Unconventional microbial systems for the cost-efficient production of high-quality protein therapeutics

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Recombinant pharmaceuticals from microbial cells: a 2015 update

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Challenges and opportunities for non-antibody scaffold drugs

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Microalgae and cyanobacteria as enzyme biofactories

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Towards systems metabolic engineering in Pichia pastoris

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An improved secretion signal enhances the secretion of model proteins from Pichia pastoris

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Emerging Trends in Genetic Engineering of Microalgae for Commercial Applications

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Industrial Production of Proteins with Pichia pastoris—Komagataella phaffii

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New biorefineries and sustainable agriculture: Increased food, biofuels, and ecosystem security

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Challenges and progress towards industrial recombinant protein production in yeasts: A review

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Recombinant protein production in Pichia pastoris under glyceraldehyde-3-phosphate dehydrogenase promoter: From carbon source metabolism to bioreactor operation parameters

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Comparative genomics and transcriptomics of Pichia pastoris

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Bacterial inclusion bodies are industrially exploitable amyloids

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The art of adapting to extreme environments: The model system Pseudoalteromonas

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Bacterial cell factories for recombinant protein production; expanding the catalogue

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Multifunctional Click Hyaluronic Acid Nanogels for Targeted Protein Delivery and Effective Cancer Treatment in Vivo

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The yeast stands alone: the future of protein biologic production

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Synthetic promoters capable of driving robust nuclear gene expression in the green alga Chlamydomonas reinhardtii

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Fine‐tuning the P. pastoris iMT1026 genome‐scale metabolic model for improved prediction of growth on methanol or glycerol as sole carbon sources

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ASA3P: An automatic and scalable pipeline for the assembly, annotation and higher-level analysis of closely related bacterial isolates

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Fed-batch operational strategies for recombinant Fab production with Pichia pastoris using the constitutive GAP promoter

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Towards protein-based viral mimetics for cancer therapies

Unzueta, U., Céspedes, M. V., Vázquez, E., Ferrer‐Miralles, N., Mangues, R., & Villaverde, A. (2015) · Trends in biotechnology · doi:10.1016/j.tibtech.2015.02.007 · Cited by 78

Systems metabolic engineering, industrial biotechnology and microbial cell factories

Lee, S. Y., Mattanovich, D., & Villaverde, A. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-156 · Cited by 78

Ecology of cold environments: new insights of bacterial metabolic adaptation through an integrated genomic-phenomic approach

Mocali, S., Chiellini, C., Fabiani, A., Decuzzi, S., de Pascale, D., Parrilli, E., Tutino, M. L., Perrin, E., Bosi, E., Fondi, M., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-00876-4 · Cited by 75

BBB-targeting, protein-based nanomedicines for drug and nucleic acid delivery to the CNS

Peluffo, H., Unzueta, U., Negro‐Demontel, M. L., Xu, Z., Váquez, E., Ferrer‐Miralles, N., & Villaverde, A. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.02.004 · Cited by 75

Enabling Low Cost Biopharmaceuticals: A Systematic Approach to Delete Proteases from a Well-Known Protein Production Host Trichoderma reesei

Landowski, C. P., Huuskonen, A., Wahl, R., Westerholm‐Parvinen, A., Kanerva, A., Hänninen, A., Salovuori, N., Penttilä, M. E., Natunen, J., Ostermeier, C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134723 · Cited by 76

Engineering protein self-assembling in protein-based nanomedicines for drug delivery and gene therapy

Ferrer-Miralles, N., Rodríguez‐Carmona, E., Corchero, J., García-Fruitós, E., Vázquez, E., & Villaverde, A. (2015) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2013.833163 · Cited by 63

Rational development of bioprocess engineering strategies for recombinant protein production in Pichia pastoris (Komagataella phaffii) using the methanol-free GAP promoter. Where do we stand?

