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Recombinant Mucin-Type Fusion Proteins with a Gal alpha 1,3Gal Substitution as Clostridium difficile Toxin A Inhibitors

Artikel i vetenskaplig tidskrift
Författare Reeja Maria Cherian
Chunsheng S. Jin
Jining Liu
Niclas G. Karlsson
Jan Holgersson
Publicerad i Infection and Immunity
Volym 84
Nummer/häfte 10
Sidor 2842-2852
ISSN 0019-9567
Publiceringsår 2016
Publicerad vid Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin
Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 2842-2852
Språk en
Länkar dx.doi.org/10.1128/iai.00341-16
Ämnesord hamster ovary cells, carbohydrate interactions, binding domain, b, determinants, high avidity, receptor, enterotoxin, metronidazole, recognition, antibodies, Immunology, Infectious Diseases
Ämneskategorier Infektionsmedicin, Immunologi inom det medicinska området

Sammanfattning

The capability of a recombinant mucin-like fusion protein, P-selectin glycoprotein ligand-1/mouse IgG2b (PSGL-1/mIgG2b), carrying Gal alpha 1,3Gal beta 1,4GlcNAc determinants to bind and inhibit Clostridium difficile toxin A (TcdA) was investigated. The fusion protein, produced by a glyco-engineered stable CHO-K1 cell line and designated C-PGC2, was purified by affinity and gel filtration chromatography from large-scale cultures. Liquid chromatography-mass spectrometry was used to characterize O-glycans released by reductive beta-elimination, and new diagnostic ions to distinguish Gal alpha 1,3Gal- from Gal alpha 1,4Gal-terminated O-glycans were identified. The C-PGC2 cell line, which was 20-fold more sensitive to TcdA than the wild-type CHO-K1, is proposed as a novel cell-based model for TcdA cytotoxicity and neutralization assays. The C-PGC2-produced fusion protein could competitively inhibit TcdA binding to rabbit erythrocytes, making it a high-efficiency inhibitor of the hemagglutination property of TcdA. The fusion protein also exhibited a moderate capability for neutralization of TcdA cytotoxicity in both C-PGC2 and CHO-K1 cells, the former with and the latter without cell surface Gal alpha 1,3Gal beta 1,4GlcNAc sequences. Future studies in animal models of C. difficile infection will reveal its TcdA-inhibitory effect and therapeutic potential in C. difficile-associated diseases.

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