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Silkworm expression system as a platform technology in life science
Many recombinant proteins have been successfully produced in silkworm larvae or pupae and used for academic and industrial purposes. Several recombinant proteins produced by silkworms have already been commercialized. However, construction of a recombinant baculovirus containing a gene of interest r...
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Formato: | Texto |
Lenguaje: | English |
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Springer-Verlag
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2802491/ https://www.ncbi.nlm.nih.gov/pubmed/19830419 http://dx.doi.org/10.1007/s00253-009-2267-2 |
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author | Kato, Tatsuya Kajikawa, Mizuho Maenaka, Katsumi Park, Enoch Y. |
author_facet | Kato, Tatsuya Kajikawa, Mizuho Maenaka, Katsumi Park, Enoch Y. |
author_sort | Kato, Tatsuya |
collection | PubMed |
description | Many recombinant proteins have been successfully produced in silkworm larvae or pupae and used for academic and industrial purposes. Several recombinant proteins produced by silkworms have already been commercialized. However, construction of a recombinant baculovirus containing a gene of interest requires tedious and troublesome steps and takes a long time (3–6 months). The recent development of a bacmid, Escherichia coli and Bombyx mori shuttle vector, has eliminated the conventional tedious procedures required to identify and isolate recombinant viruses. Several technical improvements, including a cysteine protease or chitinase deletion bacmid and chaperone-assisted expression and coexpression, have led to significantly increased protein yields and reduced costs for large-scale production. Terminal N-acetyl glucosamine and galactose residues were found in the N-glycan structures produced by silkworms, which are different from those generated by insect cells. Genomic elucidation of silkworm has opened a new chapter in utilization of silkworm. Transgenic silkworm technology provides a stable production of recombinant protein. Baculovirus surface display expression is one of the low-cost approaches toward silkworm larvae-derived recombinant subunit vaccines. The expression of pharmaceutically relevant proteins, including cell/viral surface proteins, membrane proteins, and guanine nucleotide-binding protein (G protein) coupled receptors, using silkworm larvae or cocoons has become very attractive. Silkworm biotechnology is an innovative and easy approach to achieve high protein expression levels and is a very promising platform technology in the field of life science. Like the “Silkroad,” we expect that the “Bioroad” from Asia to Europe will be established by the silkworm expression system. |
format | Text |
id | pubmed-2802491 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Springer-Verlag |
record_format | MEDLINE/PubMed |
spelling | pubmed-28024912010-01-07 Silkworm expression system as a platform technology in life science Kato, Tatsuya Kajikawa, Mizuho Maenaka, Katsumi Park, Enoch Y. Appl Microbiol Biotechnol Mini-Review Many recombinant proteins have been successfully produced in silkworm larvae or pupae and used for academic and industrial purposes. Several recombinant proteins produced by silkworms have already been commercialized. However, construction of a recombinant baculovirus containing a gene of interest requires tedious and troublesome steps and takes a long time (3–6 months). The recent development of a bacmid, Escherichia coli and Bombyx mori shuttle vector, has eliminated the conventional tedious procedures required to identify and isolate recombinant viruses. Several technical improvements, including a cysteine protease or chitinase deletion bacmid and chaperone-assisted expression and coexpression, have led to significantly increased protein yields and reduced costs for large-scale production. Terminal N-acetyl glucosamine and galactose residues were found in the N-glycan structures produced by silkworms, which are different from those generated by insect cells. Genomic elucidation of silkworm has opened a new chapter in utilization of silkworm. Transgenic silkworm technology provides a stable production of recombinant protein. Baculovirus surface display expression is one of the low-cost approaches toward silkworm larvae-derived recombinant subunit vaccines. The expression of pharmaceutically relevant proteins, including cell/viral surface proteins, membrane proteins, and guanine nucleotide-binding protein (G protein) coupled receptors, using silkworm larvae or cocoons has become very attractive. Silkworm biotechnology is an innovative and easy approach to achieve high protein expression levels and is a very promising platform technology in the field of life science. Like the “Silkroad,” we expect that the “Bioroad” from Asia to Europe will be established by the silkworm expression system. Springer-Verlag 2009-10-15 2010 /pmc/articles/PMC2802491/ /pubmed/19830419 http://dx.doi.org/10.1007/s00253-009-2267-2 Text en © The Author(s) 2009 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. |
spellingShingle | Mini-Review Kato, Tatsuya Kajikawa, Mizuho Maenaka, Katsumi Park, Enoch Y. Silkworm expression system as a platform technology in life science |
title | Silkworm expression system as a platform technology in life science |
title_full | Silkworm expression system as a platform technology in life science |
title_fullStr | Silkworm expression system as a platform technology in life science |
title_full_unstemmed | Silkworm expression system as a platform technology in life science |
title_short | Silkworm expression system as a platform technology in life science |
title_sort | silkworm expression system as a platform technology in life science |
topic | Mini-Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2802491/ https://www.ncbi.nlm.nih.gov/pubmed/19830419 http://dx.doi.org/10.1007/s00253-009-2267-2 |
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