Garcia‐Ortega, X., Cámara, E., Ferrer, P., Albiol, J., Montesinos, J. L. G., & Valero, F. (2019) · New Biotechnology · doi:10.1016/j.nbt.2019.06.002 · Cited by 70

Integration and Validation of the Genome-Scale Metabolic Models of Pichia pastoris: A Comprehensive Update of Protein Glycosylation Pathways, Lipid and Energy Metabolism

Tomàs‐Gamisans, M., Ferrer, P., & Albiol, J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148031 · Cited by 72

Efficient Transient Expression of Recombinant Proteins Using DNA Viral Vectors in Freshwater Microalgal Species

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Anti-biofilm activity of the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

Papa, R., Parrilli, E., Sannino, F., Barbato, G., Tutino, M. L., Artini, M., & Selan, L. (2013) · Research in Microbiology · doi:10.1016/j.resmic.2013.01.010 · Cited by 67

Pichia pastoris secretes recombinant proteins less efficiently than Chinese hamster ovary cells but allows higher space‐time yields for less complex proteins

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Unraveling the potential of non-conventional yeasts in biotechnology

Geijer, C., Ledesma‐Amaro, R., & Tomás‐Pejó, E. (2022) · FEMS Yeast Research · doi:10.1093/femsyr/foab071 · Cited by 64

Dynamic genome-scale metabolic modeling of the yeast Pichia pastoris

Saitua, F., Torres, P., Pérez‐Correa, J. R., & Agosin, E. E. (2017) · BMC Systems Biology · doi:10.1186/s12918-017-0408-2 · Cited by 60

Harnessing genetic engineering to drive economic bioproduct production in algae

Gupta, A., Kang, K., Pathania, R., Saxton, L., Saucedo, B., Malik, A., Torres-Tiji, Y., Diaz, C. J., Dutra Molino, J. V., & Mayfield, S. P. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2024.1350722 · Cited by 60

Recombinant vaccines in 2022: a perspective from the cell factory

Favaro, M. T. D. P., Atienza-Garriga, J., Martínez-Torró, C., Parladé, E., Vázquez, E., Corchero, J. L., Ferrer‐Miralles, N., & Villaverde, A. (2022) · Microbial Cell Factories · doi:10.1186/s12934-022-01929-8 · Cited by 64

Comprehensive clone screening and evaluation of fed-batch strategies in a microbioreactor and lab scale stirred tank bioreactor system: application on Pichia pastoris producing Rhizopus oryzae lipase

Hemmerich, J., Adelantado, N., Barrigón, J. M., Ponte, X., Hörmann, A., Ferrer, P., Kensy, F., & Valero, F. (2014) · Microbial Cell Factories · doi:10.1186/1475-2859-13-36 · Cited by 57

Engineering Secretory Amyloids for Remote and Highly Selective Destruction of Metastatic Foci

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Production of functional inclusion bodies in endotoxin-free Escherichia coli

Rueda, F. L., Cano‐Garrido, O., Mamat, U., Wilke, K., Seras‐Franzoso, J., García‐Fruitós, E., & Villaverde, A. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-6008-9 · Cited by 54

Quantitative Metabolomics and Instationary 13C-Metabolic Flux Analysis Reveals Impact of Recombinant Protein Production on Trehalose and Energy Metabolism in Pichia pastoris

Jordà, J., Cueto-Rojas, H. F., Carnicer, M., Wahl, A., Ferrer, P., & Albiol, J. (2014) · Metabolites · doi:10.3390/metabo4020281 · Cited by 52

Familiar Stranger

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Functional Protein Aggregates: Just the Tip of the Iceberg

Villaverde, A., Corchero, J. L., Seras‐Franzoso, J., & García‐Fruitós, E. (2015) · Nanomedicine · doi:10.2217/nnm.15.125 · Cited by 51

Genome‐scale metabolic reconstruction and constraint‐based modelling of the Antarctic bacterium P seudoalteromonas haloplanktis TAC 125

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A rapid, modular and marker-free chloroplast expression system for the green alga Chlamydomonas reinhardtii

Bertalan, I., Munder, M. C., Weiß, C., Kopf, J., Fischer, D., & Johanningmeier, U. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2014.12.017 · Cited by 49

Going beyond the limit: Increasing global translation activity leads to increased productivity of recombinant secreted proteins in Pichia pastoris

Staudacher, J., Rebnegger, C., Dohnal, T., Landes, N., Mattanovich, D., & Gasser, B. (2022) · Metabolic Engineering · doi:10.1016/j.ymben.2022.01.010 · Cited by 47

Improved expression of single-chain antibodies in Ustilago maydis

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Endophytic Yeasts: Biology and Applications

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A brief overview on the application and sources of α‐amylase and expression hosts properties in order to production of recombinant α‐amylase

Movahedpour, A., Asadi, M., Khatami, S. H., Taheri‐Anganeh, M., Adelipour, M., Shabaninejad, Z., Ahmadi, N., Irajie, C., & Mousavi, P. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2140 · Cited by 37

