RRJoBI

Recombinant Protein Manufacturing Using Actinomycetes as Host Cells

[{“box”:0,”content”:”

n

Year : August 28, 2022 | Volume : 09 | Issue : 02 | Page : 23-

n

n

n

n

n

n

By

n

[foreach 286]

Amaan Khan
  • [/foreach]

    n

    n

      [foreach 286] [if 1175 not_equal=””]n

    1. Researcher,Department of medical science and technology, Bharat Ayurved Medical College & Hospital Research Centre, Muzaffarnagar,Uttar Pradesh,India
    2. n [/if 1175][/foreach]

    n

    n

    Abstract

    n Actinobacteria are highly sought-after for use as cell factories or bioreactors in the pharmaceutical, agricultural, industrial, and environmental sectors. The commercial production of these proteins as recombinants and the biochemical and structural characterization of key proteins have been made possible by the genome sequencing of numerous species of actinomycetes. In this regard, better expression vectors that may be used with actinomycetes are required. As discussed in this article, recent developments in gene expression systems, knowledge of the intracellular environment, and identification and characterization of plasmids have made it possible to create workable recombinant expression systems in actinomycetes.n

    n

    n

    n

    Keywords: Actinomycetes, recombinant protein, plasmid, yeast, promoter, gene

    n [if 424 equals=”Regular Issue”][This article belongs to Research & Reviews: A Journal of Bioinformatics(rrjobi)]n

    n

    [/if 424][if 424 equals=”Special Issue”][This article belongs to Special Issue under section in Research & Reviews: A Journal of Bioinformatics(rrjobi)][/if 424][if 424 equals=”Conference”]This article belongs to Conference [/if 424]

    n

    n

    n

    How to cite this article:n Amaan Khan Recombinant Protein Manufacturing Using Actinomycetes as Host Cells rrjobi August 28, 2022; 09:23-

    n

    How to cite this URL: Amaan Khan Recombinant Protein Manufacturing Using Actinomycetes as Host Cells rrjobi August 28, 2022n {cited August 28, 2022};09:23-. Available from: https://journals.stmjournals.com/rrjobi/article=August 28, 2022/view=91698/

    n


    n

    Full Text

    n [if 992 equals=”Open Access”] nhttps://storage.googleapis.com/journals-stmjournals-com-wp-media-to-gcp-offload/2023/01/627199a3-recombinant-protein-rrjobi.pdf [else]nnvar fieldValue = “[user_role]”;nif (fieldValue == ‘indexingbodies’) {n document.write(‘https://storage.googleapis.com/journals-stmjournals-com-wp-media-to-gcp-offload/2023/01/627199a3-recombinant-protein-rrjobi.pdf’);n }nelse if (fieldValue == ‘administrator’) { document.write(‘https://storage.googleapis.com/journals-stmjournals-com-wp-media-to-gcp-offload/2023/01/627199a3-recombinant-protein-rrjobi.pdf’); }n else { document.write(‘ ‘); }nn[/if 992]nn [if 379 not_equal=””]n

