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<p>The growing need for rapid and cost-effective antibody production highlights the potential of <i>Komagataella phaffii</i> (syn. <i>Pichia pastoris</i>) as an alternative to mammalian systems. This study aimed to develop and optimize engineered scFvs (single-chain antibody fragments) against SARS-CoV-2 using <i>K. phaffii</i>. Four scFv formats, scFv-His, scFv-CH3-His, scFv-ZIP-His, and scFv-Fc, were evaluated for binding activity, neutraliation potency, expression yield, and in vivo stability. Among them, scFv-Fc demonstrated the best overall performance, with strong antigen binding (EC<sub>50</sub> = 0.0034&#xa0;µg/mL), effective neutralizing activity (IC<sub>50</sub> = 0.570&#xa0;µg/mL), and a prolonged serum half-life exceeding 5&#xa0;days. Optimization of fermentation conditions increased its expression from 23 to 110&#xa0;mg/L. These results demonstrate the feasibility of engineering scFv-based therapeutics using yeast systems and establish a framework for the rapid and economical production of next-generation antibody formats.</p>

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Development of a Komagataella phaffii-based expression system for high-activity anti-SARS-CoV-2 neutralizing antibodies

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月11日

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  • Xueqin Liu,
  • Qiaoli Lang,
  • Nan Huang,
  • Xiaoyan You,
  • Yuchun Ding,
  • Meng Wu,
  • Liangpeng Ge,
  • Xi Yang

摘要

The growing need for rapid and cost-effective antibody production highlights the potential of Komagataella phaffii (syn. Pichia pastoris) as an alternative to mammalian systems. This study aimed to develop and optimize engineered scFvs (single-chain antibody fragments) against SARS-CoV-2 using K. phaffii. Four scFv formats, scFv-His, scFv-CH3-His, scFv-ZIP-His, and scFv-Fc, were evaluated for binding activity, neutraliation potency, expression yield, and in vivo stability. Among them, scFv-Fc demonstrated the best overall performance, with strong antigen binding (EC50 = 0.0034 µg/mL), effective neutralizing activity (IC50 = 0.570 µg/mL), and a prolonged serum half-life exceeding 5 days. Optimization of fermentation conditions increased its expression from 23 to 110 mg/L. These results demonstrate the feasibility of engineering scFv-based therapeutics using yeast systems and establish a framework for the rapid and economical production of next-generation antibody formats.