PMID- 31704988 OWN - NLM STAT- MEDLINE DCOM- 20201102 LR - 20210110 IS - 2045-2322 (Electronic) IS - 2045-2322 (Linking) VI - 9 IP - 1 DP - 2019 Nov 8 TI - Reconstruction of fish allergenicity from the content and structural traits of the component beta-parvalbumin isoforms. PG - 16298 LID - 10.1038/s41598-019-52801-6 [doi] LID - 16298 AB - Most fish-allergic patients have anti-beta-parvalbumin (beta-PV) immunoglobulin E (IgE), which cross-reacts among fish species with variable clinical effects. Although the beta-PV load is considered a determinant for allergenicity, fish species express distinct beta-PV isoforms with unknown pathogenic contributions. To identify the role various parameters play in allergenicity, we have taken Gadus morhua and Scomber japonicus models, determined their beta-PV isoform composition and analyzed the interaction of the IgE from fish-allergic patient sera with these different conformations. We found that each fish species contains a major and a minor isoform, with the total PV content four times higher in Gadus morhua than in Scomber japonicus. The isoforms showing the best IgE recognition displayed protease-sensitive globular folds, and if forming amyloids, they were not immunoreactive. Of the isoforms displaying stable globular folds, one was not recognized by IgE under any of the conditions, and the other formed highly immunoreactive amyloids. The results showed that Gadus morhua muscles are equipped with an isoform combination and content that ensures the IgE recognition of all PV folds, whereas the allergenic load of Scomber japonicus is under the control of proteolysis. We conclude that the consideration of isoform properties and content may improve the explanation of fish species allergenicity differences. FAU - Perez-Tavarez, Raquel AU - Perez-Tavarez R AD - Insto Quimica-Fisica "Rocasolano", Consejo Superior de Investigaciones Cientificas, 28006, Madrid, Spain. FAU - Carrera, Monica AU - Carrera M AD - Insto Investigaciones Marinas, Consejo Superior de Investigaciones Cientificas, 36208, Vigo, Spain. FAU - Pedrosa, Maria AU - Pedrosa M AD - Dpto de Alergologia, Hospital Universitario La Paz, 28046, Madrid, Spain. AD - Insto de Investigacion Hospital Universitario La Paz (IdiPaz), 28046, Madrid, Spain. FAU - Quirce, Santiago AU - Quirce S AD - Dpto de Alergologia, Hospital Universitario La Paz, 28046, Madrid, Spain. AD - Insto de Investigacion Hospital Universitario La Paz (IdiPaz), 28046, Madrid, Spain. FAU - Rodriguez-Perez, Rosa AU - Rodriguez-Perez R AD - Insto de Investigacion Hospital Universitario La Paz (IdiPaz), 28046, Madrid, Spain. FAU - Gasset, Maria AU - Gasset M AUID- ORCID: 0000-0001-6436-4055 AD - Insto Quimica-Fisica "Rocasolano", Consejo Superior de Investigaciones Cientificas, 28006, Madrid, Spain. maria.gasset@csic.es. LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20191108 PL - England TA - Sci Rep JT - Scientific reports JID - 101563288 RN - 0 (Allergens) RN - 0 (Fish Proteins) RN - 0 (Parvalbumins) RN - 0 (Protein Isoforms) RN - 37341-29-0 (Immunoglobulin E) SB - IM MH - Allergens/*chemistry/*immunology MH - Amino Acid Sequence MH - Fish Proteins/*chemistry/*immunology MH - Humans MH - Immunoglobulin E/immunology MH - Muscles MH - Parvalbumins/*chemistry/*immunology MH - Protein Conformation MH - *Protein Isoforms MH - Species Specificity MH - Structure-Activity Relationship PMC - PMC6841720 COIS- The authors declare no competing interests. EDAT- 2019/11/11 06:00 MHDA- 2020/11/03 06:00 PMCR- 2019/11/08 CRDT- 2019/11/10 06:00 PHST- 2019/06/03 00:00 [received] PHST- 2019/10/23 00:00 [accepted] PHST- 2019/11/10 06:00 [entrez] PHST- 2019/11/11 06:00 [pubmed] PHST- 2020/11/03 06:00 [medline] PHST- 2019/11/08 00:00 [pmc-release] AID - 10.1038/s41598-019-52801-6 [pii] AID - 52801 [pii] AID - 10.1038/s41598-019-52801-6 [doi] PST - epublish SO - Sci Rep. 2019 Nov 8;9(1):16298. doi: 10.1038/s41598-019-52801-6.