate (vitamin B9), each encoded by plasmid-borne encapsulin operons [26][27][28]. Although specific functions of encapsulins in prokaryote biology are still being determined, knockout mutants of Flp-associated encapsulin in Mycobacterium xanthus have shown increased susceptibility to H 2 O 2 -induced oxidative stress.…”

Section: Bt075 Is Structurally Similar To Encapsulin Shell Proteinsmentioning

confidence: 99%

The Parasporal Body of Bacillus thuringiensis subsp. israelensis: A Unique Phage Capsid-Associated Prokaryotic Insecticidal Organelle

Rudd,

Miranda,

Curtis

et al. 2023

Biology

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The three most important commercial bacterial insecticides are all derived from subspecies of Bacillus thuringiensis (Bt). Specifically, Bt subsp. kurstaki (Btk) and Bt subsp. aizawai (Bta) are used to control larval lepidopteran pests. The third, Bt subsp. israelensis (Bti), is primarily used to control mosquito and blackfly larvae. All three subspecies produce a parasporal body (PB) during sporulation. The PB is composed of insecticidal proteins that damage the midgut epithelium, initiating a complex process that results in the death of the insect. Among these three subspecies of Bt, Bti is unique as it produces the most complex PB consisting of three compartments. Each compartment is bound by a multilaminar fibrous matrix (MFM). Two compartments contain one protein each, Cry11Aa1 and Cyt1Aa1, while the third contains two, Cry4Aa1/Cry4Ba1. Each compartment is packaged independently before coalescing into the mature spherical PB held together by additional layers of the MFM. This distinctive packaging process is unparalleled among known bacterial organelles, although the underlying molecular biology is yet to be determined. Here, we present structural and molecular evidence that the MFM has a hexagonal pattern to which Bti proteins Bt152 and Bt075 bind. Bt152 binds to a defined spot on the MFM during the development of each compartment, yet its function remains unknown. Bt075 appears to be derived from a bacteriophage major capsid protein (MCP), and though its sequence has markedly diverged, it shares striking 3-D structural similarity to the Escherichia coli phage HK97 Head 1 capsid protein. Both proteins are encoded on Bti’s pBtoxis plasmid. Additionally, we have also identified a six-amino acid motif that appears to be part of a novel molecular process responsible for targeting the Cry and Cyt proteins to their cytoplasmic compartments. This paper describes several previously unknown features of the Bti organelle, representing a first step to understanding the biology of a unique process of sorting and packaging of proteins into PBs. The insights from this research suggest a potential for future applications in nanotechnology.

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Section: Bt075 Is Structurally Similar To Encapsulin Shell Proteinsmentioning

confidence: 99%

The Parasporal Body of Bacillus thuringiensis subsp. israelensis: A Unique Phage Capsid-Associated Prokaryotic Insecticidal Organelle

Rudd,

Miranda,

Curtis

et al. 2023

Biology

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“…Since then, encapsulins have been described in various bacteria including Mycobacterium leprae (Winter et al 1995 ), M. tuberculosis (Rosenkrands et al 1998 ), Thermotoga maritima (Hicks et al 1998 ), Streptomyces coelicolor (Kawamoto et al 2001 ), and Quasibacillus thermotolerans (Giessen et al 2019 ). Furthermore, several authors have highlighted the nature, structural features, and the role of these bacterial nanocompartments (Almeida et al 2021 ; Andreas and Giessen 2021 ; Chmelyuk et al 2023 ; Giessen 2022 ; Giessen and Silver 2016 ; Giessen and Silver 2017 ; Jones and Giessen 2021 ; McDowell and Hoiczyk 2022 ; Wiryaman and Toor 2022 ).…”

Section: Introductionmentioning

confidence: 99%

Linocin M18 protein from the insect pathogenic bacterium Brevibacillus laterosporus isolates

Babar

Glare

Hampton

et al. 2023

Appl Microbiol Biotechnol

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Brevibacillus laterosporus (Bl) is a Gram-positive and spore-forming bacterium. Insect pathogenic strains have been characterised in New Zealand, and two isolates, Bl 1821L and Bl 1951, are under development for use in biopesticides. However, growth in culture is sometimes disrupted, affecting mass production. Based on previous work, it was hypothesised that Tectiviridae phages might be implicated. While investigating the cause of the disrupted growth, electron micrographs of crude lysates showed structural components of putative phages including capsid and tail-like structures. Sucrose density gradient purification yielded a putative self-killing protein of ~30 kDa. N-terminal sequencing of the ~30 kDa protein identified matches to a predicted 25 kDa hypothetical and a 31.4 kDa putative encapsulating protein homologs, with the genes encoding each protein adjacent in the genomes. BLASTp analysis of the homologs of 31.4 kDa amino acid sequences shared 98.6% amino acid identity to the Linocin M18 bacteriocin family protein of Brevibacterium sp. JNUCC-42. Bioinformatic tools including AMPA and CellPPD defined that the bactericidal potential originated from a putative encapsulating protein. Antagonistic activity of the ~30 kDa encapsulating protein of Bl 1821L and Bl 1951during growth in broth exhibited bacterial autolytic activity. LIVE/DEAD staining of Bl 1821L cells after treatment with the ~30 kDa encapsulating protein of Bl 1821L substantiated the findings by showing 58.8% cells with the compromised cell membranes as compared to 37.5% cells in the control. Furthermore, antibacterial activity of the identified proteins of Bl 1821L was validated through gene expression in a Gram-positive bacterium Bacillus subtilis WB800N. Key Points • Gene encoding the 31.4 kDa antibacterial Linocin M18 protein was identified • It defined the autocidal activity of Linocin M18 (encapsulating) protein • Identified the possible killing mechanism of the encapsulins

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“…The two most prominent types of protein compartments found in prokaryotes are bacterial microcompartments (BMCs) and encapsulins [6][7][8] . While BMCs sequester short metabolic pathways and are involved in carbon fixation [9][10][11] and various catabolic processes [12][13][14] , encapsulin function is more varied and usually relies on encapsulating a single type of cargo enzyme 7,15,16 . Encapsulins have been shown to be involved in iron storage 17,18 , sulfur metabolism 19,20 , and oxidative stress response 21,22 .…”

Section: Introductionmentioning

confidence: 99%

Structural basis for peroxidase encapsulation in a protein nanocompartment

Jones,

Andreas,

Giessen

2023

Preprint

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Encapsulins are self-assembling protein nanocompartments capable of selectively encapsulating dedicated cargo proteins, including enzymes involved in iron storage, sulfur metabolism, and stress resistance. They represent a unique compartmentalization strategy used by many pathogens to facilitate specialized metabolic capabilities. Encapsulation is mediated by specific cargo protein motifs known as targeting peptides (TPs), though the structural basis for encapsulation of the largest encapsulin cargo class, dye-decolorizing peroxidases (DyPs), is currently unknown. Here, we characterize a DyP-containing encapsulin from the enterobacterial pathogenKlebsiella pneumoniae. By combining cryo-electron microscopy with TP mutagenesis, we elucidate the molecular basis for cargo encapsulation. TP binding is mediated by cooperative hydrophobic and ionic interactions as well as shape complementarity. Our results expand the molecular understanding of enzyme encapsulation inside protein nanocompartments and lay the foundation for rationally modulating encapsulin cargo loading for biomedical and biotechnological applications.

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Encapsulins: Structure, Properties, and Biotechnological Applications

Cited by 10 publications

References 106 publications

The Parasporal Body of Bacillus thuringiensis subsp. israelensis: A Unique Phage Capsid-Associated Prokaryotic Insecticidal Organelle

The Parasporal Body of Bacillus thuringiensis subsp. israelensis: A Unique Phage Capsid-Associated Prokaryotic Insecticidal Organelle

Linocin M18 protein from the insect pathogenic bacterium Brevibacillus laterosporus isolates

Structural basis for peroxidase encapsulation in a protein nanocompartment

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