Spore coat protein H3 (CotH3) (CotH3)

Spore coat protein H3 (CotH3) is a critical cell-surface invasin expressed by fungi of the order Mucorales, most notably Rhizopus species (Gebremariam et al., 2014, J Clin Invest). It plays a pivotal role in the pathogenesis of mucormycosis by mediating the invasion of host endothelial cells through a specific interaction with the host receptor glucose-regulated protein 78 (GRP78). This binding triggers host cell endocytosis, allowing the fungus to penetrate tissues and disseminate hematogenously, particularly in patients with ketoacidosis or high iron levels (Ibrahim et al., 2013, J Clin Invest). CotH3 is highly conserved among Mucorales but is absent in other fungal pathogens like Candida or Aspergillus and mammalian hosts, making it an ideal target for highly specific antifungal therapies. Experimental approaches using monoclonal antibodies to block CotH3 have demonstrated significant protection in animal models of mucormycosis, reducing fungal burden and improving survival rates (Gebremariam et al., 2019, JCI Insight). Additionally, CotH3 serves as a promising biomarker for early diagnosis via PCR or protein detection in clinical samples (Baldin et al., 2018, J Clin Microbiol).

Other names

CotH3Spore coat protein HFungal invasin CotH3CotH protein

Neutralization of the CotH3 protein prevents its interaction with the host cell receptor GRP78 (Glucose-regulated protein 78), thereby inhibiting fungal invasion of endothelial cells and subsequent tissue dissemination (Ibrahim et al., 2013, J Clin Invest).