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. 2025 May;93(5):1067-1073.
doi: 10.1002/prot.26788. Epub 2024 Dec 25.

Cryo-EM Structure of Human Hyaluronidase PH-20

Seong-Bin Im  1 , Hyung Nam Song  2 , Tae-Kyeong Jeong  1 , Nayun Kim  1 , Kyuwan Kim  2 , Soon-Jae Park  2 , Byung-Ha Oh  1   3
Affiliations

Cryo-EM Structure of Human Hyaluronidase PH-20

Seong-Bin Im et al. Proteins. 2025 May.

Abstract

PH-20 is a specific type of hyaluronidase that plays a critical role in the fertilization process by facilitating the initial binding of sperm to the glycoprotein layer surrounding the oocyte and subsequently breaking down hyaluronic acid polymers in the cumulus cell layer. PH-20 contains an epidermal growth factor (EGF)-like domain, which may be involved in the recognition of the glycoprotein layer in addition to the catalytic domain. Herein, we report the structure of human PH-20 determined by cryogenic electron microscopy. Comparative analyses of the PH-20 structure with two other available hyaluronidase structures reveal a general similarity in the central catalytic domains, including the conservation of catalytically essential residues at the equivalent spatial positions. However, unique difference is found in the EGF-like domain, characterized by a longer sequence that is likely to form a flexibly anchored β-hairpin containing a disulfide bond.

Keywords: Cryo‐EM structure; Hyaluronidase; PH‐20.

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