ArticleMicrobial cell factories2006
A novel genetic system for recombinant protein secretion in the Antarctic Pseudoalteromonas haloplanktis TAC125.
Article in Microbial cell factories, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- From Sea to Therapy: Development and Analytical Control of Recombinant Human CDKL5 Production in the Marine BacteriumMarine drugs · 2026Article
- Postbiotics of Marine Origin and Their Therapeutic Application.Marine drugs · 2025Review
- Molecular Biology Applications of Psychrophilic Enzymes: Adaptations, Advantages, Expression, and Prospective.Applied biochemistry and biotechnology · 2024Review
- Metagenomic exploration of cold-active enzymes for detergent applications: Characterization of a novel, cold-active and alkali-stable GH8 endoglucanase from ikaite columns in SW Greenland.Microbial biotechnology · 2024Article
- Modelling hCDKL5 Heterologous Expression in Bacteria.Metabolites · 2021Article
- Aliivibrio wodanis as a production host: development of genetic tools for expression of cold-active enzymes.Microbial cell factories · 2019Article
- New insights on Pseudoalteromonas haloplanktis TAC125 genome organization and benchmarks of genome assembly applications using next and third generation sequencing technologies.Scientific reports · 2019Article
- Marine-Derived Biocatalysts: Importance, Accessing, and Application in Aromatic Pollutant Bioremediation.Frontiers in microbiology · 2017Review
- Engineering low-temperature expression systems for heterologous production of cold-adapted enzymes.Bioengineered · 2016Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- Improved cultivation and metagenomics as new tools for bioprospecting in cold environments.Extremophiles : life under extreme conditions · 2015Review
- Article
- Characterization of a cryptic plasmid pSM429 and its application for heterologous expression in psychrophilic Pseudoalteromonas.Microbial cell factories · 2011Article
- Cytoplasmic and periplasmic proteomic signatures of exponentially growing cells of the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125.Applied and environmental microbiology · 2011Article
- Fed-batch process for the psychrotolerant marine bacterium Pseudoalteromonas haloplanktis.Microbial cell factories · 2010Article
- Microbial factories for recombinant pharmaceuticals.Microbial cell factories · 2009Article
- Characterization of a cryptic plasmid from a Greenland ice core Arthrobacter isolate and construction of a shuttle vector that replicates in psychrophilic high G+C Gram-positive recipients.Extremophiles : life under extreme conditions · 2008Article
- Development of an improved Pseudoalteromonas haloplanktis TAC125 strain for recombinant protein secretion at low temperature.Microbial cell factories · 2008Article
- Recombinant protein production in the new Millennium.Microbial cell factories · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe final aim of recombinant protein production is both to have a high specific production rate and a high product quality. It was already shown that using cold-adapted bacteria as host vectors, some "intractable" proteins can be efficiently produced at temperature as low as 4 degrees C.
resultsA novel genetic system for the production and secretion of recombinant proteins in the Antarctic Gram-negative bacterium Pseudoalteromonas haloplanktis TAC125 was set up. This system aims at combining the low temperature recombinant product production with the advantages of extra-cellular protein targeting. The psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis TAB23 was used as secretion carrier. Three chimerical proteins were produced by fusing intra-cellular proteins to C-terminus of the psychrophilic alpha-amylase and their secretion was analysed. Data reported in this paper demonstrate that all tested chimeras were translocated with a secretion yield always higher than 80%.
conclusionData presented here demonstrate that the "cold" gene-expression system is efficient since the secretion yield of tested chimeras is always above 80%. These secretion performances place the alpha-amylase derived secretion system amongst the best heterologous secretion systems in Gram-negative bacteria reported so far. As for the quality of the secreted passenger proteins, data presented suggest that the system also allows the correct disulphide bond formation of chimera components, secreting a fully active passenger.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.