An unusual aspect of the biology of nematodes is the attachment of phosphorylcholine (PC) to carbohydrate. The attachment appears to play an important role in nematode development and, in some parasitic species, in immunomodulation. This article considers the nature of the biosynthetic pathway of nematode PC-containing glycoconjugates and, in particular, the identity of the final component in the pathway - the enzyme that transfers PC to carbohydrate (the 'PC transferase'). We offer the opinion that the PC transferase could be a member of the fukutin family (fukutin refers to the mutated gene product that causes Fukuyama congenital muscular dystrophy), a group of enzymes with apparent phosphoryl-ligand transferase activity that are found in organisms ranging from bacteria to humans.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.pt.2009.12.003DOI Listing

Publication Analysis

Top Keywords

nematodes transfer
4
transfer phosphorylcholine
4
phosphorylcholine carbohydrates?
4
carbohydrates? unusual
4
unusual aspect
4
aspect biology
4
biology nematodes
4
nematodes attachment
4
attachment phosphorylcholine
4
phosphorylcholine carbohydrate
4

Similar Publications

Carbohydrate-active enzymes (CAZymes) involved in the degradation of plant cell walls and/or the assimilation of plant carbohydrates for energy uptake are widely distributed in microorganisms. In contrast, they are less frequent in animals, although there are exceptions, including examples of CAZymes acquired by horizontal gene transfer (HGT) from bacteria or fungi in several of phytophagous arthropods and plant-parasitic nematodes. Although the whitefly Bemisia tabaci is a major agricultural pest, knowledge of HGT-acquired CAZymes in this phloem-feeding insect of the Hemiptera order (subfamily Aleyrodinae) is still lacking.

View Article and Find Full Text PDF

Background/objective: There is little data on infections of the genus Cosmocercoides Wilkie, 1930 in toad populations in Iran. Hence, the present study aims to report the first morphological description of the new genus Cosmocercoides Wilkie, 1930 (Ascaridida: Cosmocercidae) in Iranian toads (Bufotes surdus).

Methods: During the helminthological survey from October 2023 to December 2023, 10 specimens of Bufotes surdus were collected.

View Article and Find Full Text PDF

E3 ubiquitin ligases have been linked to developmental diseases including autism, Angelman syndrome (UBE3A), and Johanson-Blizzard syndrome (JBS) (UBR1). Here, we report variants in the E3 ligase UBR5 in 29 individuals presenting with a neurodevelopmental syndrome that includes developmental delay, autism, intellectual disability, epilepsy, movement disorders, and/or genital anomalies. Their phenotype is distinct from JBS due to the absence of exocrine pancreatic insufficiency and the presence of autism, epilepsy, and, in some probands, a movement disorder.

View Article and Find Full Text PDF

Synergistic Co-Cu Dual-Atom Nanozyme with Promoted Catalase-like Activity for Parkinson's Disease Treatment.

ACS Appl Mater Interfaces

January 2025

Experimental Center of Advanced Materials, School of Materials Science & Engineering, Beijing Institute of Technology, Beijing 100081, China.

Neurodegenerative diseases like Parkinson's disease (PD) are intimately associated with oxidative stress due to the excessive highly reactive oxygen species (ROS), leading to the damage of dopaminergic neurons. Herein, we develop a Co-Cu dual-atom nanozyme (CoCu-DAzyme) by uniformly anchoring Co and Cu active sites onto an AlO(OH) substrate that exhibits remarkable catalase-like catalytic activity, far exceeding that of the Co or Cu single-atom counterparts. The following density functional theory calculations reveal that the Co sites efficiently enable HO adsorption, while Cu sites promote charge transfer, synergistically promoting the catalytic decomposition of HO into HO and O.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!