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Book: Biochemical and biophysical roles of cell surface molecules

Chattopadhyay, Kausik / Basu, Subhash

(Advances in experimental medicine and biology ; 1112)

2018

Author's details	Kausik Chattopadhyay, Subhash C. Basu editors
Series title	Advances in experimental medicine and biology ; 1112
Collection
Keywords	Cell Membrane ; Cell Surface Receptors ; Cholesterol ; Glycolipids ; Glycoprotein
Subject code	570
Language	English
Size	xi, 363 Seiten, Illustrationen, Diagramme, 25.4 cm x 17.8 cm
Publisher	Springer
Publishing place	Singapore
Publishing country	Singapore
Document type	Book
HBZ-ID	HT019984268
ISBN	978-981-13-3064-3 ; 981-13-3064-6 ; 9789811330650 ; 9811330654
Database	Catalogue ZB MED Medicine, Health

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Article: Current Perspective on the Membrane-Damaging Action of Thermostable Direct Hemolysin, an Atypical Bacterial Pore-forming Toxin.

Verma, Pratima / Chattopadhyay, Kausik

Frontiers in molecular biosciences

2021 Volume 8, Page(s) 717147

Abstract: Thermostable direct hemolysin (TDH) is the major virulence determinant of the gastroenteric bacterial ... ...

Abstract	Thermostable direct hemolysin (TDH) is the major virulence determinant of the gastroenteric bacterial pathogen
Language	English
Publishing date	2021-07-23
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2021.717147
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Article ; Online: Current Perspective on the Membrane-Damaging Action of Thermostable Direct Hemolysin, an Atypical Bacterial Pore-forming Toxin

Pratima Verma / Kausik Chattopadhyay

Frontiers in Molecular Biosciences, Vol

2021 Volume 8

Abstract: Thermostable direct hemolysin (TDH) is the major virulence determinant of the gastroenteric bacterial pathogen Vibrio parahaemolyticus. TDH is a membrane-damaging pore-forming toxin (PFT). TDH shares remarkable structural similarity with the actinoporin ... ...

Abstract	Thermostable direct hemolysin (TDH) is the major virulence determinant of the gastroenteric bacterial pathogen Vibrio parahaemolyticus. TDH is a membrane-damaging pore-forming toxin (PFT). TDH shares remarkable structural similarity with the actinoporin family of eukaryotic PFTs produced by the sea anemones. Unlike most of the PFTs, it exists as tetramer in solution, and such assembly state is crucial for its functionality. Although the structure of the tetrameric assembly of TDH in solution is known, membrane pore structure is not available yet. Also, the specific membrane-interaction mechanisms of TDH, and the exact role of any receptor(s) in such process, still remain unclear. In this mini review, we discuss some of the unique structural and physicochemical properties of TDH, and their implications for the membrane-damaging action of the toxin. We also present our current understanding regarding the membrane pore-formation mechanism of this atypical bacterial PFT.
Keywords	pore-forming toxin ; thermostable direct hemolysin ; membranes ; actinoporins ; oligomer ; Biology (General) ; QH301-705.5
Subject code	612
Language	English
Publishing date	2021-07-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
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Article ; Online: Structures and functions of the membrane-damaging pore-forming proteins.

Mondal, Anish Kumar / Chattopadhyay, Kausik

Advances in protein chemistry and structural biology

2021 Volume 128, Page(s) 241–288

Abstract: Pore-forming proteins (PFPs) of the diverse life forms have emerged as the potent cell-killing entities owing to their specialized membrane-damaging properties. PFPs have the unique ability to perforate the plasma membranes of their target cells, and ... ...

Abstract	Pore-forming proteins (PFPs) of the diverse life forms have emerged as the potent cell-killing entities owing to their specialized membrane-damaging properties. PFPs have the unique ability to perforate the plasma membranes of their target cells, and they exert this functionality by creating oligomeric pores in the membrane lipid bilayer. Pathogenic bacteria employ PFPs as toxins to execute their virulence mechanisms, whereas in the higher vertebrates PFPs are deployed as the part of the immune system and to generate inflammatory responses. PFPs are the unique dimorphic proteins that are generally synthesized as water-soluble molecules, and transform into membrane-inserted oligomeric pore assemblies upon interacting with the target membranes. In spite of sharing very little sequence similarity, PFPs from diverse organisms display incredible structural similarity. Yet, at the same time, structure-function mechanisms of the PFPs document remarkable versatility. Such notions establish PFPs as the fascinating model system to explore variety of unsolved issues pertaining to the structure-function paradigm of the proteins that interact and act in the membrane environment. In this article, we discuss our current understanding regarding the structural basis of the pore-forming functions of the diverse class of PFPs. We attempt to highlight the similarities and differences in their structures, membrane pore-formation mechanisms, and their implications for the various biological processes, ranging from the bacterial virulence mechanisms to the inflammatory immune response generation in the higher animals.
MeSH term(s)	Animals ; Bacteria ; Cell Membrane
Language	English
Publishing date	2021-07-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1876-1631 ; 1876-1623
ISSN (online)	1876-1631
ISSN	1876-1623
DOI	10.1016/bs.apcsb.2021.07.001
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Article ; Online: Membrane Dynamics and Remodelling in Response to the Action of the Membrane-Damaging Pore-Forming Toxins.