Biofabrication of functional protein nanoparticles through simple His-tag engineering

López‐Laguna, H., Sánchez, J. M., Carratalá, J. V., Rojas-Peña, M., Sánchez‐García, L., Parladé, E., Sánchez‐Chardi, A., Voltà‐Durán, E., Serna, N., Cano‐Garrido, O., et al. (2021) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.1c04256 · Cited by 37

Recombinant Protein Materials for Bioengineering and Nanomedicine

Corchero, J. L., Vázquez, E., García‐Fruitós, E., Ferrer‐Miralles, N., & Villaverde, A. (2014) · Nanomedicine · doi:10.2217/nnm.14.153 · Cited by 35

A novel synthetic medium and expression system for subzero growth and recombinant protein production in Pseudoalteromonas haloplanktis TAC125

Sannino, F., Giuliani, M., Salvatore, U., Apuzzo, G. A., de Pascale, D., Fani, R., Fondi, M., Marino, G., Tutino, M. L., & Parrilli, E. (2016) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-016-7942-5 · Cited by 35

Engineering the supply chain for protein production/secretion in yeasts and mammalian cells

Klein, T., Niklas, J., & Heinzle, E. (2015) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-014-1569-2 · Cited by 32

Expanding the recombinant protein quality in Lactococcus lactis

Cano‐Garrido, O., Rueda, F. L., Sánchez‐García, L., Ruíz-Ávila, L., Bosser, R., Villaverde, A., & García‐Fruitós, E. (2014) · Microbial Cell Factories · doi:10.1186/s12934-014-0167-3 · Cited by 31

Bioreactor-scale cell performance and protein production can be substantially increased by using a secretion signal that drives co-translational translocation in Pichia pastoris

Barrero, J. J., Pagazartaundua, A., Glick, B. S., Valero, F., & Ferrer, P. (2020) · New Biotechnology · doi:10.1016/j.nbt.2020.09.001 · Cited by 30

A Nanostructured Bacterial Bioscaffold for The Sustained Bottom-Up Delivery of Protein Drugs

Seras‐Franzoso, J., Peebo, K., Corchero, J. L., Tsimbouri, P. M., Unzueta, U., Rinas, U., Dalby, M. J., Vázquez, E., García‐Fruitós, E., & Villaverde, A. (2013) · Nanomedicine · doi:10.2217/nnm.12.188 · Cited by 31

Improving recombinant protein production in the Chlamydomonas reinhardtii chloroplast using vivid Verde Fluorescent Protein as a reporter

Braun‐Galleani, S., Baganz, F., & Purton, S. (2015) · Biotechnology Journal · doi:10.1002/biot.201400566 · Cited by 28

Deregulation of methanol metabolism reverts transcriptional limitations of recombinant Pichia pastoris ( Komagataella spp) with multiple expression cassettes under control of the AOX1 promoter

Cámara, E., Monforte, S., Albiol, J., & Ferrer, P. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.26947 · Cited by 27

A novel salt-inducible CrGPDH3 promoter of the microalga Chlamydomonas reinhardtii for transgene overexpression

Beltran-Aguilar, A. G., Peraza-Echeverría, S., López-Ochoa, L., Borges-Argáez, I. C., & Herrera-Valencia, V. A. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-09733-y · Cited by 27

Nanotechnology‐based approaches for treating lysosomal storage disorders, a focus on Fabry disease

Abasolo, I., Seras‐Franzoso, J., Moltó‐Abad, M., Díaz‐Riascos, V., Corchero, J. L., Pintos‐Morell, G., & Schwartz, S. (2020) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1684 · Cited by 27

Human recombinant lysosomal enzymes produced in microorganisms

Espejo-Mojica, A. J., Alméciga-Díaz, C. J., Rodríguez‐López, A., Mosquera, Á., Díaz, D., Beltrán, L., Díaz, S., Pimentel, N., Moreno, J., Sánchez, J., et al. (2015) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2015.06.001 · Cited by 27

Microbial Biofabrication for Nanomedicine: Biomaterials, Nanoparticles and Beyond

Vázquez, E., & Villaverde, A. (2013) · Nanomedicine · doi:10.2217/nnm.13.164 · Cited by 26

Production, secretion and purification of a correctly folded staphylococcal antigen in Lactococcus lactis

Samazan, F., Rokbi, B., Seguin, D., Telles, F., Gautier, V., Richarme, G., Chevret, D., Varela, P. F., Velours, C., & Poquet, I. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0271-z · Cited by 24