    Browse Figures

    n

    n

    [foreach 379]n

    n [/foreach]n

    nn

    n

    n [/if 379]n

    n

    n Referencesn

    n [if 1104 equals=””]n

    1. Kashima Y, Udaka S. High-level production of hyperthermophilic cellulase in the Bacillus brevis expression and secretion system. Biosci Biotechnol Biochem. 2004;68:235–237.
    2. Udaka S, Yamagata HY. Protein secretion in Bacillus brevis. Antonie Van Leeuwenhoek. 1993;64:137–143.
    3. Lam KHE, Chow KC, Wong WKR. Construction of an efficient Bacillus subtilis system for extracellular production of heterologous proteins. J Biotechnol. 1998;63:167–177.
    4. Loir YL, Azevedo V, Oliveira SC, Freitas DA, Miyoshi A, Bermúdez-Humarán LG, Nouaille S, Ribeiro LA, Leclercq S, Gabriel JE, Guimaraes VD, Oliveira MN, Charlier C, Gautier M, Langella P. Protein secretion in Lactococcus lactis: an efficient way to increase the overall heterologous protein production. Microb Cell Fact. 2005;4:2.
    5. Kuipers OP, de Ruyter PG, Kleerebezem M, de Vos WM. Controlled overproduction of proteins by lactic acid bacteria. Trends Biotechnol. 1997;15:135–140.
    6. Billman-Jacobe H. Expression in bacteria other than Escherichia coli. Curr Opin Biotechnol. 1996;7:500–504.
    7. Brooks SA. Appropriate glycosylation of recombinant proteins for human use: implications of choice of expression system. Mol Biotechnol. 2004;28:241–256.
    8. Connell ND. Expression systems for use in actinomycetes and related organisms. Curr Opin Biotechnol. 2001;12:446–449.
    9. Flores FJ, Rincón J, Martin JF. Characterization of the iron-regulated desA promoter of Streptomyces pilosus as a system for controlled gene expression in actinomycetes. Microb Cell Fact. 2003;2:5.
    10. Herai S, Hashimoto Y, Higashibata H, Maseda H, Ikeda H, Omura S, Kobayashi M. Hyper- inducible expression system for streptomycetes. Proc Natl Acad Sci USA. 2004;101:14031–14035.
    11. Nakashima N, Tamura T. A novel system for expressing recombinant proteins over a wide temperature range from 4 to 35 degrees C. Biotechnol Bioeng. 2004;86:136–148.
    12. Nakashima N, Tamura T. Isolation and characterization of a rolling-circle-type plasmid from Rhodococcus erythropolis and application of the plasmid to multiple-recombinant protein expression. Appl Environ Microbiol. 2004;70:5557–5568.
    13. Tokiwa Y, Buenaventurada PC. Degradation of microbial polyesters. Biotechnol Lett. 2004;26:1181–1189.
    14. Weber T, Welzel K, Pelzer S, Vente A, Wohlleben W. Exploiting the genetic potential of polyketide producing streptomycetes. J Biotechnol. 2003;106:221–232.
    15. Komeda H, Hori Y, Kobayashi M, Shimizu S. Transcriptional regulation of the Rhodococcus rhodochrous J1 nitA gene encoding a nitrilase. Proc Natl Acad Sci USA. 1996;93:10572–10577.
    16. Triccas JA, Parish T, Britton WJ, Gicquel B. An inducible expression system permitting the efficient purification of a recombinant antigen from Mycobacterium smegmatis. FEMS Microbiol Lett. 1998;167:151–156.
