Dataset Information

RhGAA ADA epitopes determination

ABSTRACT: Here, we have determined rhGAA ADA epitopes in the plasma samples of Pompe disease patients using series of affinity purifications combined with epitope extraction and label free quantitation LC-MS methodology

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): B Cell, Blood Plasma

DISEASE(S): Glycogen Storage Disease Ii

SUBMITTER: Evgeniy Petrotchenko

LAB HEAD: Christoph Borchers

PROVIDER: PXD065994 | Pride | 2025-09-01

REPOSITORIES: pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	EV002848_EP_GAA_TD.msf	Msf
	EV002848_EP_GAA_TD.raw	Raw
	EV002849_EP_a-GAA_TD_K2.msf	Msf
	EV002849_EP_a-GAA_TD_K2.raw	Raw
	EV002850_EP_a-GAA_TD_MLM.raw	Raw

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Publications

Determination of the Epitopes of Alpha-Glucosidase Anti-Drug Antibodies in Pompe Disease Patient Plasma Samples.

Petrotchenko Evgeniy V EV Hahn Andreas A Borchers Christoph H CH

Antibodies (Basel, Switzerland) 20250728 3

Pompe disease is a rare autosomal-recessive neuromuscular disorder caused by a deficiency of the lysosomal enzyme acid alpha-glucosidase (GAA), leading to the pathological accumulation of glycogen and impaired autophagy. Enzyme replacement therapy (ERT) with recombinant human alpha-glucosidase (rhGAA) has been available since 2006, but may lead to the formation of anti-drug antibodies (ADAs) against the recombinant human enzyme, which, in turn, may adversely affect the response to ERT. Knowledge ...[more]

PMID: 40843676

Similar Datasets

Project description:Alkylation damage to DNA occurs when cells encounter alkylating agents in the environment or when active alkylators are generated by nitrosation of amino acids in metabolic pathways. To cope with DNA alkylation damage, cells have evolved genes that encode proteins with alkylation-specific DNA repair activities. It is notable that these repair systems are conserved from bacteria to humans. In Escherichia coli, cells exposed to a low concentration of an alkylating agent, such as N-methyl-Nâ-nitro-N-nitrosoguanidine (MNNG) or methyl methanesulfonate (MMS), show a remarkable increase in resistance to both the lethal and mutagenic effects of subsequent high-level challenge treatments with the same or other alkylating agents. This increased resistance has been known as âadaptive responseâ to alkylation damage in DNA. To date, four genes have been identified as components of this response, ada, alkA, alkB and aidB. The ada gene encodes the Ada protein, which has the dual function of a transcriptional regulator for the genes involved in the adaptive response, and a methyltransferase that demethylates two methylated bases (O6meG and O4meT) and methylphosphotriesters produced by methylating agents in the sugar phosphate backbone. The differences between the wild-type and mutant strains were characterized at transcriptome levels. In addition, the global changes in gene expressions in response to alkylating agents (MMS), in E. coli K-12 W3110 and ada mutant strains were also analyzed. The analysis of time- and strain-dependent adaptive responses revealed the regulatory and physiological characteristics of the Ada-dependent adaptive response in E. coli. In order to examine the intracellular changes that are induced by the ada gene deletion in the MMS-untreated, normal growth condition, the expression levels of genes of ada mutant cells were compared with those of wild-type cells at the mid-log growth phase (at 0.5 h sampling point). Cells were cultivated at 37oC and 250 rpm in 100 mL of Luria-Bertani (LB) medium (10 g/L tryptone, 5 g/L yeast extract, and 5 g/L NaCl) in 250-mL Erlenmeyer flasks. Transcriptome analysis were also performed for the samples (E. coli wildtype and ada mutant strains) taken at 0.5, 1.5 and 3.9 h following MMS treatment for both MMS-treated and -untreated control cultures, and the expression levels were compared.