Tryptophan usage by Helicobacter pylori differs among strains View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-01-29

AUTHORS

Diana F. Rojas-Rengifo, Cindy P. Ulloa-Guerrero, Markus Joppich, Rainer Haas, Maria del Pilar Delgado, Carlos Jaramillo, Luisa F. Jiménez-Soto

ABSTRACT

Because of its association with severe gastric pathologies, including gastric cancer, Helicobacter pylori has been subject of research for more than 30 years. Its capacity to adapt and survive in the human stomach can be attributed to its genetic flexibility. Its natural competence and its capacity to turn genes on and off allows H. pylori to adapt rapidly to the changing conditions of its host. Because of its genetic variability, it is difficult to establish the uniqueness of each strain obtained from a human host. The methods considered to-date to deliver the best result for differentiation of strains are Rapid Amplification of Polymorphic DNA (RAPD), Multilocus Sequence Typing (MLST) and Whole Genome Sequencing (WGS) analysis. While RAPD analysis is cost-effective, it requires a stable genome for its reliability. MLST and WGS are optimal for strain identification, however, they require analysis of data at the bioinformatics level. Using the StainFree method, which modifies tryptophan residues on proteins using 2, 2, 2, - trichloroethanol (TCE), we observed a strain specific pattern of tryptophan in 1D acrylamide gels. In order to establish the effectiveness of tryptophan fingerprinting for strain identification, we compared the graphic analysis of tryptophan-labelled bands in the gel images with MLST results. Based on this, we find that tryptophan banding patterns can be used as an alternative method for the differentiation of H. pylori strains. Furthermore, investigating the origin for these differences, we found that H. pylori strains alters the number and/or position of tryptophan present in several proteins at the genetic code level, with most exchanges taking place in membrane- and cation-binding proteins, which could be part of a novel response of H. pylori to host adaptation. More... »

PAGES

873

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-37263-6

DOI

http://dx.doi.org/10.1038/s41598-018-37263-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1111766115

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30696868


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