RESUMEN
Spinal dysraphisms (SDs) are congenital malformations of the spinal cord, determined by derangement in the complex cascade of embryologic events involved in spinal development. They represent a heterogeneous group ranging from mild clinical manifestations-going unnoticed or being discovered at clinical examination-to a causal factor of life quality impairment, especially when associated with musculoskeletal, gastrointestinal, genitourinary, or respiratory system malformations. Knowledge of the normal embryologic development of the spinal cord-which encompasses three main steps (gastrulation, primary neurulation, and secondary neurulation)-is crucial for understanding the pathogenesis, neuroradiologic scenarios, and clinical-radiologic classification of congenital malformations of the spinal cord. SDs can be divided with clinical examination or neuroradiologic study into two major groups: open SDs and closed SDs. Congenital malformations of the spinal cord include a wide range of abnormalities that vary considerably in imaging and clinical characteristics and complexity and therefore may represent a diagnostic challenge, even for the experienced radiologist. Online supplemental material is available for this article. ©RSNA, 2021.
Asunto(s)
Imagen por Resonancia Magnética , Disrafia Espinal , Desarrollo Embrionario , Humanos , Médula Espinal , Disrafia Espinal/diagnóstico por imagen , Columna VertebralRESUMEN
A cellulase gene cluster of Clostridium josui was sequenced, and was found to encode 11 proteins responsible for cellulosome (cellulolytic complex) formation, viz., cipA, cel48A, cel8A, cel9A, cel9B, orfX, cel9C, cel9D, man5A, cel9E, and cel5B, in order from the upstream side. All the predicted enzymes had a dockerin module, suggesting that these proteins are members of the C. josui cellulosome. Among these genes, the man5A gene encoding ß-mannanase was expressed in Escherichia coli and the recombinant enzyme (rMan5A) was characterized. rMan5A showed strong activity toward carob galactomannan and low activity toward guar gum, suggesting that it prefers non-galactosylated mannan to galactomannan. This enzyme hydrolyzed ivory nut mannan to produce mainly mannotriose and larger mannooligosaccharides, and was not active toward mannotriose. An antiserum raised against the recombinant enzyme detected Man5A in the culture supernatants of C. josui, which was grown on either ball-milled cellulose or glucose as a carbon source.
Asunto(s)
Proteínas Bacterianas/genética , Celulasa/genética , Clostridium/enzimología , Clostridium/genética , Familia de Multigenes/genética , Proteínas Recombinantes/genética , Secuencia de Aminoácidos , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo , Medios de Cultivo Condicionados , Escherichia coli/genética , Immunoblotting , Polisacárido Liasas/genética , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Análisis de Secuencia de ADNRESUMEN
The Clostridium josui aga27A gene encodes the cellulosomal alpha-galactosidase Aga27A, which comprises a catalytic domain of family 27 of glycoside hydrolases and a dockerin domain responsible for cellulosome assembly. The catalytic domain is highly homologous to those of various alpha-galactosidases of family 27 of glycoside hydrolases from eukaryotic organisms, especially plants. The recombinant Aga27A alpha-galactosidase devoid of the dockerin domain preferred highly polymeric galactomannan as a substrate to small saccharides such as melibiose and raffinose.
