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. 2019 Dec 5;17(1):50–63. doi: 10.1038/s41423-019-0339-5

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — The CagA protein is composed of a structural N-terminal region and an intrinsically disordered C-terminal region. The K-Xn-R-X-R motif is required for CagA to physically associate with the membrane phospholipid phosphatidylserine (PS) in cells. The EPIYA (Glu-Pro-Ile-Tyr-Ala) motifs in the C-terminal region are the tyrosine phosphorylation sites of CagA. The EPIYA-repeat region of CagA includes the common EPIYA segments, EPIYA-A, EPIYA-B, and an East Asian CagA-specific EPIYA-D segment, or a variable number of Western CagA-specific EPIYA-C segments, which are a results of the sequence polymorphisms of the CagA protein. The CM motif, which is composed of 16 amino acid residues, serves as a PAR1b binding site, promoting the multimerization of the CagA protein. Based on sequence polymorphisms, the CM motif is subdivided into 2 groups: a canonical CM motif, which has conserved PAR1b-binding ability, and a noncanonical CM motif, which lacks the binding ability. East Asian CagA possesses a single East Asian CagA-specific CM motif (CM^E), whereas Western CagA possesses multiple Western CagA-specific CM motifs (CM^W). The structure of CagA with noncanonical CM motifs, which lack binding ability to PAR1b/MARK2, is shown (bottom panel). The Amerindian CagA, which is derived from the H. pylori v225 strain, possesses an internally deleted noncanonical CM motif. The ABC’-type Western CagA, which was cloned from the H. pylori TH2099 strain that had colonized housed macaques, possesses a derivative of the CM^W motif with amino acid substitutions (CM^W’) as well as the atypical EPIYA-C segment that contains the ELIYA sequence.