Functional evaluation of novel variants of B4GALNT1 in a patient with hereditary spastic paraplegia and the general population

Author:

Inamori Kei-ichiro,Nakamura Katsuya,Shishido Fumi,Hsu Jia-Chen,Nagafuku Masakazu,Nitta Takahiro,Ikeda Junji,Yoshimura Hidekane,Kodaira Minori,Tsuchida Naomi,Matsumoto Naomichi,Uemura Satoshi,Ohno Shiho,Manabe Noriyoshi,Yamaguchi Yoshiki,Togayachi Akira,Aoki-Kinoshita Kiyoko F.,Nishihara Shoko,Furukawa Jun-ichi,Kaname Tadashi,Nakamura Masahiko,Shimohata Takayoshi,Tadaka Shu,Shirota Matsuyuki,Kinoshita Kengo,Nakamura Yutaka,Ohno Isao,Sekijima Yoshiki,Inokuchi Jin-ichi

Abstract

Hereditary spastic paraplegia (HSP) is a heterogeneous group of neurological disorders that are characterized by progressive spasticity and weakness in the lower limbs. SPG26 is a complicated form of HSP, which includes not only weakness in the lower limbs, but also cognitive impairment, developmental delay, cerebellar ataxia, dysarthria, and peripheral neuropathy, and is caused by biallelic mutations in the B4GALNT1 (beta-1,4-N-acetylgalactosaminyltransferase 1) gene. The B4GALNT1 gene encodes ganglioside GM2/GD2 synthase (GM2S), which catalyzes the transfer of N-acetylgalactosamine to lactosylceramide, GM3, and GD3 to generate GA2, GM2, and GD2, respectively. The present study attempted to characterize a novel B4GALNT1 variant (NM_001478.5:c.937G>A p.Asp313Asn) detected in a patient with progressive multi-system neurodegeneration as well as deleterious variants found in the general population in Japan. Peripheral blood T cells from our patient lacked the ability for activation-induced ganglioside expression assessed by cell surface cholera toxin binding. Structural predictions suggested that the amino acid substitution, p.Asp313Asn, impaired binding to the donor substrate UDP-GalNAc. An in vitro enzyme assay demonstrated that the variant protein did not exhibit GM2S activity, leading to the diagnosis of HSP26. This is the first case diagnosed with SPG26 in Japan. We then extracted 10 novel missense variants of B4GALNT1 from the whole-genome reference panel jMorp (8.3KJPN) of the Tohoku medical megabank organization, which were predicted to be deleterious by Polyphen-2 and SIFT programs. We performed a functional evaluation of these variants and demonstrated that many showed perturbed subcellular localization. Five of these variants exhibited no or significantly decreased GM2S activity with less than 10% activity of the wild-type protein, indicating that they are carrier variants for HSP26. These results provide the basis for molecular analyses of B4GALNT1 variants present in the Japanese population and will help improve the molecular diagnosis of patients suspected of having HSP.

Publisher

Frontiers Media SA

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