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Article ; Online: The Need for Next-Generation Antivenom for Snakebite Envenomation in India.

Vanuopadath, Muralidharan / Rajan, Karthika / Alangode, Aswathy / Nair, Sudarslal Sadasivan / Nair, Bipin Gopalakrishnan

Toxins

2023 Volume 15, Issue 8

Abstract: The limitations posed by currently available antivenoms have emphasized the need for alternative treatments to counteract snakebite envenomation. Even though exact epidemiological data are lacking, reports have indicated that most global snakebite deaths ...

Abstract	The limitations posed by currently available antivenoms have emphasized the need for alternative treatments to counteract snakebite envenomation. Even though exact epidemiological data are lacking, reports have indicated that most global snakebite deaths are reported in India. Among the many problems associated with snakebite envenomation, issues related to the availability of safer and more efficient antivenoms are of primary concern. Since India has the highest number of global snakebite deaths, efforts should be made to reduce the burden associated with snakebite envenoming. Alternative methods, including aptamers, camel antivenoms, phage display techniques for generating high-affinity antibodies and antibody fragments, small-molecule inhibitors, and natural products, are currently being investigated for their effectiveness. These alternative methods have shown promise in vitro, but their in vivo effectiveness should also be evaluated. In this review, the issues associated with Indian polyvalent antivenoms in neutralizing venom components from geographically distant species are discussed in detail. In a nutshell, this review gives an overview of the current drawbacks of using animal-derived antivenoms and several alternative strategies that are currently being widely explored.
MeSH term(s)	Animals ; Humans ; Snake Bites/drug therapy ; Antivenins/therapeutic use ; Asian People ; Biological Products ; Camelus ; India
Chemical Substances	Antivenins ; Biological Products
Language	English
Publishing date	2023-08-18
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2518395-3
ISSN	2072-6651 ; 2072-6651
ISSN (online)	2072-6651
ISSN	2072-6651
DOI	10.3390/toxins15080510
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Article ; Online: Venomics and antivenomics of Indian spectacled cobra (Naja naja) from the Western Ghats.

Vanuopadath, Muralidharan / Raveendran, Dileepkumar / Nair, Bipin Gopalakrishnan / Nair, Sudarslal Sadasivan

Acta tropica

2022 Volume 228, Page(s) 106324

Abstract: Venom proteome profiling of Naja naja from the Western Ghats region in Kerala was achieved through SDS-PAGE and RP-HPLC followed by Q-TOF LC-MS/MS analysis, incorporating PEAKS and Novor assisted de novo sequencing methodologies. A total of 115 proteins ... ...

Abstract	Venom proteome profiling of Naja naja from the Western Ghats region in Kerala was achieved through SDS-PAGE and RP-HPLC followed by Q-TOF LC-MS/MS analysis, incorporating PEAKS and Novor assisted de novo sequencing methodologies. A total of 115 proteins distributed across 17 different enzymatic and non-enzymatic venom protein families were identified through conventional and 39 peptides through homology-driven proteomics approaches. Fourteen peptides derived through de novo complements the Mascot data indicating the importance of homology-driven approaches in improving protein sequence information. Among the protein families identified, glutathione peroxidase and endonuclease were reported for the first time in the Indian cobra venom. Immunological cross-reactivity assessed using Indian polyvalent antivenoms suggested that VINS showed better EC
MeSH term(s)	Animals ; Antivenins ; Chromatography, Liquid ; Elapid Venoms/analysis ; Naja naja/metabolism ; Proteome ; Tandem Mass Spectrometry
Chemical Substances	Antivenins ; Elapid Venoms ; Proteome
Language	English
Publishing date	2022-01-28
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	210415-5
ISSN	1873-6254 ; 0001-706X
ISSN (online)	1873-6254
ISSN	0001-706X
DOI	10.1016/j.actatropica.2022.106324
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Article: Venomics and antivenomics of Indian spectacled cobra (Naja naja) from the Western Ghats

