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Order Blubervirales: Surface Protein
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
Some other registered and commercially successful hepatitis B vaccines using yeast-derived protein SHBs were produced by original technologies based on the employment of highly productive species of yeast other than S. cerevisiae. First, methylotrophic yeast Hansenula polymorpha was used to produce the SHBs protein. The Brazilian vaccine ButaNG was developed using H. polymorpha by the N.G. Biotecnologia Ltda and produced by the Instituto Butantan (Costa et al. 1997; Ioshimoto et al. 1999). Hepavax-Gene vaccine was also developed using H. polymorpha by Rhein Biotech (Hieu et al. 2002), now belonging to the Dynavax company (United States) and produced by the Korean Green Cross. A new low-cost H. polymorpha-produced vaccine GeneVac B was registered in India (Vijayakumar et al. 2004; Kulkarni et al. 2006).
Recombinant Antibodies
Published in Siegfried Matzku, Rolf A. Stahel, Antibodies in Diagnosis and Therapy, 2019
Melvyn Little, Sergey M. Kipriyanov
The methylotrophic yeast Pichia pastoris has been shown to be suitable for the high-level expression of various heterologous proteins, either intracellular or secreted into the culture supernatant (see review by Cregg et al., 1993). Recently, Ridder et al. (1995) demonstrated the applicability of the Pichia expression system for the secretion of antibody fragments. A rabbit scFv against the human leukemia inhibitory factor (hLIF) was expressed in Pichia cells using the expression vector pPIC9 that provides the α-mating factor signal sequence for secretion and the HIS4 gene for selection of the recombinant yeast clones. The yield was about 100 mg per liter of shake flask culture.
Molecular Farming Antibodies in Plants: From Antibody Engineering to Antibody Production
Published in Maurizio Zanetti, J. Donald Capra, The Antibodies, 2002
Rainer Fischer, Ricarda Finnern, Olga Artsaenko, Stefan Schillberg
Like other methylotrophic yeasts, Pichia has been widely used for the production of therapeutically relevant macromolecules [220, 221, 223, 224]. This species has gained interest compared to S. cerevisiae and the Pichia expression system is now available as a commercial kit (InVitrogen, San Diego, CA).
Effects of the Cobalt-60 gamma radiation on Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase
Published in International Journal of Radiation Biology, 2022
Abdelghani Iddar, Mohammed El Mzibri, Adnane Moutaouakkil
This work was carried out to assess the adaptive response of Pichia pastoris, used as a eukaryotic model, after gamma irradiation. Indeed, the methylotrophic yeast P. pastoris represents a good eukaryotic model for many studies. Similar to Escherichia coli, P. pastoris can be grown easily in a laboratory with a relatively short regeneration time and it is able to grow up to high cell densities, resulting in high protein production yields (Potvin et al. 2010). P. pastoris is a single cell organism considered as most effective heterologous expression system with an easy carry out of genetic manipulation and it has become more extensively used for industrial applications (Gasser et al. 2013). P. pastoris allowed the expression and production of proteins that could not be produced efficiently by bacteria or other host organisms (Cereghino et al. 2002). Moreover, P. pastoris has a number of promoters that allow the regulation of proteins in the cell (Stadlmayr et al. 2010). The purpose of this study was to evaluate the effect of Cobalt-60 gamma radiation on P. pastoris GAPDH activity and protein levels. The effect of radiation on induction of some oxidative damages and on antioxidant enzymes activities was also explored.
Formaldehyde as an alternative to antibiotics for treatment of refractory impetigo and other infectious skin diseases
Published in Expert Review of Anti-infective Therapy, 2019
Philip Nikolic, Poonam Mudgil, John Whitehall
In addition to its wide use in manufacturing and as a preservative, formaldehyde is also an important cellular metabolite in the metabolism of methylated compounds in methylotrophic bacteria. It is generally produced by methanotrophic and methylotrophic bacteria during oxidation of hydrocarbons such as methane and methanol [10]. As a result, bacteria have developed methods to tolerate the toxic effects of formaldehyde. This has been primarily through the enzymatic breakdown of formaldehyde into less toxic products. One such method is found in Amycolatopsis methanolica and Mycobacterium gastri in the form of a formaldehyde dismutase that breaks formaldehyde down into formate and methanol. However, both species are still susceptible to formaldehyde at concentrations above 0.8 mM [39].
Mechanisms Behind Pyrroloquinoline Quinone Supplementation on Skeletal Muscle Mitochondrial Biogenesis: Possible Synergistic Effects with Exercise
Published in Journal of the American College of Nutrition, 2018
Paul Hwang, Darryn S. Willoughby
Historically, work in the 1960s on cofactors of bacterial methanol dehydrogenase and glucose dehydrogenase within separate laboratories generated the identification of the same novel cofactor PQQ within bacteria [45]. Furthermore, researchers could extract this prosthetic group from the quinoprotein methanol dehydrogenase of methylotrophs in order to elucidate its molecular structure via X-ray crystallographic analysis [15]. Based upon this approach, the structure of PQQ could be identified. To reiterate, PQQ was first identified within methylotrophic bacteria [49,50] as a coenzyme for methanol dehydrogenase. Beyond its identified role as a cofactor, PQQ has also been suggested to be a trophic factor relevant toward the growth and metabolism of bacteria [18]. Scientists originally termed proteins that interact with PQQ to be identified as quinoproteins [23]. Additional coenzymes such as topaquinone and tryptophan tryptophenylquinone were also identified as quinoproteins in a similar fashion to PQQ [23]. Researchers have also identified the first eukaryotic PQQ-dependent sugar oxidoreductase within a mushroom (basidiomycete Coprinopsis cinerea) [51]. PQQ was also found to stimulate growth within bacteria [52]. Although the effects of PQQ upon mammals were observed by Killgore et al. [53], there are no identified enzymes to date having PQQ as a cofactor within mammals.