Lata, Kusum / Singh, Mahendra / Chatterjee, Shamaita / Chattopadhyay, Kausik

The Journal of membrane biology

2022 Volume 255, Issue 2-3, Page(s) 161–173

Abstract: Pore-forming protein toxins (PFTs) represent a diverse class of membrane-damaging proteins that are produced by a wide variety of organisms. PFT-mediated membrane perforation is largely governed by the chemical composition and the physical properties of ... ...

Abstract	Pore-forming protein toxins (PFTs) represent a diverse class of membrane-damaging proteins that are produced by a wide variety of organisms. PFT-mediated membrane perforation is largely governed by the chemical composition and the physical properties of the plasma membranes. The interaction between the PFTs with the target membranes is critical for the initiation of the pore-formation process, and can lead to discrete membrane reorganization events that further aids in the process of pore-formation. Punching holes on the plasma membranes by the PFTs interferes with the cellular homeostasis by disrupting the ion-balance inside the cells that in turn can turn on multiple signalling cascades required to restore membrane integrity and cellular homeostasis. In this review, we discuss the physicochemical attributes of the plasma membranes associated with the pore-formation processes by the PFTs, and the subsequent membrane remodelling events that may start off the membrane-repair mechanisms.
MeSH term(s)	Cell Membrane/metabolism ; Membranes ; Pore Forming Cytotoxic Proteins/chemistry ; Toxins, Biological/metabolism
Chemical Substances	Pore Forming Cytotoxic Proteins ; Toxins, Biological
Language	English
Publishing date	2022-03-19
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	3082-x
ISSN	1432-1424 ; 0022-2631
ISSN (online)	1432-1424
ISSN	0022-2631
DOI	10.1007/s00232-022-00227-z
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Article ; Online: Unveiling the Role of Hidden Isomers in Large Stokes Shift in mKeima: Harnessing pH-Sensitive Dual-Emission in Bioimaging.

Bhutani, Garima / Verma, Pratima / Jayachandran, Ajay / Paul, Sasthi / Chattopadhyay, Kausik / De, Arijit K

The journal of physical chemistry. B

2023 Volume 127, Issue 14, Page(s) 3197–3207

Abstract: Elucidating the origin of large Stokes shift (LSS) in certain fluorescent proteins absorbing in blue/blue-green and emitting in red/far-red has been quite illusive. Using a combination of spectroscopic measurements, corroborated by theoretical ... ...

Abstract	Elucidating the origin of large Stokes shift (LSS) in certain fluorescent proteins absorbing in blue/blue-green and emitting in red/far-red has been quite illusive. Using a combination of spectroscopic measurements, corroborated by theoretical calculations, the presence of four distinct forms of the chromophore of the red fluorescent protein mKeima is confirmed, two of which are found to be emissive: a feeble bluish-green fluorescence (∼520 nm), which is enhanced appreciably in a low pH or deuterated medium but significantly at cryogenic temperatures, and a strong emission in red (∼615 nm). Using femtosecond transient absorption spectroscopy, the trans-protonated form is found to isomerize within hundreds of femtoseconds to the cis-protonated form, which further yields the cis-deprotonated form within picoseconds followed by structural reorganization of the local environment of the chromophore. Thus, the mechanism of LSS is substantiated to proceed via stepwise excited-state isomerization followed by proton transfer involving three isomers, leaving the fourth one (trans-deprotonated) as a bystander. The exquisite pH sensitivity of the dual emission is further exploited in fluorescence microscopy.
MeSH term(s)	Isomerism ; Luminescent Proteins/chemistry ; Protons ; Spectrum Analysis ; Temperature ; Hydrogen-Ion Concentration ; Green Fluorescent Proteins/chemistry
Chemical Substances	Luminescent Proteins ; Protons ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2023-04-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1520-5207
ISSN (online)	1520-5207
DOI	10.1021/acs.jpcb.3c01531
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Article ; Online: Vibrio parahaemolyticus thermostable direct haemolysin induces non-classical programmed cell death despite caspase activation.

