4.7 Article

Epitope peptides of Helicobacter pylori CagA antibodies from sera by whole-peptide mapping

期刊

JOURNAL OF GASTROENTEROLOGY
卷 54, 期 12, 页码 1039-1051

出版社

SPRINGER JAPAN KK
DOI: 10.1007/s00535-019-01584-8

关键词

Helicobacter pylori; CagA; IgG; ELISA; Peptide

资金

  1. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) of Japan [16H05191, 18KK0266, 17K09353]
  2. Japan Society for the Promotion of Science [Core-to-Core Program]
  3. National Institutes of Health [DK62813]
  4. Oita University
  5. Grants-in-Aid for Scientific Research [17K09353, 18KK0266, 16H05191] Funding Source: KAKEN

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Background Helicobacter 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. Methods Sera 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. Results The 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. Conclusions Our 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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