jf1c07922_si_001.pdf (450.58 kB)
Crystal Structure Analysis and IgE Epitope Mapping of Allergic Predominant Region in Scylla paramamosain Filamin C, Scy p 9
journal contribution
posted on 2022-01-18, 14:37 authored by Xin-Rong He, Yang Yang, Shuai Kang, Ye-Xin Chen, Pei-Yi Zheng, Gui-Xia Chen, Xiao-Mei Chen, Min-Jie Cao, Tengchuan Jin, Guang-Ming LiuFilamin
C (FLN c) is a novel allergen in shellfish. In this study,
FLN c from Scylla paramamosain was
divided into three regions for recombinant expression based on the
number of domains and amino acids. Using dot blot and basophil activation
tests, the allergic predominant region of FLN c was determined to
be 336–531 amino acid positions (named FLN c-M). It was confirmed
that by X-ray diffraction, the crystal structure of FLN c-M with immunoglobulin-like
folding at a resolution of 1.7 Å was obtained. The monomer was
a barrel structure composed of 16 β-strands and 2 α-helices.
Three conformational epitopes were predicted, six linear epitopes
were verified by serological test, and they were positioned on the
crystal structure of FLN c-M. For the first time, the crystal structure
of the allergic predominant region of FLN c was determined, and it
provided an accurate template for the localization of IgE epitopes.
History
Usage metrics
Categories
Keywords
using dot blotrecombinant expression basedbasophil activation testsallergic predominant regionsix linear epitopesbarrel structure composedige epitope mappingthree conformational epitopescrystal structure analysisnamed fln cige epitopescrystal structurefln cthree regionsserological testscylla paramamosainray diffractionnovel allergenlike foldingfirst timeamino acidsaccurate template7 å2 α16 β
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC