z-logo
open-access-imgOpen Access
Helicobacter Pylori Variants with ABC-Type Tyrosine Phosphorylation Motif in Gastric Biopsies of Ghanaian Patients
Author(s) -
Emmanuel Ayitey Tagoe,
Gordon A. Awandare,
Osbourne Quaye,
Richard Harry Asmah,
Timothy Archampong,
Mahasin A. Osman,
Charles Brown
Publication year - 2021
Publication title -
biomed research international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 126
eISSN - 2314-6141
pISSN - 2314-6133
DOI - 10.1155/2021/6616059
Subject(s) - caga , helicobacter pylori , gene , biology , tyrosine , amino acid , microbiology and biotechnology , peptide sequence , tyrosine phosphorylation , genetics , biochemistry , virulence
Background Helicobacter pylori pathogenicity and disease severity are determined by the tyrosine phosphorylation motifs of CagA protein. This study is aimed at detecting the presence of H . pylori and identifying the CagA tyrosine phosphorylation motifs in Ghanaian patients. Material and Methods . A total of 94 archival genomic DNA samples from gastric biopsies were used for the study, and H . pylori was detected by amplifying the 16S rRNA gene. The 3′-end variable region of the cagA gene was amplified, and the entire 3′-end was sequenced and translated into amino acids.Results H . pylori was detected in 53.2% (50/94) of the samples, and all the detected bacteria harboured the cagA gene. Two variants of the bacteria were identified based on the size of the amplified cagA gene: 207 bp and 285 bp. The 207 bp and 285 bp variants accounted for 74% and 22%, respectively, and 4% showed both fragments. Translated amino acid sequence of the cagA gene showed EPIYA-A, EPIYA-B, and EPIYA-C (ABC type) motifs, indicating the Western variant. The CagA protein C-terminal showed insertion of amino acids in the sequence flanking the EPIYA-A motif at the N-terminal and a complete deletion of the EPIYA-CC and EPIYA-CCC motifs together with the flanking sequences.Conclusions H . pylori identified were Western variant (ABC type) with unique amino acid insertions, suggesting unique variants in Ghanaian patients. Further investigation is however required to understand the role of the molecular diversity of the variant in gastric disease outcome.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom