Membrane bound monomer of Staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.

<h4>Background</h4>Wild type Staphylococcal alpha-hemolysin (alpha-HL) assembly on target mammalian cells usually results in necrotic form of cell death; however, caspase activation also occurs. The pathways of caspase activation due to binding/partial assembly by alpha-HL are unknown ti...

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Autores principales: Saumya S Srivastava, Satyabrata Pany, Amita Sneh, Neesar Ahmed, Aejazur Rahman, Krishnasastry V Musti
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Publicado: Public Library of Science (PLoS) 2009
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Acceso en línea:https://doaj.org/article/a47a6a8880ae4da0be153eea14ba6d5e
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spelling oai:doaj.org-article:a47a6a8880ae4da0be153eea14ba6d5e2021-11-25T06:21:31ZMembrane bound monomer of Staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.1932-620310.1371/journal.pone.0006293https://doaj.org/article/a47a6a8880ae4da0be153eea14ba6d5e2009-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19621082/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Wild type Staphylococcal alpha-hemolysin (alpha-HL) assembly on target mammalian cells usually results in necrotic form of cell death; however, caspase activation also occurs. The pathways of caspase activation due to binding/partial assembly by alpha-HL are unknown till date.<h4>Results</h4>Cells treated with H35N (a mutant of alpha-HL that remains as membrane bound monomer), have been shown to accumulate hypodiploid nuclei, activate caspases and induce intrinsic mitochondrial apoptotic pathway. We have earlier shown that the binding and assembly of alpha-HL requires functional form of Caveolin-1 which is an integral part of caveolae. In this report, we show that the caveolae of mammalian cells, which undergo a continuous cycle of 'kiss and run' dynamics with the plasma membrane, have become immobile upon the binding of the monomer. The cells treated with H35N were unable to recover despite activation of membrane repair mechanism involving caspase-1 dependent activation of sterol regulatory element binding protein-1.<h4>Conclusions</h4>This is for the first time we show the range of cellular changes and responses that take place immediately after the binding of the monomeric form of staphylococcal alpha-hemolysin.Saumya S SrivastavaSatyabrata PanyAmita SnehNeesar AhmedAejazur RahmanKrishnasastry V MustiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 7, p e6293 (2009)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Saumya S Srivastava
Satyabrata Pany
Amita Sneh
Neesar Ahmed
Aejazur Rahman
Krishnasastry V Musti
Membrane bound monomer of Staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.
description <h4>Background</h4>Wild type Staphylococcal alpha-hemolysin (alpha-HL) assembly on target mammalian cells usually results in necrotic form of cell death; however, caspase activation also occurs. The pathways of caspase activation due to binding/partial assembly by alpha-HL are unknown till date.<h4>Results</h4>Cells treated with H35N (a mutant of alpha-HL that remains as membrane bound monomer), have been shown to accumulate hypodiploid nuclei, activate caspases and induce intrinsic mitochondrial apoptotic pathway. We have earlier shown that the binding and assembly of alpha-HL requires functional form of Caveolin-1 which is an integral part of caveolae. In this report, we show that the caveolae of mammalian cells, which undergo a continuous cycle of 'kiss and run' dynamics with the plasma membrane, have become immobile upon the binding of the monomer. The cells treated with H35N were unable to recover despite activation of membrane repair mechanism involving caspase-1 dependent activation of sterol regulatory element binding protein-1.<h4>Conclusions</h4>This is for the first time we show the range of cellular changes and responses that take place immediately after the binding of the monomeric form of staphylococcal alpha-hemolysin.
format article
author Saumya S Srivastava
Satyabrata Pany
Amita Sneh
Neesar Ahmed
Aejazur Rahman
Krishnasastry V Musti
author_facet Saumya S Srivastava
Satyabrata Pany
Amita Sneh
Neesar Ahmed
Aejazur Rahman
Krishnasastry V Musti
author_sort Saumya S Srivastava
title Membrane bound monomer of Staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.
title_short Membrane bound monomer of Staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.
title_full Membrane bound monomer of Staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.
title_fullStr Membrane bound monomer of Staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.
title_full_unstemmed Membrane bound monomer of Staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.
title_sort membrane bound monomer of staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway.
publisher Public Library of Science (PLoS)
publishDate 2009
url https://doaj.org/article/a47a6a8880ae4da0be153eea14ba6d5e
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