Search

The article presents a case study of a 3-year-old boy who was referred to the hospital regarding his erythroderma with severe scales and was diagnosed with suggestive of harlequin ichthyosis (HI). The patient was suggested to be treated with etretinate and tacalcitol for his whitish scales. The article also discusses the survival and mortality rates for patients with HI.

We herein report two patients with anti-muscle-specific kinase (MuSK) antibody-positive myasthenia gravis who experienced rapid deterioration of weakness, particularly respiratory muscle weakness, necessitating non-invasive positive pressure ventilation (NIPPV) and were treated with efgartigimod. After treatment initiation, a rapid reduction in IgG levels and recovery from clinical symptoms were observed. NIPPV was no longer required two to three weeks after the first infusion of efgartigimod. These findings suggest that the reduction of IgG levels using efgartigimod is a good treatment option in patients with myasthenia gravis positive for anti-MuSK antibodies, even during the acute phase of the disease.

Endo-beta-N-acetylglucosaminidases are thought to be key enzymes in the catabolism of asparagine-linked oligosaccharides. However, little is known about the enzymes of this type in basidiomycetes. We investigated endo-beta-N-acetylglucosaminidases in basidiomycetes using fluorescence-labeled glycoasparagines as substrates. Flammulina velutipes showed high activity and its enzyme was named endo-beta-N-acetylglucosaminidase FV (Endo FV). The enzyme purified from the fruiting bodies of F. velutipes was separated into two forms. Endo FV was specific for high mannose and hybrid-type oligosaccharides. The enzyme was remarkably less active against asparagine-linked oligosaccharides attached to glycoproteins. It transferred an asparagine-linked oligosaccharide to Glc, but not to Gal. cDNA of Endo FV was cloned. It was composed of a 996-bp open reading frame encoding 331 amino acid residues. A recombinant Endo FV expressed in Escherichia coli showed enzymatic activity. The Endo FV gene in the genome of F. velutipes had no introns. The gene encoding Endo FV showed little homology with genes of known endo-beta-N-acetylglucosaminidases. A chitinase active site motif existed in the deduced primary structure, indicating that Endo FV belongs to glycoside hydrolase family 18. The deduced amino acid sequence of Endo FV had regions conserved in class III chitinases from fungi though it showed little homology with the sequence of any other endo-beta-N-acetylglucosaminidases. A folding model of Endo FV indicated it to be homologous with the tertiary structure of Endo H which is quite similar in specificity for asparagine-linked oligosaccharides. This study suggests that Endo FV may become similar to Endo H in substrate specificity as a result of evolutionary convergence.