Vaccination is of paramount importance to global health. With the advent of the more recent pandemics, the urgency to expand the range has become even more evident. However, the potential limited availability and affordability of vaccines to resource low- and middle-income countries has created a need for solutions that will ensure cost-effective vaccine production methods for these countries. Pichia pastoris (P. pastoris) (also known as Komagataella phaffii) is one of the most promising candidates for expression of heterologous proteins in vaccines development. It combines the speed and ease of highly efficient prokaryotic platforms with some key capabilities of mammalian systems, potentially reducing manufacturing costs. This review will examine the latest developments in P. pastoris from cell engineering and design to industrial production systems with focus on vaccine development and with reference to specific key case studies.
The limited availability and affordability of vaccines to low-and middle-income countries (LMIC) has created a need for solutions that will ensure effective, affordable vaccine production technology. To establish a rapid and economical platform for the expression of viral proteins in high yield and purity by Pichia pastoris (X33), the receptor-binding domain (RBD) protein of the SARS-CoV2 was selected in this study. After fermentation at the 5 L scale, the protein was purified by a simplified chromatography, with minimal sample treatment. The purified protein was characterized biochemically, and after its formulation, the immunogenicity was evaluated in mice. Collectively, the data suggested that the vaccine candidate is a suitable COVID-19 vaccine candidate antigen for technology transfer. Furthermore, this study creates a robust foundation for industrial production at scale.
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