Verma, Pratima / Chauhan, Aakanksha / Thakur, Reena / Lata, Kusum / Sharma, Arpita / Chattopadhyay, Kausik / Mukhopadhaya, Arunika

Molecular microbiology

2023 Volume 120, Issue 6, Page(s) 845–873

Abstract: Thermostable direct haemolysin (TDH) is the key virulence factor secreted by the human gastroenteric bacterial pathogen Vibrio parahaemolyticus. TDH is a membrane-damaging pore-forming toxin. It evokes potent cytotoxicity, the mechanism of which still ... ...

Abstract	Thermostable direct haemolysin (TDH) is the key virulence factor secreted by the human gastroenteric bacterial pathogen Vibrio parahaemolyticus. TDH is a membrane-damaging pore-forming toxin. It evokes potent cytotoxicity, the mechanism of which still remains under-explored. Here, we have elucidated the mechanistic details of cell death response elicited by TDH. Employing Caco-2 intestinal epithelial cells and THP-1 monocytic cells, we show that TDH induces some of the hallmark features of apoptosis-like programmed cell death. TDH triggers caspase-3 and 7 activations in the THP-1 cells, while caspase-7 activation is observed in the Caco-2 cells. Interestingly, TDH appears to induce caspase-independent cell death. Higher XIAP level and lower Smac/Diablo level upon TDH intoxication provide plausible explanation for the functional inability of caspases in the THP-1 cells, in particular. Further exploration reveals that mitochondria play a central role in the TDH-induced cell death. TDH triggers mitochondrial damage, resulting in the release of AIF and endonuclease G, responsible for the execution of caspase-independent cell death. Among the other critical mediators of cell death, ROS is found to play an important role in the THP-1 cells, while PARP-1 appears to play a critical role in the Caco-2 cells. Altogether, our work provides critical new insights into the mechanism of cell death induction by TDH, showing a common central theme of non-classical programmed cell death. Our study also unravels the interplay of crucial molecules in the underlying signalling processes. Our findings add valuable insights into the role of TDH in the context of the host-pathogen interaction processes.
MeSH term(s)	Humans ; Caco-2 Cells ; Vibrio parahaemolyticus ; Apoptosis ; Caspases
Chemical Substances	thermostable direct hemolysin (135433-21-5) ; Caspases (EC 3.4.22.-)
Language	English
Publishing date	2023-10-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.15180
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Article: Curcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming Toxin

Singh, Mahendra / Rupesh, N / Pandit, Shashi Bhushan / Chattopadhyay, Kausik

Frontiers in microbiology

2022 Volume 12, Page(s) 809782

Abstract: Vibrio cholerae cytolysin (VCC) is a β-barrel pore-forming toxin (β-PFT). Upon encountering the target cells, VCC forms heptameric β-barrel pores and permeabilizes the cell membranes. Structure-function mechanisms of VCC have been extensively studied in ... ...

Abstract	Vibrio cholerae cytolysin (VCC) is a β-barrel pore-forming toxin (β-PFT). Upon encountering the target cells, VCC forms heptameric β-barrel pores and permeabilizes the cell membranes. Structure-function mechanisms of VCC have been extensively studied in the past. However, the existence of any natural inhibitor for VCC has not been reported yet. In the present study, we show that curcumin can compromise the membrane-damaging activity of VCC. Curcumin is known to modulate a wide variety of biological processes and functions. However, the application of curcumin in the physiological scenario often gets limited due to its extremely poor solubility in the aqueous environment. Interestingly, we find that VCC can associate with the insoluble fraction of curcumin in the aqueous medium and thus gets separated from the solution phase. This, in turn, reduces the availability of VCC to attack the target membranes and thus blocks the membrane-damaging action of the toxin. We also observe that the soluble aqueous extract of curcumin, generated by the heat treatment, compromises the pore-forming activity of VCC. Interestingly, in the presence of such soluble extract of curcumin, VCC binds to the target membranes and forms the oligomeric assembly. However, such oligomers appear to be non-functional, devoid of the pore-forming activity. The ability of curcumin to bind to VCC and neutralize its membrane-damaging activity suggests that curcumin has the potential to act as an inhibitor of this potent bacterial β-PFT.
Language	English
Publishing date	2022-01-24
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.809782
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Article ; Online: Scrub typhus with cerebral venous sinus thrombosis: a rare presentation.