Vanuopadath, Muralidharan / Raveendran, Dileepkumar / Nair, Bipin Gopalakrishnan / Nair, Sudarslal Sadasivan

Acta tropica. 2022 Apr., v. 228

2022

Abstract	Venom proteome profiling of Naja naja from the Western Ghats region in Kerala was achieved through SDS-PAGE and RP-HPLC followed by Q-TOF LC-MS/MS analysis, incorporating PEAKS and Novor assisted de novo sequencing methodologies. A total of 115 proteins distributed across 17 different enzymatic and non-enzymatic venom protein families were identified through conventional and 39 peptides through homology-driven proteomics approaches. Fourteen peptides derived through de novo complements the Mascot data indicating the importance of homology-driven approaches in improving protein sequence information. Among the protein families identified, glutathione peroxidase and endonuclease were reported for the first time in the Indian cobra venom. Immunological cross-reactivity assessed using Indian polyvalent antivenoms suggested that VINS showed better EC₅₀ (2.48 µg/mL) value than that of PSAV (6.04 µg/mL) and Virchow (6.03 µg/mL) antivenoms. Western blotting experiments indicated that all the antivenoms elicited poor binding specificities, especially towards low molecular mass proteins. Second-generation antivenomics studies revealed that VINS antivenom was less efficient to detect many low molecular mass proteins such as three-finger toxins and Kunitz-type serine protease Inhibitors. Taken together, the present study enabled a large-scale characterization of the venom proteome of Naja naja from the Western Ghats and emphasized the need for developing more efficient antivenoms.
Keywords	Naja naja ; amino acid sequences ; antivenoms ; cobra venoms ; cross reaction ; glutathione peroxidase ; molecular weight ; peptides ; polyacrylamide gel electrophoresis ; proteome ; proteomics ; serine proteinases ; India
Language	English
Dates of publication	2022-04
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	210415-5
ISSN	1873-6254 ; 0001-706X
ISSN (online)	1873-6254
ISSN	0001-706X
DOI	10.1016/j.actatropica.2022.106324
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Article: Aspergillus niger Culture Filtrate (ACF) Mediated Biocontrol of Enteric Pathogens in Wastewater

Subhash, Suja / Babu, Pradeesh / Vijayakumar, Amrutha / Suresh, Reshma Alookaran / Madhavan, Ajith / Nair, Bipin Gopalakrishnan / Pal, Sanjay

Water. 2022 Jan. 05, v. 14, no. 1

2022

Abstract: Robust control of pathogens in sewage facilitates safe reuse of wastewater rich in valuable nutrients for potential valorization through biological means. Aspergillus niger is widely reported in bioremediation of wastewater but studies on control of ... ...

Abstract	Robust control of pathogens in sewage facilitates safe reuse of wastewater rich in valuable nutrients for potential valorization through biological means. Aspergillus niger is widely reported in bioremediation of wastewater but studies on control of enteric pathogens in sewage are very sparse. So, this study aimed at exploring the antibacterial and nematicidal activity of A. niger culture filtrate (ACF). Antibacterial activity of ACF on enteric pathogens (Klebsiella pneumoniae, Pseudomonas aeruginosa, Vibrio cholerae, Salmonella enterica, Shigella dysenteriae, Escherichia coli, Staphylococcus aureus, Klebsiella variicola) was determined by spectrophotometric growth analysis, resazurin based viability assay and biofilm formation assay. ACF showed inhibition against all enteric pathogens except Pseudomonas aeruginosa. Nematicidal studies on Caenorhabditis elegans showed 85% egg hatch inhibition and 52% mortality of L1 larvae. Sewage treatment with ACF at 1:1 (v/v) showed 2–3 log reduction in coliforms, Klebsiella, Shigella, Salmonella, S. aureus and Vibrio except Pseudomonas, indicating significant alteration of complex microbial dynamics in wastewater. Application of ACF can potentially be used as a robust biocontrol strategy against infectious microbes in wastewater and subsequent valorization by cultivating beneficial Pseudomonas.
Keywords	Aspergillus niger ; Caenorhabditis elegans ; Escherichia coli ; Klebsiella pneumoniae ; Klebsiella variicola ; Pseudomonas aeruginosa ; Salmonella enterica ; Shigella dysenteriae ; Staphylococcus aureus ; Vibrio cholerae ; antibacterial properties ; biofilm ; biological control ; bioremediation ; culture filtrates ; eggs ; mortality ; nematicidal properties ; sewage ; sewage treatment ; viability assays ; wastewater ; water ; water reuse
Language	English
Dates of publication	2022-0105
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2521238-2
ISSN	2073-4441
ISSN	2073-4441
DOI	10.3390/w14010119
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Article ; Online: Identification of carbonylated proteins from monocytic cells under diabetes-induced stress conditions.

