ArticleJournal of gastroenterology2019
Epitope peptides of Helicobacter pylori CagA antibodies from sera by whole-peptide mapping.
Article in Journal of gastroenterology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Characterization of a novel Helicobacter pylori East Asian-type CagA ELISA for detecting patients infected with various cagA genotypes.Medical microbiology and immunology · 2020Article
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8 authors.
Funding
Abstract
backgroundHelicobacter pylori CagA has been found to be immuno-dominant protein and utilized for the diagnosis of the infection with cagA-positive strains. It is important to characterize the peptide epitopes capable of detecting serum anti-CagA antibodies to understand CagA immunogenicity.
methodsSera from 171 Japanese patients were subjected for the epitope mapping study. Eighty seven peptides were designed from the CagA consensus sequence and were used for ELISA protocol to test the serum samples. The reacting anti-CagA IgG amounts to specific peptides were measured and compared.
resultsThe study revealed a strong reactivity of two peptides (c7-NNTEPIYAQVNKKKAGQAT and c8-AGQATSPEEPIYAQVAKKV) in H. pylori-infected group. Interestingly, these two peptides contained the well-known EPIYA-A and EPIYA-B region, respectively, which are two out of three CagA phosphorylation domains. Tyrosine-phosphorylation of these peptides reduced their reactivity in most sera. Moreover, additional peptides' mapping and chimeric-peptides' experiments indicated that the amino acids (QV and KK) accommodated in right-side flanking regions of both EPIYA-motifs were essential for their strong reactivity, whereas the third EPIYA-motif containing peptide (c12-GRSASPEPIYATIDFDEA) with differing flanking amino acids was not reactive in most cases.
conclusionsOur results suggest that the amino acid sequences constituted in the two reactive peptides are the important immunogenic regions of CagA which would be useful to develop next-generation peptide-based diagnostic assays.
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