Das, Sayonee / Chattopadhyay, Sidhartha / Munsi, Kausik / Basu, Sagar

BMJ case reports

2021 Volume 14, Issue 4

Abstract: This is a rare presentation of scrub typhus with cerebral venous thrombosis. A 32-year-old woman presented with signs of raised intracranial tension. Examination revealed maculopapular skin rashes and an 'eschar' over the right thigh. Nuchal rigidity and ...

Abstract	This is a rare presentation of scrub typhus with cerebral venous thrombosis. A 32-year-old woman presented with signs of raised intracranial tension. Examination revealed maculopapular skin rashes and an 'eschar' over the right thigh. Nuchal rigidity and bilateral papilloedema were found. Scrub typhus was diagnosed by the presence of IgM antibody in serum. CT scan of the brain showed cerebral oedema. MRI of the brain was normal. Magnetic resonance venography of the brain showed thrombosis of several venous sinuses. Cerebrospinal fluid analysis revealed lymphocytic pleocytosis with raised protein level. Other causes of prothrombotic states were ruled out by doing specific test results. There was no history of hormonal contraception and prolonged bed rest. A case of scrub typhus complicated with meningoencephalitis and cerebral venous thrombosis was diagnosed. She responded to treatment with doxycycline, anticoagulants, antipyrectics and intravenous saline. Early identification of such atypical neurological involvement in scrub typhus was helpful in satisfactory outcome.
MeSH term(s)	Adult ; Doxycycline ; Female ; Humans ; Immunoglobulin M ; Magnetic Resonance Imaging ; Scrub Typhus/complications ; Scrub Typhus/diagnosis ; Scrub Typhus/drug therapy ; Sinus Thrombosis, Intracranial/diagnostic imaging ; Sinus Thrombosis, Intracranial/drug therapy
Chemical Substances	Immunoglobulin M ; Doxycycline (N12000U13O)
Language	English
Publishing date	2021-04-28
Publishing country	England
Document type	Case Reports ; Journal Article
ISSN	1757-790X
ISSN (online)	1757-790X
DOI	10.1136/bcr-2020-241401
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Article ; Online: Pore-forming toxins in infection and immunity.

Verma, Pratima / Gandhi, Shraddha / Lata, Kusum / Chattopadhyay, Kausik

Biochemical Society transactions

2021 Volume 49, Issue 1, Page(s) 455–465

Abstract: The integrity of the plasma membranes is extremely crucial for the survival and proper functioning of the cells. Organisms from all kingdoms of life employ specialized pore-forming proteins and toxins (PFPs and PFTs) that perforate cell membranes, and ... ...

Abstract	The integrity of the plasma membranes is extremely crucial for the survival and proper functioning of the cells. Organisms from all kingdoms of life employ specialized pore-forming proteins and toxins (PFPs and PFTs) that perforate cell membranes, and cause detrimental effects. PFPs/PFTs exert their damaging actions by forming oligomeric pores in the membrane lipid bilayer. PFPs/PFTs play important roles in diverse biological processes. Many pathogenic bacteria secrete PFTs for executing their virulence mechanisms. The immune system of the higher vertebrates employs PFPs to kill pathogen-infected cells and transformed cancer cells. The most obvious consequence of membrane pore-formation by the PFPs/PFTs is the killing of the target cells due to the disruption of the permeability barrier function of the plasma membranes. PFPs/PFTs can also activate diverse cellular processes that include activation of the stress-response pathways, induction of programmed cell death, and inflammation. Upon attack by the PFTs, host cells may also activate pathways to repair the injured membranes, restore cellular homeostasis, and trigger inflammatory immune responses. In this article, we present an overview of the diverse cellular responses that are triggered by the PFPs/PFTs, and their implications in the process of pathogen infection and immunity.
MeSH term(s)	Animals ; Cell Membrane/drug effects ; Humans ; Immunity/drug effects ; Immunity/physiology ; Infections/immunology ; Infections/pathology ; Lipid Bilayers/metabolism ; Pore Forming Cytotoxic Proteins/pharmacology ; Toxins, Biological/pharmacology ; Virulence/physiology
Chemical Substances	Lipid Bilayers ; Pore Forming Cytotoxic Proteins ; Toxins, Biological
Language	English
Publishing date	2021-01-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20200836
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