Nair, Divya / Nedungadi, Divya / Mishra, Nandita / Nair, Bipin Gopalakrishnan / Nair, Sudarslal Sadasivan

Biomedical chromatography : BMC

2021 Volume 35, Issue 6, Page(s) e5065

Abstract: Diabetes is a metabolic disorder characterized by the presence of elevated glucose in the blood and enhanced oxidative stress. It affects the cellular homeostasis that leads to the development of micro-and macro-vascular complications. Monocytes are the ... ...

Abstract	Diabetes is a metabolic disorder characterized by the presence of elevated glucose in the blood and enhanced oxidative stress. It affects the cellular homeostasis that leads to the development of micro-and macro-vascular complications. Monocytes are the primary immune cells present in the circulatory system. Under high-glucose conditions, the cells undergo oxidative stress and secrete reactive oxygen species. The enhanced release of reactive species is known to modify biomolecules like proteins and nucleic acids. Protein carbonylation, one of the most harmful and irreversible protein modifications, is considered as a key player in the progression of diabetes and associated complications. Hence, the present study explores the identification of carbonylated proteins from the monocytes under diabetic stress and determination of their site of modification. Combined avidin affinity chromatography and bottom-up proteomics experiments identified 13 consistently expressed carbonylated proteins. Most of the identified proteins were reported to have altered functions under diabetic conditions that contribute to the development of diabetes-associated inflammation and complications. We were able to determine oxidative stress-induced modifications on Lys, Val, Ile, Cys, Thr and Asp residues.
MeSH term(s)	Amino Acids/analysis ; Amino Acids/chemistry ; Amino Acids/metabolism ; Chromatography, Affinity ; Diabetes Mellitus/metabolism ; Glucose/pharmacology ; Humans ; Mass Spectrometry ; Monocytes/drug effects ; Monocytes/metabolism ; Oxidative Stress/drug effects ; Protein Carbonylation/drug effects ; Reactive Oxygen Species/analysis ; Reactive Oxygen Species/chemistry ; Reactive Oxygen Species/metabolism ; THP-1 Cells
Chemical Substances	Amino Acids ; Reactive Oxygen Species ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2021-01-18
Publishing country	England
Document type	Journal Article
ZDB-ID	632848-9
ISSN	1099-0801 ; 0269-3879
ISSN (online)	1099-0801
ISSN	0269-3879
DOI	10.1002/bmc.5065
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Article: Delineating the venom toxin arsenal of Malabar pit viper (Trimeresurus malabaricus) from the Western Ghats of India and evaluating its immunological cross-reactivity and in vitro cytotoxicity

Vanuopadath, Muralidharan / Shaji, Sanu Korumadathil / Raveendran, Dileepkumar / Nair, Bipin Gopalakrishnan / Nair, Sudarslal Sadasivan

International journal of biological macromolecules. 2020 Apr. 01, v. 148

2020

Abstract: The venom protein components of Malabar pit viper (Trimeresurus malabaricus) were identified by combining SDS-PAGE and ion-exchange chromatography pre-fractionation techniques with LC-MS/MS incorporating Novor and PEAKS-assisted de novo sequencing ... ...

