The future of recombinant host defense peptides

Roca-Pinilla, Ramon; Lisowski, Leszek; Arı́s, Anna; García‐Fruitós, Elena

doi:10.1186/s12934-022-01991-2

Cited by 3 publications

(3 citation statements)

References 158 publications

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“…Antimicrobial peptides (AMPs) play a role in host defense and are promising therapeutic agents [ 18 ]. AMPs are small, making them easily degradable, and because of their antimicrobial properties, they are toxic to producer bacteria, hindering the production of recombinant AMPs [ 19 ]. Previous works have explored the activity of AMPs, such as defensin-5, lingual antimicrobial peptides [ 17 ], and multiple antimicrobial protein domains [ 20 ] in the formation of inclusion bodies (IBs).…”

Section: Introductionmentioning

confidence: 99%

Immunomodulation Evidence of Nanostructured Recombinant Proteins in Salmonid Cells

Torrealba,

López,

Zelada

et al. 2024

Animals

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Recent studies have demonstrated that immune-related recombinant proteins can enhance immune function, increasing host survival against infectious diseases in salmonids. This research evaluated inclusion bodies (IBs) of antimicrobial peptides (CAMPIB and HAMPIB) and a cytokine (IL1βIB and TNFαIB) as potential immunostimulants in farmed salmonids. For this purpose, we produced five IBs (including iRFPIB as a control), and we evaluated their ability to modulate immune marker gene expression of three IBs in the RTS11 cell line by RT–qPCR. Additionally, we characterized the scale-up of IBs production by comparing two different scale systems. The results showed that CAMPIB can increase the upregulation of tnfα, il1β, il8, and il10, HAMPIB significantly increases the upregulation of tnfα, inos, and il10, and IL1βIB significantly upregulated the expression of tnfα, il1β, and cox2. A comparison of IL1βIB production showed that the yield was greater in shake flasks than in bioreactors (39 ± 1.15 mg/L and 14.5 ± 4.08 mg/L), and larger nanoparticles were produced in shake flasks (540 ± 129 nm and 427 ± 134 nm, p < 0.0001, respectively). However, compared with its shake flask counterpart, the IL1βIB produced in a bioreactor has an increased immunomodulatory ability. Further studies are needed to understand the immune response pathways activated by IBs and the optimal production conditions in bioreactors, such as a defined medium, fed-batch production, and mechanical bacterial lysis, to increase yield.

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Section: Introductionmentioning

confidence: 99%

Immunomodulation Evidence of Nanostructured Recombinant Proteins in Salmonid Cells

Torrealba,

López,

Zelada

et al. 2024

Animals

Self Cite

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“…Natural biological defense factors (defensins) are distributed in almost all biological groups [1], mainly through physical binding with virus coat proteins, causing virus inactivation, making it difficult for microorganisms to develop resistance [2]. Most defense factors can be developed and produced through genetic engineering and protein recombination technology [3]. There are many naturally occurring proteins with biological defense functions in mammalian milk, which form part of the defense mechanism mediated by the mother to the offspring through milk [4].…”

Section: Introductionmentioning

confidence: 99%

Safety Evaluation of Recombinant Bovine Lactoferrin as a Novel Biomaterial

Sun,

Zhang,

Wang

et al. 2024

IJBECS

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This study introduces the physical principles and safety evaluation of recombinant bovine lactoferrin (fusion factor) as an innovative biomaterial. Fusion factor is a recombinant lactoferrin expressed by fusing lactoferrin, which has natural biological defense function, with other peptide segments through sequence optimization. It is named fusion factor. Its molecular weight is about 36kDa, which is much greater than the 1kDa molecular weight limit of macromolecular transdermal absorption, so it is not absorbed when used externally on the epithelial mucosa. The lactoferrin based biological defense functional peptide segment in the fusion factor can neutralize the virus by binding to viral protein nucleic acid through the physical action of charge adsorption, and can also compete with cell receptors to inhibit virus infection in cells. The molar ratio of the transmembrane peptide (Pep-1) fragment to the carrier protein is 1:1, so only the transport protein is anchored to the cell surface, forming a physical isolation protein protective wall against viruses and bacteria, without penetrating the cell or damaging the cell membrane. The fusion factor and its derived vaginal bacteria blocking gel have no significant toxicity, sensitization, anaphylaxis or delayed hypersensitivity in vitro cell experiments, in vivo animal experiments and clinical observation tests, and have no side effects with highly safety.

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“…Additionally, AMPs demonstrate rapid germ-killing abilities and low bactericidal concentrations, making them effective even against traditional antibiotic-resistant strains [18]. Despite these promising characteristics, the widespread clinical use of AMPs remains limited due to concerns about low stability, potential toxicity, and high production costs [19]. The oral delivery of AMPs to the gut poses particular challenges, as these molecules are susceptible to degradation before reaching the site of infection in sufficient quantities, leading to treatment failure [20].…”

Section: Introductionmentioning

confidence: 99%

Novel Genetically Engineered Probiotics for Targeted Elimination of Pseudomonas aeruginosa in Intestinal Colonization

Kim,

Jang,

Jung

et al. 2023

Biomedicines

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The intestinal carriage rates of Pseudomonas aeruginosa are notably elevated in immunosuppressed individuals and hospitalized patients, increasing the risk of infection and antibiotic-associated diarrhea. A potential solution to this issue lies in autonomous antibacterial therapy, remaining inactive until a pathogen is detected, and releasing antibacterial compounds on demand to eliminate the pathogen. This study focuses on the development of genetically engineered probiotics capable of detecting and eradicating P. aeruginosa by producing and secreting PA2-GNU7, a P. aeruginosa-selective antimicrobial peptide (AMP), triggered by the presence of P. aeruginosa quorum-sensing molecule N-(3-oxododecanoyl)-L-homoserine lactone (3OC12HSL). To achieve this goal, plasmid-based systems were constructed to produce AMPs in response to 3OC12HSL and secrete them into the extracellular medium using either the microcin V secretion system or YebF as a carrier protein. Following the transfer of these plasmid-based systems to Escherichia coli Nissle 1917 (EcN), we successfully demonstrated the ability of the engineered EcN to express and secrete PA2-GNU7, leading to the inhibition of P. aeruginosa growth in vitro. In addition, in a mouse model of intestinal P. aeruginosa colonization, the administration of engineered EcN resulted in reduced levels of P. aeruginosa in both the feces and the colon. These findings suggest that engineered EcN holds promise as a potential option for combating intestinal P. aeruginosa colonization, thus mitigating the risk of future endogenous infections in vulnerable patients.

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The future of recombinant host defense peptides

Cited by 3 publications

References 158 publications

Immunomodulation Evidence of Nanostructured Recombinant Proteins in Salmonid Cells

Immunomodulation Evidence of Nanostructured Recombinant Proteins in Salmonid Cells

Safety Evaluation of Recombinant Bovine Lactoferrin as a Novel Biomaterial

Novel Genetically Engineered Probiotics for Targeted Elimination of Pseudomonas aeruginosa in Intestinal Colonization

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