The Synergistic Role of Tip α, Nucleolin and Ras in Helicobacter pylori Infection Regulates the Cell Fate Towards Inflammation or Apoptosis
Infection with Helicobacter pylori ( H . pylori ) leads to a fork in the road situation where it is critical and complex to judge the fate of the cell. We propose for the first time an in silico representation of a protein level network model that can unfold the mystery behind the cell fate decision...
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Published in | Current microbiology Vol. 78; no. 10; pp. 3720 - 3732 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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01.10.2021
Springer Nature B.V |
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Abstract | Infection with
Helicobacter pylori
(
H
.
pylori
) leads to a fork in the road situation where it is critical and complex to judge the fate of the cell. We propose for the first time an in silico representation of a protein level network model that can unfold the mystery behind the cell fate decision between inflammation or cell proliferation or cell death. Upon infection TNF inducible protein α (Tip α) is internalised after binding with the cell surface receptor Nucleolin which is overexpressed on the cell surface thereby activating the Ras pathway. Tip α, Nucleolin and Ras decides the cell fate for apoptosis or abnormal cell proliferation along with ulcers in the gastric tract, hence we term it as the “death triad”, which otherwise triggers the inflammatory pathway through downstream signalling of NF-κβ. A series of proteins involved in the signalling cascade are portrayed through compartmentalization of the bacteria and the gut wall. The depicted network works synchronously toward an overarching goal of deciding between apoptosis or inflammation or proliferation. The model has been validated by simulating it with existing transcriptomic data along with clinical findings from patients infected with
H
.
pylori
across different regions in India. The results clearly indicate that for a short period of time there is increased binding of Tip α to Nucleolin and the receptor starts to saturate. This increases the tenacity of binding and the cell triggers an inflammatory cascade reaction which involves proinflammatory cytokines such as TNF α thereby progressing to inflammation by activating NF-κβ downstream. On the other hand, Ras involved in interaction with nucleolin can be present both in its activated or inactivated state. Binding of Tip α as a monomer leads to desensitization of Nucleolin leading to cell survival and proliferation. |
---|---|
AbstractList | Infection with
Helicobacter pylori
(
H
.
pylori
) leads to a fork in the road situation where it is critical and complex to judge the fate of the cell. We propose for the first time an in silico representation of a protein level network model that can unfold the mystery behind the cell fate decision between inflammation or cell proliferation or cell death. Upon infection TNF inducible protein α (Tip α) is internalised after binding with the cell surface receptor Nucleolin which is overexpressed on the cell surface thereby activating the Ras pathway. Tip α, Nucleolin and Ras decides the cell fate for apoptosis or abnormal cell proliferation along with ulcers in the gastric tract, hence we term it as the “death triad”, which otherwise triggers the inflammatory pathway through downstream signalling of NF-κβ. A series of proteins involved in the signalling cascade are portrayed through compartmentalization of the bacteria and the gut wall. The depicted network works synchronously toward an overarching goal of deciding between apoptosis or inflammation or proliferation. The model has been validated by simulating it with existing transcriptomic data along with clinical findings from patients infected with
H
.
pylori
across different regions in India. The results clearly indicate that for a short period of time there is increased binding of Tip α to Nucleolin and the receptor starts to saturate. This increases the tenacity of binding and the cell triggers an inflammatory cascade reaction which involves proinflammatory cytokines such as TNF α thereby progressing to inflammation by activating NF-κβ downstream. On the other hand, Ras involved in interaction with nucleolin can be present both in its activated or inactivated state. Binding of Tip α as a monomer leads to desensitization of Nucleolin leading to cell survival and proliferation. Infection with Helicobacter pylori (H. pylori) leads to a fork in the road situation where it is critical and complex to judge the fate of the cell. We propose for the first time an in silico representation of a protein level network model that can unfold the mystery behind the cell fate decision between inflammation or cell proliferation or cell death. Upon infection TNF inducible protein α (Tip α) is internalised after binding with the cell surface receptor Nucleolin which is overexpressed on the cell surface thereby activating the Ras pathway. Tip α, Nucleolin and Ras decides the cell fate for apoptosis or abnormal cell proliferation along with ulcers in the gastric tract, hence we term it as the "death triad", which otherwise triggers the inflammatory pathway through downstream signalling of NF-κβ. A series of proteins involved in the signalling cascade are portrayed through compartmentalization of the bacteria and the gut wall. The depicted network works synchronously toward an overarching goal of deciding between apoptosis or inflammation or proliferation. The model has been validated by simulating it with existing transcriptomic data along with clinical findings from patients infected with H. pylori across different regions in India. The results clearly indicate that for a short period of time there is increased binding of Tip α to Nucleolin and the receptor starts to saturate. This increases the tenacity of binding and the cell triggers an inflammatory cascade reaction which