Abstract	The venom protein components of Malabar pit viper (Trimeresurus malabaricus) were identified by combining SDS-PAGE and ion-exchange chromatography pre-fractionation techniques with LC-MS/MS incorporating Novor and PEAKS-assisted de novo sequencing strategies. Total 97 proteins that belong to 16 protein families such as L-amino acid oxidase, metalloprotease, serine protease, phospholipase A2, 5′-nucleotidase, C-type lectins/snaclecs and disintegrin were recognized from the venom of a single exemplar species. Of the 97 proteins, eighteen were identified through de novo approaches. Immunological cross-reactivity assessed through ELISA and western blot indicate that the Indian antivenoms binds less effectively to Malabar pit viper venom components compared to that of Russell's viper venom. The in vitro cell viability assays suggest that compared to the normal cells, MPV venom induces concentration dependent cell death in various cancer cells. Moreover, crude venom resulted in chromatin condensation and apoptotic bodies implying the induction of apoptosis. Taken together, the present study enabled in dissecting the venom proteome of Trimeresurus malabaricus and revealed the immuno-cross-reactivity profiles of commercially available Indian polyvalent antivenoms that, in turn, is expected to provide valuable insights on the need in improving antivenom preparations against its bite.
Keywords	Daboia russelii ; L-amino-acid oxidase ; Trimeresurus ; Western blotting ; amino acids ; antivenoms ; apoptosis ; cell viability ; chromatin ; cross reaction ; cytotoxicity ; enzyme-linked immunosorbent assay ; ion exchange chromatography ; lectins ; metalloproteinases ; neoplasm cells ; neoplasms ; phospholipase A2 ; phospholipases ; polyacrylamide gel electrophoresis ; proteome ; serine proteinases ; tandem mass spectrometry ; viability assays ; viper venoms ; India
Language	English
Dates of publication	2020-0401
Size	p. 1029-1045.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2020.01.226
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Article ; Online: Delineating the venom toxin arsenal of Malabar pit viper (Trimeresurus malabaricus) from the Western Ghats of India and evaluating its immunological cross-reactivity and in vitro cytotoxicity.

Vanuopadath, Muralidharan / Shaji, Sanu Korumadathil / Raveendran, Dileepkumar / Nair, Bipin Gopalakrishnan / Nair, Sudarslal Sadasivan

International journal of biological macromolecules

2020 Volume 148, Page(s) 1029–1045

Abstract	The venom protein components of Malabar pit viper (Trimeresurus malabaricus) were identified by combining SDS-PAGE and ion-exchange chromatography pre-fractionation techniques with LC-MS/MS incorporating Novor and PEAKS-assisted de novo sequencing strategies. Total 97 proteins that belong to 16 protein families such as L-amino acid oxidase, metalloprotease, serine protease, phospholipase A
MeSH term(s)	5'-Nucleotidase/chemistry ; Animals ; Antivenins/chemistry ; Apoptosis/drug effects ; Cell Line ; Cell Survival/drug effects ; Chromatography, High Pressure Liquid ; Crotalid Venoms/analysis ; Crotalid Venoms/enzymology ; Crotalid Venoms/toxicity ; Humans ; India ; L-Amino Acid Oxidase/chemistry ; Lectins, C-Type/chemistry ; Metalloproteases/chemistry ; Mice ; Phospholipases A2/chemistry ; Proteome/chemistry ; Daboia ; Serine Proteases/chemistry ; Tandem Mass Spectrometry ; Trimeresurus
Chemical Substances	Antivenins ; Crotalid Venoms ; Lectins, C-Type ; Proteome ; L-Amino Acid Oxidase (EC 1.4.3.2) ; Phospholipases A2 (EC 3.1.1.4) ; 5'-Nucleotidase (EC 3.1.3.5) ; Metalloproteases (EC 3.4.-) ; Serine Proteases (EC 3.4.-)
Language	English
Publishing date	2020-01-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2020.01.226
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Article ; Online: Identification, purification, biochemical and mass spectrometric characterization of novel phycobiliproteins from a marine red alga, Centroceras clavulatum.