    17. Enguita FJ, de la Fuente JL, Martín JF, Liras P. An inducible expression system of histidine-tagged proteins in Streptomyces lividans for one-step purification by Ni2+ affinity chromatography. FEMS Microbiol Lett. 1996;137:135–140.
    18. McDaniel R, Ebert-Khosla S, Hopwood DA, Khosla C. Engineered biosynthesis of novel polyketides. Science. 1993;262:1546–1550.
    19. Rowe CJ, Cortés J, Gaisser S, Staunton J, Leadlay PF. Construction of new vectors for high-level expression in actinomycetes. Gene. 1998;216:215–223.
    20. Spratt JM, Britton WJ, Triccas JA. Identification of strong promoter elements of Mycobacterium smegmatis and their utility for foreign gene expression in mycobacteria. FEMS Microbiol Lett. 2003;224:139–142.
    21. Kataoka M, Tatsuta T, Suzuki I, Kosono S, Seki T, Yoshida T. Development of a temperature- inducible expression system for Streptomyces spp. J Bacteriol. 1996;178:5540–5542.
    22. Lim A, Boon C, Dick T. Inducibility of the Streptomyces traRts107-Ptra expression cassette in Mycobacterium smegmatis. Biol Chem. 2000;381:517–519.
    23. Binnie C, Cossar JD, Stewart DIH. Heterologous biopharmaceutical protein expression in Streptomyces. Trends Biotechnol. 1997;15:315–320.
    24. Schmitt-John T, Engels JW. Promoter constructions for efficient secretion expression in Streptomyces lividans. Appl Microbiol Biotechnol. 1992;36:493–498.
    25. Zazopoulos E, Huang K, Staffa A, Liu W, Bachman BO, Nonaka K, Ahlert J, Thorson JS, Shen B, Farnet CM. A genomics-guided approach for discovering and expressing cryptic metabolic pathways. Nat Biotechnol. 2003;21:187–190.
    26. Lammertyn E, Anné J. Modifications of Streptomyces signal peptides and their effects on prior production and secretion. FEMS Microbiol Lett. 1998;160:1–10.
    27. Fornwald JA, Donovan MJ, Geber R, Keller J, Taylor DP, Arcuri EJ, Brawner ME. Soluble forms of the human T cell receptor CD4 are efficiently expressed by Streptomyces lividans. Bio/Technology. 1993;11:1031–1036.
    28. Singer ME, Finnerty WR. Construction of an Eschericha coli-Rhodococcus shuttle vector and plasmid transformation in Rhodococcus spp. J Bacteriol. 1988;170:638–645.
    29. Mujacic M, Cooper KW, Baneyx F. Cold-inducible cloning vectors for low-temperature protein expression in Escherichia coli : application to the production of a toxic and proteolytically sensitive fusion protein. Gene. 1999;238:325–332.
    30. Qing G, Ma LC, Khorchid A, Swapna GVT, Tapas KM, Takayama MM, Xia B, Phadtare S, Ke H, Acton T, Montelione GT, Ikura M, Inouye M. Cold-shock induced high-yield protein production in Escherichia coli. Nat Biotechnol. 2004;22:877–882.
    31. Mitani Y, Meng XY, Kamagata Y, Tamura T. Characterization of LtsA from Rhodococcus erythropolis-an enzyme with glutamine amidotransferase activity. J Bacteriol.

