Swedish Institute

government📍 Stockholm, Sweden
Swedish Institute
2
Alpha-gal Syndrome Publications
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Alpha-gal Syndrome Researchers

Publications

Impaired allergy diagnostics among parasite-infected patients caused by IgE antibodies to the carbohydrate epitope galactose-α 1,3-galactose.

Arkestål K, Sibanda E, Thors C, Troye-Blomberg M, Mduluza T, et al.
The Journal of allergy and clinical immunology •

The carbohydrate epitope galactose-α 1,3-galactose (α-Gal) is abundantly expressed on nonprimate mammalian proteins. We have recently shown that α-Gal is responsible for the IgE binding to cat IgA, a newly identified cat allergen (Fel d 5). We sought to investigate the diagnostic relevance of IgE antibodies to Fel d 5 and α-Gal among parasite-infected patients from central Africa without cat allergy compared with patients with cat allergy from the same region. Sera from 47 parasite-infected patients and 31 patients with cat allergy were analyzed for total IgE and IgE antibodies against cat dander extract (CDE) by using the ImmunoCAP system. Inhibition assay was performed with α-Gal on solid phase-bound CDE. The presence of IgE specific for the major cat allergen Fel d 1, Fel d 5, and α-Gal was analyzed by means of ELISA. Among the 47 parasite-infected patients, 85% had IgE antibodies against α-Gal (OD; median, 0.175; range, 0.102-1.466) and 66% against Fel d 5 (OD; median, 0.13; range, 0.103-1.285). Twenty-four of the parasite-infected patients were sensitized to CDE, and 21 of them had IgE antibodies to Fel d 5 and α-Gal. There was no correlation between IgE levels to CDE and rFel d 1 among the parasite-infected patients but a strong correlation between CDE and Fel d 5 and α-Gal (P < .001). Among the group with cat allergy, only 5 patients had IgE to α-Gal, and nearly 75% (n = 23) had IgE to rFel d 1 (median, 7.07 kU(A)/L; range, 0.51-148.5 kU(A)/L). In contrast, among the patients with cat allergy, there was a correlation between IgE levels to CDE and rFel d 1 (P < .05) but no correlation between CDE and Fel d 5 and α-Gal. IgE to α-Gal causes impaired allergy diagnostics in parasite-infected patients. Screening for IgE to rFel d 1 and other allergens without carbohydrates might identify patients with true cat sensitization/allergy in parasite-infested areas.

Epitopes of the P-fimbrial adhesin of E. coli cause different urinary tract infections.

Roberts JA, Kaack MB, Baskin G, Marklund BI, Normark S
The Journal of urology •

This is a study of the interaction of the tip protein of P-fimbriae E. coli, its specific urothelial adhesin, and urothelial receptors for the adhesin. This tip protein has several epitopes that adhere to different isoreceptors containing the urothelial alpha-gal-1-4 beta-gal disaccharide. Renal tubular cells of our monkey model contain the globoside isoreceptor, and thus ureteral inoculation of E. coli with the class II tip protein leads to pyelonephritis. The class III tip protein adheres to the Forssman antigen and causes cystitis in humans. An E. coli strain, DS17 which originally caused pyelonephritis in a child, is P-fimbriated and contains a class II tip adhesin. A mutant was produced to contain a class III tip adhesin. Eight monkeys had a ureteral inoculation of E. coli DS17 and 4 monkeys with E. coli DS17-1. In addition, we studied in vitro adherence by these strains. We show that in vitro adherence by the tip protein of P-fimbriae to bladder cells of the monkey occurs by several mechanisms, adhering to specific receptors for the class II and III epitopes of the tip protein as well as by means of type 1 fimbriae. In addition, the PapE protein of the fibrillum of the P-fimbriae adheres to fibronectin. As always, electrostatic and hydrophobic interaction remain important contributions to adherence. E. coli DS17 caused pyelonephritis, but DS17-1 caused cystitis. Bacteriuria was prolonged by DS17 infection. The site of a urinary tract infection from P-fimbriated E. coli can be predicted by the epitope of the tip protein of P-fimbriae.