Release of functional fibroblast growth factor-2 from artificial inclusion bodies

Serna, N., Cano‐Garrido, O., Sánchez, J. M., Sánchez‐Chardi, A., Sánchez‐García, L., López‐Laguna, H., Fernández, E., Vázquez, E., & Villaverde, A. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.08.007 · Cited by 24

Biosynthesis of protein-based drugs using eukaryotic microalgae

Xie, Z., He, J., Peng, S., Zhang, X., & Kong, W. (2023) · Algal Research · doi:10.1016/j.algal.2023.103219 · Cited by 21

Conformational and functional variants of CD44-targeted protein nanoparticles bio-produced in bacteria

Pesarrodona, M., Fernández, Y., Foradada, L., Sánchez‐Chardi, A., Conchillo‐Solé, O., Unzueta, U., Xu, Z., Roldán, M., Villegas, S., Ferrer‐Miralles, N., et al. (2016) · Biofabrication · doi:10.1088/1758-5090/8/2/025001 · Cited by 20

Towards a synthetic nuclear transcription system in green algae: Characterization of Chlamydomonas reinhardtii nuclear transcription factors and identification of targeted promoters

Anderson, M. S., Muff, T. J., Georgianna, D. R., & Mayfield, S. P. (2016) · Algal Research · doi:10.1016/j.algal.2016.12.002 · Cited by 20

Protein scaffolds in human clinics

Cano‐Garrido, O., Serna, N., Unzueta, U., Parladé, E., Mangues, R., Villaverde, A., & Vázquez, E. (2022) · Biotechnology Advances · doi:10.1016/j.biotechadv.2022.108032 · Cited by 20

Genomics and transcriptomics analysis reveals the mechanism of isobutanol tolerance of a laboratory evolved Lactococcus lactis strain

Gupta, J. A., Thapa, S., Verma, M., Som, R., & Mukherjee, K. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-67635-w · Cited by 19

Sequential Release of Proteins from Structured Multishell Microcapsules

Shimanovich, U., Michaels, T. C. T., Genst, E. D., Matak‐Vinković, D., Dobson, C. M., & Knowles, T. P. J. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b00351 · Cited by 19

Gene expression engineering in fungi

Mojžita, D., Rantasalo, A., & Jäntti, J. (2019) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2019.04.007 · Cited by 19

Structural and functional features of self-assembling protein nanoparticles produced in endotoxin-free Escherichia coli

Rueda, F. L., Céspedes, M. V., Sánchez‐Chardi, A., Seras‐Franzoso, J., Pesarrodona, M., Ferrer‐Miralles, N., Vázquez, E., Rinas, U., Unzueta, U., Mamat, U., et al. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0457-z · Cited by 16

Modelling microbial metabolic rewiring during growth in a complex medium

Fondi, M., Bosi, E., Presta, L., Natoli, D., & Fani, R. (2016) · BMC Genomics · doi:10.1186/s12864-016-3311-0 · Cited by 17

A Stochastic Landscape Approach for Protein Folding State Classification

Faran, M., Ray, D., Nag, S., Raucci, U., Parrinello, M., & Bisker, G. (2024) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c00464 · Cited by 14

Genome-scale phylogenetic and DNA composition analyses of Antarctic Pseudoalteromonas bacteria reveal inconsistencies in current taxonomic affiliation

Bosi, E., Fondi, M., Maida, I., Perrin, E., de Pascale, D., Tutino, M. L., Parrilli, E., Giudice, A. L., Filloux, A., & Fani, R. (2015) · Hydrobiologia · doi:10.1007/s10750-015-2396-9 · Cited by 16

Recombinant production of a single-chain antibody fragment in Pseudoalteromonas haloplanktis TAC125

Giuliani, M., Parrilli, E., Sannino, F., Apuzzo, G. A., Marino, G., & Tutino, M. L. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5582-1 · Cited by 16

Magnetic nanoparticle mediated-gene delivery for simpler and more effective transformation of Pichia pastoris

Arslan, Ş. Y., Solak, K., Acar, M., Mavi, A., & Ünver, Y. (2021) · Nanoscale Advances · doi:10.1039/d1na00079a · Cited by 15

Comparison of intracellular and secretion-based strategies for production of human α-galactosidase A in the filamentous fungus Trichoderma reesei

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Combined metabolic and enzymatic engineering for de novo biosynthesis of δ-tocotrienol in Yarrowia lipolytica

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