ArticlePLoS neglected tropical diseases2019
The most abundant cyst wall proteins of Acanthamoeba castellanii are lectins that bind cellulose and localize to distinct structures in developing and mature cyst walls.
Article in PLoS neglected tropical diseases, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- New Viability Assays for Acanthamoeba castellanii Trophozoites and Cysts Allow Rapid Assessment of Drug Activity.The Journal of infectious diseases · 2026Article
- Signal peptide variation in cyst lectins as a potential marker for pathogenic Acanthamoeba spp.Parasites & vectors · 2026Article
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- Targets for the diagnosis ofmSphere · 2025Article
- Encystment and Excystment Processes inPathogens (Basel, Switzerland) · 2025Review
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- Cellulose binding and the timing of expression influence protein targeting to the double-layered cyst wall ofmSphere · 2024Article
- Phylogenomic, structural, and cell biological analyses reveal thatMicrobiology spectrum · 2024Article
- β-1,3-Glucan recognition byApplied and environmental microbiology · 2024Article
- An overview of viral chitinases: General properties and biotechnological potential.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- Inhibitory effect of host ocular microenvironmental factors on chlorhexidine digluconate activity.Antimicrobial agents and chemotherapy · 2023Article
- SLAMF7/STAT6 Pathway Inhibits Innate Immune Response in Late-Stage HumanMicroorganisms · 2023Article
- Biological characteristics and pathogenicity ofFrontiers in microbiology · 2023Review
- Combinatorial treatment with β-glucanase enzyme and chlorhexidine induces cysticidal effects in Acanthamoeba cyst.Parasitology research · 2022Article
- A time-resolved multi-omics atlas of Acanthamoeba castellanii encystment.Nature communications · 2022Article
- Opportunistic free-living amoebal pathogens.Pathogens and global health · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundAcanthamoeba castellanii, which causes keratitis and blindness in under-resourced countries, is an emerging pathogen worldwide, because of its association with contact lens use. The wall makes cysts resistant to sterilizing reagents in lens solutions and to antibiotics applied to the eye. METHODOLOGY/PRINCIPAL
findingsTransmission electron microscopy and structured illumination microscopy (SIM) showed purified cyst walls of A. castellanii retained an outer ectocyst layer, an inner endocyst layer, and conical ostioles that connect them. Mass spectrometry showed candidate cyst wall proteins were dominated by three families of lectins (named here Jonah, Luke, and Leo), which bound well to cellulose and less well to chitin. An abundant Jonah lectin, which has one choice-of-anchor A (CAA) domain, was made early during encystation and localized to the ectocyst layer of cyst walls. An abundant Luke lectin, which has two carbohydrate-binding modules (CBM49), outlined small, flat ostioles in a single-layered primordial wall and localized to the endocyst layer and ostioles of mature walls. An abundant Leo lectin, which has two unique domains with eight Cys residues each (8-Cys), localized to the endocyst layer and ostioles. The Jonah lectin and glycopolymers, to which it binds, were accessible in the ectocyst layer. In contrast, Luke and Leo lectins and the glycopolymers, to which they bind, were mostly inaccessible in the endocyst layer and ostioles. CONCLUSIONS/SIGNIFICANCE: The most abundant A. castellanii cyst wall proteins are three sets of lectins, which have carbohydrate-binding modules that are conserved (CBM49s of Luke), newly characterized (CAA of Jonah), or unique to Acanthamoebae (8-Cys of Leo). Cyst wall formation is a tightly choreographed event, in which lectins and glycopolymers combine to form a mature wall with a protected endocyst layer. Because of its accessibility in the ectocyst layer, an abundant Jonah lectin is an excellent diagnostic target.
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