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All Journal HAYATI Journal of Biosciences
Sri Swasthikawati, Sri
Fak. Biologi, UGM, Yogyakarta
Agriculture, Biological Sciences & Forestry Earth & Planetary Sciences

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Truncation on N-Terminal Hydrophobic Domain of L1 Major Capsid Protein of Human Papillomavirus Type 52 Enhances Its Expression in Hansenula polymorpha Arifah, Rosyida Khusniatul; Firdaus, Moh Egy Rahman; Chairunnisa, Sheila; Irawan, Shasmita; Ekawati, Nurlaili; Irawan, Herman; Nurfatwa, Maritsa; Hertati, Ai; Swasthikawati, Sri; Novianti, Ela; Mustafawi, Wike Zahra; Nur Umami, Rifqiyah; Mustopa, Apon Zaenal
HAYATI Journal of Biosciences Vol. 32 No. 4 (2025): July 2025
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.32.4.1062-1072

Abstract

Human papillomavirus (HPV) infection is the main cause of cervical cancer. The administration of the HPV prophylactic vaccine, which is commonly produced based on HPV L1 major capsid protein, significantly reduces the incidence of cervical cancer. However, the coverage of the HPV vaccination program is often hindered due to its relatively high cost. This study aimed to evaluate the impact of N-terminal hydrophobic domain truncation on the expression of L1 major capsid protein of HPV type 52 in Hansenula polymorpha. The truncation enhanced the yield of L1 protein expression compared with the full length, which was confirmed by Western blot and ELISA. Furthermore, the truncated L1 protein formed virus-like particles (VLPs), which were confirmed by transmission electron microscopy (TEM). Bioinformatics analysis showed that the truncated L1 protein was more soluble compared with the full length, possibly increasing the protein expression. These findings could pave the way for the development of a more cost-effective HPV type 52 L1 protein production in H. polymorpha to be used as a VLP-based prophylactic vaccine.
Medium Optimization for Recombinant Human Papillomavirus Type 52 L1 Protein Production in Pichia pastoris GS115 Platform on Bioreactor Scale Mustopa, Apon Zaenal; Nur Amani, Febriyanti; Irawan, Herman; Novianti, Ela; Swasthikawati, Sri; Ekawati, Nurlaili; Nurfatwa, Maritsa; Joko Wahyono, Daniel; Juanssilfero, Ario Betha; Mamangkey, Jendri; Purnomo, Yudi; Hertati, Ai; Wijaya, Hans; Dewi, Kartika Sari; Ningrum, Ratih Asmana
HAYATI Journal of Biosciences Vol. 32 No. 5 (2025): September 2025
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.32.5.1283-1294

Abstract

Human papillomavirus (HPV) stands as the primary etiological agent in the development of invasive cervical cancer worldwide. The L1 protein is a pivotal constituent of prophylactic HPV vaccines. Notably, HPV type 52 is one of the most prevalent genotypes found in squamous cell carcinoma cases in Indonesia. This research endeavor aims to enhance the productivity of recombinant HPV-52 L1 protein by optimizing the culture conditions of P. pastoris GS115 cells. In this study, we conducted trials employing 17 different media variants to optimize the expression of recombinant HPV-52 L1 protein. The results from small-scale experiments revealed three media, namely SYN6.10, BMMY, and SYN6.1, which exhibited promising yields of recombinant HPV-52 L1 protein as assessed through ELISA or immunoassay analysis. We succeeded in refining the SYN6.10 derivative, denoted as SYN6.10b, specifically designed for use in 1-L and 5-L bioreactors. This achievement was realized by adjusting Trace Element Solution (TES) and Vitamin Solution (VS) concentrations and implementing a methanol fed-batch phase with the addition of 0.3% methanol after 24 and 48 hours of fermentation in the P. pastoris medium. Further visualizations through SDS-PAGE and western blot analysis confirmed the protein after 72 hours of fermentation in a 1-L bioreactor using the SYN6.10b medium. In conclusion, the SYN6.10b medium required a 72 hours fermentation period to successfully express recombinant HPV-52 L1 protein in the P. pastoris platform.
Co-Authors Ai Hertati, Ai Apon Zaenal Mustopa Arifah, Rosyida Khusniatul Ario Betha Juanssilfero Chairunnisa, Sheila Ekawati, Nurlaili Firdaus, Moh Egy Rahman Irawan, Herman Irawan, Shasmita Jendri Mamangkey Joko Wahyono, Daniel Kartika Sari Dewi Mustafawi, Wike Zahra Novianti, Ela Nur Amani, Febriyanti Nur Umami, Rifqiyah Nurfatwa, Maritsa RATIH ASMANA NINGRUM Wijaya, Hans Yudi Purnomo