    nn [/if 1104][if 1104 not_equal=””]n

      [foreach 1102]n

    1. [if 1106 equals=””], [/if 1106][if 1106 not_equal=””],[/ifn 1106]
    2. n [/foreach]n

    n [/if 1104]n

    nn


    n [if 1114 equals=”Yes”]n

    n [/if 1114]nnn

    n

    n

    Regular Issue Open Access Article

    n

    n

    n

    n

    n

    Research & Reviews: A Journal of Bioinformatics

    n

    [if 344 not_equal=””]ISSN: 2393-8722[/if 344]n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    n

    Volume 09
    Issue 02
    Received August 11, 2022
    Accepted August 25, 2022
    Published August 28, 2022

    n

    n

    n

    n

    [if 1190 not_equal=””]n

    Editor

    n

    [foreach 1188]n

    n [/foreach]n

    n [/if 1190] [if 1177 not_equal=””]n

    Reviewer

    n

    [foreach 1176]n

    n [/foreach]n

    n [/if 1177]n

    n

    n

    nn

    nn function myFunction2() {n var x = document.getElementById(“browsefigure”);n if (x.style.display === “block”) {n x.style.display = “none”;n }n else { x.style.display = “Block”; }n }n document.querySelector(“.prevBtn”).addEventListener(“click”, () => {n changeSlides(-1);n });n document.querySelector(“.nextBtn”).addEventListener(“click”, () => {n changeSlides(1);n });n var slideIndex = 1;n showSlides(slideIndex);n function changeSlides(n) {n showSlides((slideIndex += n));n }n function currentSlide(n) {n showSlides((slideIndex = n));n }n function showSlides(n) {n var i;n var slides = document.getElementsByClassName(“Slide”);n var dots = document.getElementsByClassName(“Navdot”);n if (n > slides.length) { slideIndex = 1; }n if (n (item.style.display = “none”));n Array.from(dots).forEach(n item => (item.className = item.className.replace(” selected”, “”))n );n slides[slideIndex – 1].style.display = “block”;n dots[slideIndex – 1].className += ” selected”;n }nnn function myfun() {n x = document.getElementById(“editor”);n y = document.getElementById(“down”);n z = document.getElementById(“up”);n if (x.style.display == “none”) {n x.style.display = “block”;n }n else {n x.style.display = “none”;n }n if (y.style.display == “none”) {n y.style.display = “block”;n }n else {n y.style.display = “none”;n }n if (z.style.display == “none”) {n z.style.display = “block”;n }n else {n z.style.display = “none”;n }n }n function myfun2() {n x = document.getElementById(“reviewer”);n y = document.getElementById(“down2”);n z = document.getElementById(“up2”);n if (x.style.display == “none”) {n x.style.display = “block”;n }n else {n x.style.display = “none”;n }n if (y.style.display == “none”) {n y.style.display = “block”;n }n else {n y.style.display = “none”;n }n if (z.style.display == “none”) {n z.style.display = “block”;n }n else {n z.style.display = “none”;n }n }n”}]

    Read More
    RRJoBI

    New methods for relevant applications in drug design

    [{“box”:0,”content”:”

    n

    n

    Research & Reviews: A Journal of Bioinformatics

    ISSN: 2393-8722

    Editors Overview

    rrjobi maintains an Editorial Board of practicing researchers from around the world, to ensure manuscripts are handled by editors who are experts in the field of study.

    n

    n

    n

    n

    n

    n

    Open Access

    n

    Special Issue

    n

    Topic

    n

    n New methods for relevant applications in drug designn

    n

    Abstract Submission Deadline : November 30, 2023

    n

    Manuscript Submission Deadline : December 25, 2023

    n [if 457 equals=”Special Issue”]

    [This article belongs to Special Issue New methods for relevant applications in drug design under section rrjobi in Research & Reviews: A Journal of Bioinformatics(rrjobi)] [/if 457]n

    n Special Issue Descriptionn

    De novo drug design is a computational method for creating novel molecular structures from atomic building blocks with no prior knowledge of their relationships. Over the last three decades, software-based drug discovery and development methods have played a significant role in the development of bioactive compounds. These methods are conventional methods, including structure-based and ligand-based designs, which are based on the properties of a biological target’s active site or known active binders, respectively. Artificial intelligence, including machine learning, is a developing field that has had a positive impact on drug discovery. Deep reinforcement learning is a subset of machine learning in which artificial neural networks are combined with reinforcement-learning architectures. This method has been used successfully to develop novel de novo drug design approaches by utilizing a variety of artificial networks such as recurrent neural networks, convolutional neural networks, generative adversarial networks, and autoencoders. Other than AI there are other novels software-based methods such as molecular modeling, structure-based drug design, structure-based virtual screening, ligand interaction, and molecular dynamics that are regarded as powerful tools for studying drug pharmacokinetic and pharmacodynamic properties, as well as the structural activity relationship between a ligand and its target.

    n [if 233 not_equal=””]Editor [foreach 234]n

    ,

    n [/foreach][/if 233]n Keywordsn

    Artificial intelligence, Ligand targets drug discovery, De novo drug design, Machine learning, Computational methods

    n Manuscript Submission informationn

    Manuscripts should be submitted online via the manuscript Engine. Once you register on APID, click here to go to the submission form. Manuscripts can be submitted until the deadline.n All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the email address:[email protected] for announcement on this website.n Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a Double-blind peer-review process. A guide for authors and other relevant information for the submission of manuscripts is available on the Instructions for Authors page.

    n Participating journals:n

    n

    [foreach 176] n  2393-8722n [/foreach]

    n

    n

    n

    Abbrivation

    n rrjobin

    n

    n

    ISSN

    n

    n 2393-8722

    n

    n

    Since

    n

    n

    n

    APC

    950u00a0 $

    n

    n

    n

    n[if 259 not_equal=””]

    Published articles

    View Published Paper[/if 259]n

    n

    n

    n

    n

    n