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HP0953 - hypothetical virulence factor overexpresion and localization during Helicobacter pylori infection of gastric epithelium
BACKGROUND: The high prevalence and persistence of Helicobacter pylori (H. pylori) infection, as well as the diversity of pathologies related to it, suggest that the virulence factors used by this microorganism are varied. Moreover, as its proteome contains 340 hypothetical proteins, it is important...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Baishideng Publishing Group Inc
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9367236/ https://www.ncbi.nlm.nih.gov/pubmed/36157534 http://dx.doi.org/10.3748/wjg.v28.i29.3886 |
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author | Arteaga-Resendiz, Nancy K Rodea, Gerardo E Ribas-Aparicio, Rosa María Olivares-Cervantes, Alma L Castelán-Vega, Juan Arturo Olivares-Trejo, José de Jesús Mendoza-Elizalde, Sandra López-Villegas, Edgar O Colín, Christian Aguilar-Rodea, Pamela Reyes-López, Alfonso Salazar García, Marcela Velázquez-Guadarrama, Norma |
author_facet | Arteaga-Resendiz, Nancy K Rodea, Gerardo E Ribas-Aparicio, Rosa María Olivares-Cervantes, Alma L Castelán-Vega, Juan Arturo Olivares-Trejo, José de Jesús Mendoza-Elizalde, Sandra López-Villegas, Edgar O Colín, Christian Aguilar-Rodea, Pamela Reyes-López, Alfonso Salazar García, Marcela Velázquez-Guadarrama, Norma |
author_sort | Arteaga-Resendiz, Nancy K |
collection | PubMed |
description | BACKGROUND: The high prevalence and persistence of Helicobacter pylori (H. pylori) infection, as well as the diversity of pathologies related to it, suggest that the virulence factors used by this microorganism are varied. Moreover, as its proteome contains 340 hypothetical proteins, it is important to investigate them to completely understand the mechanisms of its virulence and survival. We have previously reported that the hypothetical protein HP0953 is overexpressed during the first hours of adhesion to inert surfaces, under stress conditions, suggesting its role in the environmental survival of this bacterium and perhaps as a virulence factor. AIM: To investigate the expression and localization of HP0953 during adhesion to an inert surface and against gastric (AGS) cells. METHODS: Expression analysis was performed for HP0953 during H. pylori adhesion. HP0953 expression at 0, 3, 12, 24, and 48 h was evaluated and compared using the Kruskal-Wallis equality-of-populations rank test. Recombinant protein was produced and used to obtain polyclonal antibodies for immunolocalization. Immunogold technique was performed on bacterial sections during adherence to inert surfaces and AGS cells, which was analyzed by transmission electron microscopy. HP0953 protein sequence was analyzed to predict the presence of a signal peptide and transmembrane helices, both provided by the ExPASy platform, and using the GLYCOPP platform for glycosylation sites. Different programs, via, I-TASSER, RaptorX, and HHalign-Kbest, were used to perform three-dimensional modeling. RESULTS: HP0953 exhibited its maximum expression at 12 h of infection in gastric epithelium cells. Immunogold technique revealed HP0953 localization in the cytoplasm and accumulation in some peripheral areas of the bacterial body, with greater expression when it is close to AGS cells. Bioinformatics analysis revealed the presence of a signal peptide that interacts with the transmembrane region and then allows the release of the protein to the external environment. The programs also showed a similarity with the Tip-alpha protein of H. pylori. Tip-alpha is an exotoxin that penetrates cells and induces tumor necrosis factor alpha production, and HP0953 could have a similar function as posttranslational modification sites were found; modifications in turn require enzymes located in eukaryotic cells. Thus, to be functional, HP0953 may necessarily need to be translocated inside the cell where it can trigger different mechanisms producing cellular damage. CONCLUSION: The location of HP0953 around infected cells, the probable posttranslational modifications, and its similarity to an exotoxin suggest that this protein is a virulence factor. |
format | Online Article Text |
id | pubmed-9367236 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Baishideng Publishing Group Inc |
record_format | MEDLINE/PubMed |
