High-Level Expression of Recombinant Bovine Lactoferrin in Pichia pastoris with Antimicrobial Activity

Iglesias-Figueroa, Blanca Flor; Valdiviezo-Godina, Norberto; Siqueiros-Cendón, Tania; Sinagawa-García, Sugey Ramona; Arévalo-Gallegos, Sigifredo; Rascón-Cruz, Quintín

doi:10.3390/ijms17060902

Cited by 34 publications

(26 citation statements)

References 45 publications

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“…Concerning this, Lf from different origins, mainly from human and bovine, but also from camel, buffalo, and other animals, has been obtained from milk and colostrum. To have a better quality and production of Lf, since 25 years ago Lf has been cloned in different vectors and expressed overall in eukaryotic systems which can glycosylate it, such as yeasts and fungi [154][155][156]. From these organisms, Lf has been highly purified as a recombinant protein and its biological role, mainly antibacterial, has been confirmed.…”

Section: High-scale Production Of Lactoferrinmentioning

confidence: 99%

“…From these organisms, Lf has been highly purified as a recombinant protein and its biological role, mainly antibacterial, has been confirmed. In addition, human Lf has been cloned in transgenic cows and plants [156][157][158][159]. Interestingly, recombinant hLf expressed in cows enhanced systematic and intestinal immune responses in piglets, used as a model of infants [160].…”

Section: High-scale Production Of Lactoferrinmentioning

confidence: 99%

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Lactoferrin in the Battle against Intestinal Parasites: A Review

León-Sicairos¹,

Ordaz-Pichardo²,

Carrero³

et al. 2017

Natural Remedies in the Fight Against Parasites

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Lactoferrin is an iron-binding glycoprotein of the innate immune system, which is present in some mammalian fluids and secreted into the mucosae; it is also produced by the secondary granules of the polymorphonuclear neutrophils and secreted at infection sites. Lactoferricins (Lfcins) are peptides derived from the N-terminus of Lf. Lf avoids the iron availability to parasites in the body fluids due to its high avidity for iron, maintaining together with transferrin the free-iron concentration in about 10 −18 M, which is too low to support the pathogenic invader survival. Intestinal parasitic diseases affect people worldwide, mainly in developing countries with poor hygienic conditions; for example, parasites such as Entamoeba histolytica, Giardia intestinalis, and Cryptosporidium parvum infect the human intestine when are orally ingested as cysts. Human and bovine Lf have been found parasiticidal in experiments in vitro and in animal models. Interestingly, Lf synergizes with metronidazole, the main drug used against E. histolytica and G. intestinalis. The aim of this chapter is to show the benefits of using Lf and Lfcins against intestinal parasitic diseases.

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Section: High-scale Production Of Lactoferrinmentioning

confidence: 99%

Section: High-scale Production Of Lactoferrinmentioning

confidence: 99%

Lactoferrin in the Battle against Intestinal Parasites: A Review

León-Sicairos¹,

Ordaz-Pichardo²,

Carrero³

et al. 2017

Natural Remedies in the Fight Against Parasites

View full text Add to dashboard Cite

show abstract

“…It is characterized by its strong regulator promoter, rapid growth and easy genetic manipulation. Moreover, it has the ability to perform eukaryotic post‐translational modifications (Iglesias‐Figueroa et al., ). Given that the production of recombinant IGF‐1 and IGF‐2 is critical for investigating the physiological functions and potential application of these hormones in tongue sole, the aims of the present study were (1) to obtain recombinant proteins of tongue sole IGF‐1 and IGF‐2 expressed in P. pastoris and (2) to examine the comparative activity of IGF‐1 and IGF‐2 in the tongue sole.…”

Section: Introductionmentioning

confidence: 99%

Recombinant expression and comparative bioactivity of tongue sole insulin-like growth factor (IGF)-1 and IGF-2 in Pichia pastoris

Wang

Liu

et al. 2018

Aquac Res

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Insulin-like growth factor (IGF) plays a key role in the complex system that regulates bony fish growth, differentiation, and reproduction. In the current study, recombinant tongue sole IGF-1 and IGF-2 were obtained using the Pichia pastoris expression system and their comparative bioactivities were investigated. Tricine-SDS-PAGE and western blot analysis showed that the recombinant tongue sole IGFs were secreted into the culture medium and had a molecular weight of 8.7 kDa. The optimal incubation time and pH for recombinant expression of IGFs were 36 hr and 5.0 respectively. Functional analysis demonstrated that both recombinant tongue sole IGF-1 and IGF-2 significantly promoted cell proliferation of MFC-7 in vitro. In addition, the recombinant tongue sole IGF-1 and IGF-2 proteins could suppress hepatic mRNA levels of igf-1 and igf-2 in vitro, which showed that they have similar physiological functions. Taken together, the biologically active recombinant tongue sole IGF-I and IGF-II proteins will allow us to further investigate their physiological roles in growth regulation of this species. Furthermore, the present results also hinted at the potential application of these two recombinant IGF-I and IGF-II proteins into the tongue sole farming industry. K E Y W O R D SCynoglossus semilaevis, insulin-like growth factor, Pichia pastoris, recombinant expression

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“…Alcohol oxidase 1 promoter (AOX1) is one of the most widely utilized among all the available promoters for P. pastoris 12, 13. It is tightly repressed during yeast growth on glucose or ethanol, but effectively induced by methanol, 14 which, however, is toxic at high levels 15 .…”

Section: Introductionmentioning

confidence: 99%

Cultivation of Pichia pastoris carrying the scFv anti LDL (−) antibody fragment. Effect of preculture carbon source

Arias

Marques

Malpiedi

et al. 2017

Brazilian Journal of Microbiology

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Antibodies and antibody fragments are nowadays among the most important biotechnological products, and Pichia pastoris is one of the most important vectors to produce them as well as other recombinant proteins. The conditions to effectively cultivate a P. pastoris strain previously genetically modified to produce the single-chain variable fragment anti low density lipoprotein (−) under the control of the alcohol oxidase promoter have been investigated in this study. In particular, it was evaluated if, and eventually how, the carbon source (glucose or glycerol) used in the preculture preceding cryopreservation in 20% glycerol influences both cell and antibody fragment productions either in flasks or in bioreactor. Although in flasks the volumetric productivity of the antibody fragment secreted by cells precultured, cryopreserved and reactivated in glycerol was 42.9% higher compared with cells precultured in glucose, the use of glycerol in bioreactor led to a remarkable shortening of the lag phase, thereby increasing it by no less than thrice compared to flasks. These results are quite promising in comparison with those reported in the literature for possible future industrial applications of this cultivation, taking into account that the overall process time was reduced by around 8 h.

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High-Level Expression of Recombinant Bovine Lactoferrin in Pichia pastoris with Antimicrobial Activity

Cited by 34 publications

References 45 publications

Lactoferrin in the Battle against Intestinal Parasites: A Review

Lactoferrin in the Battle against Intestinal Parasites: A Review

Recombinant expression and comparative bioactivity of tongue sole insulin-like growth factor (IGF)-1 and IGF-2 in Pichia pastoris

Cultivation of Pichia pastoris carrying the scFv anti LDL (−) antibody fragment. Effect of preculture carbon source

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