Use of Murine Models To Detect the Allergenicity of Genetically Modified Lactococcus lactis NZ9000/pNZPNK

Chiang, Shen-Shih; Liu, Chin-Feng; Ku, Ting-Wei; Mau, Jeng‐Leun; Lin, Hsin-Tang; Pan, Tzu‐Ming

doi:10.1021/jf104656m

Cited by 6 publications

(6 citation statements)

References 33 publications

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“…We identified only 2 studies (1 observational and 1 quasi-experimental) that involved actual ingestion of a GM product. 26 106,111,113,114,117,118 These animal studies were conducted in rat or mouse models and involved ingestion of a GM product and assessment of various safety and toxicity parameters, including measurement of serologic allergic or immunologic markers.…”

Section: Resultsmentioning

confidence: 99%

The allergenicity of genetically modified foods from genetically engineered crops

Dunn

Vicini

Glenn

et al. 2017

Annals of Allergy, Asthma & Immunology

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INSTRUCTIONSCredit can now be obtained, free for a limited time, by reading the review article and completing all activity components. Please note the instructions listed below:Review the target audience, learning objectives and all disclosures.Complete the pre-test.Read the article and reflect on all content as to how it may be applicable to your practice.Complete the post-test/evaluation and claim credit earned. At this time, physicians will have earned up to 1.0 AMA PRA Category 1 Credit TM . Minimum passing score on the post-test is 70%. Overall Purpose Participants will be able to demonstrate increased knowledge of the clinical treatment of allergy/asthma/immunology and how new information can be applied to their own practices. Learning ObjectivesAt the conclusion of this activity, participants should be able to:Recognize the testing and safety features that genetically modified products are subject to in determining their allergenicity Identify the basis and rationale for genetic modification Review the evidence regarding genetically modified products and any association with food allergy Release position to control or influence the content of an activity must disclose all relevant financial relationships with any commercial interest that have occurred within the past 12 months. All identified conflicts of interest must be resolved and the educational content thoroughly vetted for fair balance, scientific objectivity, and appropriateness of patient care recommendations. It is required that disclosure be provided to the learners prior to the start of the activity. Individuals with no relevant financial relationships must also inform the learners that no relevant financial relationships exist. Learners must also be informed when off-label, experimental/ investigational uses of drugs or devices are discussed in an educational activity or included in related materials. Disclosure in no way implies that the information presented is biased or of lesser quality. It is incumbent upon course participants to be aware of these factors in interpreting the program contents and evaluating recommendations. Moreover, expressed views do not necessarily reflect the opinions of ACAAI. All identified conflicts of interest have been resolved.

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Section: Resultsmentioning

confidence: 99%

The allergenicity of genetically modified foods from genetically engineered crops

Dunn

Vicini

Glenn

et al. 2017

Annals of Allergy, Asthma & Immunology

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“…Nattokinase is expressed in B. subtilis [ 14 ] and E. coli [ 15 , 16 ]; however, complicated purification processes must be performed before the expressed enzyme can be applied for clinical use. Although the intracellular [ 17 ] and intercellular [ 18 ] expression of Nattokinase in L. lactis was studied, the recombinant strains contained antibiotic (chloramphenicol and erythromycin, respectively) resistance genes and thus, do not adhere to the real “food-grade” definition [ 5 ]. Without using antibiotics, Subtilisin QK-2 was expressed in L. lactis NZ3900 (pRF02), which was selected by the complementation of the lacF gene in this study, which allowed it to meet the food-grade requirements.…”

Section: Discussionmentioning

confidence: 99%

Subtilisin QK-2: secretory expression in Lactococcus lactis and surface display onto gram-positive enhancer matrix (GEM) particles

et al. 2016

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BackgroundPurified from the supernatant of Bacillus subtilis QK02 culture broth, Subtilisin QK-2 is a type of effective thrombolytic reagent that has great exploitable potential. However, the unbearable flavor that occurs with fermentation and the complicated methods that are required to obtain pure products limit the application of this enzyme. Lactic acid bacteria (LAB)-based delivery vehicles are promising as cheap and safe options for medicinal compounds. The secretory expression and surface display using LAB may popularize Subtilisin QK-2 more easily and conveniently with minimal adverse effects.ResultsSubtilisin QK-2 was expressed successfully in two forms using lactic acid bacteria. For the secretory expression in Lactococcus lactis, Subtilisin QK-2 was efficiently secreted into the culture using the promoter PnisA and signal peptide SPUsp. The expression levels were not different in L. lactis NZ9000 and NZ3900 without the effect of different selection markers. However, leaky expression was only detected in L. lactis NZ3900. The biological activity of this secreted Subtilisin QK-2 was enhanced by modulating the pH of medium to slightly alkaline during induction and by codon optimization of either the entire gene sequence (qk′) or only the propeptide gene sequence (qkpro′). For surface display onto gram-positive enhancer matrix (GEM) particles, n LysM repeats from the C-terminal region of the major autolysin AcmA of L. lactis were fused to either the C-terminus (n = 1, 3, 5) or the N-terminus (n = 1) of the Subtilisin QK-2. These fusion proteins were secreted into the culture medium, and the QK-3LysM was able to bind to the surface of various LAB GEM particles without a loss of fibrinolytic activity. Furthermore, the binding capacity significantly increased with a higher concentration of QK-3LysM. Compared to the free-form Subtilisin QK-2, the QK-3LysM displayed on the surface of GEM particles was more stable in the simulated gastric juice.ConclusionsCombined with the safety and popularity of LAB, Subtilisin QK-2 may be easily applied worldwide to prevent and control thrombosis diseases.Electronic supplementary materialThe online version of this article (doi:10.1186/s12934-016-0478-7) contains supplementary material, which is available to authorized users.

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“…The signal peptide is present to enable the normal secretion of NK into the extracellular compartment, while the lead peptide helps NK to fold normally into an active conformation. 50 The intra-molecular chaperone (IMC) conveys structural information to the subtilisin structural domain during the folding of the precursor and helps the protein to fold…”

Section: Process and Mechanisms Of Nk Synthesismentioning

confidence: 99%

Microbial nattokinase: from synthesis to potential application

et al. 2023

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Use of Murine Models To Detect the Allergenicity of Genetically Modified Lactococcus lactis NZ9000/pNZPNK

Cited by 6 publications

References 33 publications

The allergenicity of genetically modified foods from genetically engineered crops

The allergenicity of genetically modified foods from genetically engineered crops

Subtilisin QK-2: secretory expression in Lactococcus lactis and surface display onto gram-positive enhancer matrix (GEM) particles

Microbial nattokinase: from synthesis to potential application

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