spelling | pubmed-93672362022-09-23 HP0953 - hypothetical virulence factor overexpresion and localization during Helicobacter pylori infection of gastric epithelium Arteaga-Resendiz, Nancy K Rodea, Gerardo E Ribas-Aparicio, Rosa María Olivares-Cervantes, Alma L Castelán-Vega, Juan Arturo Olivares-Trejo, José de Jesús Mendoza-Elizalde, Sandra López-Villegas, Edgar O Colín, Christian Aguilar-Rodea, Pamela Reyes-López, Alfonso Salazar García, Marcela Velázquez-Guadarrama, Norma World J Gastroenterol Basic Study BACKGROUND: The high prevalence and persistence of Helicobacter pylori (H. pylori) infection, as well as the diversity of pathologies related to it, suggest that the virulence factors used by this microorganism are varied. Moreover, as its proteome contains 340 hypothetical proteins, it is important to investigate them to completely understand the mechanisms of its virulence and survival. We have previously reported that the hypothetical protein HP0953 is overexpressed during the first hours of adhesion to inert surfaces, under stress conditions, suggesting its role in the environmental survival of this bacterium and perhaps as a virulence factor. AIM: To investigate the expression and localization of HP0953 during adhesion to an inert surface and against gastric (AGS) cells. METHODS: Expression analysis was performed for HP0953 during H. pylori adhesion. HP0953 expression at 0, 3, 12, 24, and 48 h was evaluated and compared using the Kruskal-Wallis equality-of-populations rank test. Recombinant protein was produced and used to obtain polyclonal antibodies for immunolocalization. Immunogold technique was performed on bacterial sections during adherence to inert surfaces and AGS cells, which was analyzed by transmission electron microscopy. HP0953 protein sequence was analyzed to predict the presence of a signal peptide and transmembrane helices, both provided by the ExPASy platform, and using the GLYCOPP platform for glycosylation sites. Different programs, via, I-TASSER, RaptorX, and HHalign-Kbest, were used to perform three-dimensional modeling. RESULTS: HP0953 exhibited its maximum expression at 12 h of infection in gastric epithelium cells. Immunogold technique revealed HP0953 localization in the cytoplasm and accumulation in some peripheral areas of the bacterial body, with greater expression when it is close to AGS cells. Bioinformatics analysis revealed the presence of a signal peptide that interacts with the transmembrane region and then allows the release of the protein to the external environment. The programs also showed a similarity with the Tip-alpha protein of H. pylori. Tip-alpha is an exotoxin that penetrates cells and induces tumor necrosis factor alpha production, and HP0953 could have a similar function as posttranslational modification sites were found; modifications in turn require enzymes located in eukaryotic cells. Thus, to be functional, HP0953 may necessarily need to be translocated inside the cell where it can trigger different mechanisms producing cellular damage. CONCLUSION: The location of HP0953 around infected cells, the probable posttranslational modifications, and its similarity to an exotoxin suggest that this protein is a virulence factor. Baishideng Publishing Group Inc 2022-08-07 2022-08-07 /pmc/articles/PMC9367236/ /pubmed/36157534 http://dx.doi.org/10.3748/wjg.v28.i29.3886 Text en ©The Author(s) 2022. Published by Baishideng Publishing Group Inc. All rights reserved. https://creativecommons.org/licenses/by-nc/4.0/This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: https://creativecommons.org/Licenses/by-nc/4.0/ |
spellingShingle | Basic Study Arteaga-Resendiz, Nancy K Rodea, Gerardo E Ribas-Aparicio, Rosa María Olivares-Cervantes, Alma L Castelán-Vega, Juan Arturo Olivares-Trejo, José de Jesús Mendoza-Elizalde, Sandra López-Villegas, Edgar O Colín, Christian Aguilar-Rodea, Pamela Reyes-López, Alfonso Salazar García, Marcela Velázquez-Guadarrama, Norma HP0953 - hypothetical virulence factor overexpresion and localization during Helicobacter pylori infection of gastric epithelium |
title | HP0953 - hypothetical virulence factor overexpresion and localization during Helicobacter pylori infection of gastric epithelium |
title_full | HP0953 - hypothetical virulence factor overexpresion and localization during Helicobacter pylori infection of gastric epithelium |
title_fullStr | HP0953 - hypothetical virulence factor overexpresion and localization during Helicobacter pylori infection of gastric epithelium |
title_full_unstemmed | HP0953 - hypothetical virulence factor overexpresion and localization during Helicobacter pylori infection of gastric epithelium |
title_short | HP0953 - hypothetical virulence factor overexpresion and localization during Helicobacter pylori infection of gastric epithelium |
title_sort | hp0953 - hypothetical virulence factor overexpresion and localization during helicobacter pylori infection of gastric epithelium |
topic | Basic Study |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9367236/ https://www.ncbi.nlm.nih.gov/pubmed/36157534 http://dx.doi.org/10.3748/wjg.v28.i29.3886 |
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