کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8359423 | 1542292 | 2018 | 27 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A systematic analysis of the expression of the anti-HIV VRC01 antibody in Pichia pastoris through signal peptide optimization
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کلمات کلیدی
BNAbsYPdVRC01NourseothricinAlcohol oxidase 1AOX1BMMYBMGYHEKαTα-MFIgGα-Amylase - α-آمیلازSerum albumin - آلبومین سرم alkaline phosphate - آلکالن فسفاتBroadly neutralizing antibodies - آنتی بادی های ضد عفونی به طور گسترده ایimmunoglobulin G - ایمونوگلوبولین Ginvertase - اینورتازInulinase - اینولینازbroadly neutralizing antibody - به طور گسترده ای آنتی بادی خنثی می کندYeast peptone dextrose - دکس استراز پپتون مخمرα-mating factor - ضریب همبستگی αlysozyme - لیزوزیم Signal peptide - پپتید سیگنالhuman embryonic kidney - کلیه جنین انسانGlucoamylase - گلوکومیلاز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: A systematic analysis of the expression of the anti-HIV VRC01 antibody in Pichia pastoris through signal peptide optimization A systematic analysis of the expression of the anti-HIV VRC01 antibody in Pichia pastoris through signal peptide optimization](/preview/png/8359423.png)
چکیده انگلیسی
Pichia pastoris (Komagataella phaffi) has been used for recombinant protein production for over 30 years with over 5000 proteins reported to date. However, yields of antibody are generally low. We have evaluated the effect of secretion signal peptides on the production of a broadly neutralizing antibody (VRC01) to increase yield. Eleven different signal peptides, including the murine IgG1 signal peptide, were combinatorially evaluated for their effect on antibody titer. Strains using different combinations of signal peptides were identified that secreted approximately 2-7 fold higher levels of VRC01 than the previous best secretor, with the highest yield of 6.50â¯mgâ¯Lâ1 in shake flask expression. Interestingly it was determined that the highest yields were achieved when the murine IgG1 signal peptide was fused to the light chain, with several different signal peptides leading to high yield when fused to the heavy chain. Finally, we have evaluated the effect of using a 2A signal peptide to create a bicistronic vector in the attempt to reduce burden and increase transformation efficiency, but found it to give reduced yields compared to using two independent vectors.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 149, September 2018, Pages 43-50
Journal: Protein Expression and Purification - Volume 149, September 2018, Pages 43-50
نویسندگان
Rochelle Aw, Paul F. McKay, Robin J. Shattock, Karen M. Polizzi,