involves proinflammatory cytokines such as TNF α thereby progressing to inflammation by activating NF-κβ downstream. On the other hand, Ras involved in interaction with nucleolin can be present both in its activated or inactivated state. Binding of Tip α as a monomer leads to desensitization of Nucleolin leading to cell survival and proliferation. Infection with Helicobacter pylori (H. pylori) leads to a fork in the road situation where it is critical and complex to judge the fate of the cell. We propose for the first time an in silico representation of a protein level network model that can unfold the mystery behind the cell fate decision between inflammation or cell proliferation or cell death. Upon infection TNF inducible protein α (Tip α) is internalised after binding with the cell surface receptor Nucleolin which is overexpressed on the cell surface thereby activating the Ras pathway. Tip α, Nucleolin and Ras decides the cell fate for apoptosis or abnormal cell proliferation along with ulcers in the gastric tract, hence we term it as the "death triad", which otherwise triggers the inflammatory pathway through downstream signalling of NF-κβ. A series of proteins involved in the signalling cascade are portrayed through compartmentalization of the bacteria and the gut wall. The depicted network works synchronously toward an overarching goal of deciding between apoptosis or inflammation or proliferation. The model has been validated by simulating it with existing transcriptomic data along with clinical findings from patients infected with H. pylori across different regions in India. The results clearly indicate that for a short period of time there is increased binding of Tip α to Nucleolin and the receptor starts to saturate. This increases the tenacity of binding and the cell triggers an inflammatory cascade reaction which involves proinflammatory cytokines such as TNF α thereby progressing to inflammation by activating NF-κβ downstream. On the other hand, Ras involved in interaction with nucleolin can be present both in its activated or inactivated state. Binding of Tip α as a monomer leads to desensitization of Nucleolin leading to cell survival and proliferation. |
Author | Gehlot, Valentina Bose, Sudeep Chakraborty, Amlan Das, Kunal Mahant, Shweta Mukhopadhyay, Asish Kumar Das, Rajashree Som, Anup Mehra, Shubham |
Author_xml | – sequence: 1 givenname: Shweta surname: Mahant fullname: Mahant, Shweta organization: Amity Institute of Biotechnology, Amity University – sequence: 2 givenname: Amlan surname: Chakraborty fullname: Chakraborty, Amlan organization: Department of Pharmacology, Biomedicine Discovery Institute, Monash University, Victorian Heart Institute, Monash University – sequence: 3 givenname: Anup surname: Som fullname: Som, Anup organization: Centre of Bioinformatics, University of Allahabad – sequence: 4 givenname: Shubham surname: Mehra fullname: Mehra, Shubham organization: Amity Institute of Biotechnology, Amity University – sequence: 5 givenname: Kunal surname: Das fullname: Das, Kunal organization: Department of Gastroenterology, Manipal Hospital – sequence: 6 givenname: Asish Kumar surname: Mukhopadhyay fullname: Mukhopadhyay, Asish Kumar organization: Division of Bacteriology, National Institute of Cholera and Enteric Diseases – sequence: 7 givenname: Valentina surname: Gehlot fullname: Gehlot, Valentina organization: Amity Institute of Biotechnology, Amity University – sequence: 8 givenname: Sudeep surname: Bose fullname: Bose, Sudeep email: sbose1@amity.edu organization: Amity Institute of Biotechnology, Amity University – sequence: 9 givenname: Rajashree orcidid: 0000-0003-1202-4942 surname: Das fullname: Das, Rajashree email: rajashreepatra79@yahoo.co.in, rdas@amity.edu organization: Amity Institute of Biotechnology, Amity University |
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Cites_doi | 10.1128/JCM.37.7.2274-2279.1999 10.1038/nbt1156 10.1136/gut.48.3.290 10.1136/jcp.2005.036111 10.1111/cmi.13006 10.3748/wjg.v20.i21.6374 10.1128/IAI.71.6.3529-3539.2003 10.1007/s00284-007-9083-7 10.1016/j.yexcr.2008.03.016 10.4161/cib.4.3.14884 10.1248/bpb.33.796 10.1093/nar/29.9.e45 10.1016/j.bbrc.2009.07.121 10.1158/0008-5472.CAN-10-2887 10.1016/j.str.2011.04.006 10.1074/jbc.RA119.009981 10.1371/journal.pone.0075269 10.1111/j.1523-5378.2008.00633.x 10.1073/pnas.93.25.14648 10.1096/fasebj.13.14.1911 10.1093/bioinformatics/btg015 10.1371/journal.pone.0015787 10.1177/1947601911411084 10.2478/v10052-008-0003-1 10.1016/S0016-5085(97)70223-3 10.1093/molbev/msm092 10.1002/ijc.23484 10.1038/embor.2009.210 10.1038/nrc2857 10.1158/1535-7163.MCT-05-0361 10.1016/j.sjbs.2012.10.006 |
ContentType | Journal Article |
Copyright | The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021. |
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Snippet | Infection with
Helicobacter pylori
(
H
.
pylori
) leads to a fork in the road situation where it is critical and complex to judge the fate of the cell. We... Infection with Helicobacter pylori (H. pylori) leads to a fork in the road situation where it is critical and complex to judge the fate of the cell. We propose... |
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SubjectTerms | Apoptosis Bacterial Proteins - metabolism Binding Biomedical and Life Sciences Biotechnology Cascade chemical reactions Cell death Cell fate Cell growth Cell proliferation Cell surface Cell survival Cytokines Desensitization Gastric Mucosa Helicobacter Infections Helicobacter pylori Humans Infections Inflammation Life Sciences Microbiology Nucleolin Phosphoproteins Proteins Ras protein ras Proteins - metabolism Receptors RNA-Binding Proteins Signal transduction Signaling Tumor necrosis factor Tumor Necrosis Factor-alpha Ulcers |
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Title | The Synergistic Role of Tip α, Nucleolin and Ras in Helicobacter pylori Infection Regulates the Cell Fate Towards Inflammation or Apoptosis |
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