Nair, Divya / Krishna, Jissa Gopala / Panikkar, Mamkoottathil Velayudhan Nataraja / Nair, Bipin Gopalakrishnan / Pai, Jayashree Gopalakrishna / Nair, Sudarslal Sadasivan

International journal of biological macromolecules

2018 Volume 114, Page(s) 679–691

Abstract: Phycobilisomes are light-harvesting protein complexes and are widely distributed in red algae and cyanobacteria. Each phycobilisome contains highly fluorescent protein components called phycobiliproteins. Based upon the distinct physiochemical properties, ...

Abstract	Phycobilisomes are light-harvesting protein complexes and are widely distributed in red algae and cyanobacteria. Each phycobilisome contains highly fluorescent protein components called phycobiliproteins. Based upon the distinct physiochemical properties, phycobiliproteins are classified as allophycocyanin, phycocyanin, phycoerythrin and phycoerythrocyanin. In the present study, we describe purification and structural characterization of a novel phycocyanin and phycoerythrin isolated from a marine red macroalga, Centroceras clavulatum. The absorbance and fluorescence studies indicated that the purified proteins belong to R-Phycocyanin (R-PC) and R-Phycoerythrin (R-PE). The single bands under native-polyacrylamide gel electrophoresis revealed the intact molecular weights of R-PC and R-PE as 110kDa and 250kDa. The polypeptide compositions of the two proteins were demonstrated by SDS-PAGE. The result showed that R-PC contains two bands at 17 and 21kDa and were identified as α and β subunits through mass spectrometry based proteomics experiments. SDS-PAGE of R-PE showed three distinct bands at 18, 19 and 35kDa and was subsequently identified as α, β and γ subunits. The near-complete amino acid sequences of α and β subunits of R-PC and R-PE were derived from mass spectrometric data combined with Mascot software and multiple de novo sequencing tools followed by homology search and manual validation.
MeSH term(s)	Phycobiliproteins/chemistry ; Phycobiliproteins/isolation & purification ; Plant Proteins/chemistry ; Plant Proteins/isolation & purification ; Rhodophyta/chemistry
Chemical Substances	Phycobiliproteins ; Plant Proteins
Language	English
Publishing date	2018-03-27
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2018.03.153
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Article: Phlorotannins from Padina tetrastromatica: structural characterisation and functional studies

Nair, Divya / Anil, Abhishek Nair / Balasubramanian, Akshaya / Bose, Chinchu / Ganesh, Shankar / Iyer, Akshay / Nair, Bipin Gopalakrishnan / Nair, Sudarslal Sadasivan / Pai, Jayashree Gopalakrishna / Pillai, Prasanth / Vanuopadath, Muralidharan / Vikraman, Vijesh

Journal of applied phycology. 2019 Oct., v. 31, no. 5

2019

Abstract: In this study, LC–MS/MS-based structural characterisation of phlorotannins from Padina tetrastromatica, a marine brown macroalga collected from South-West coastal region of Kerala, and its bioactivities are presented. The tandem mass spectrometric data ... ...

Abstract	In this study, LC–MS/MS-based structural characterisation of phlorotannins from Padina tetrastromatica, a marine brown macroalga collected from South-West coastal region of Kerala, and its bioactivities are presented. The tandem mass spectrometric data revealed a series of phlorotannins with degree of polymerisation ranging from 2 to 18. The characteristic neutral loss of tandem mass spectra further confirmed that these molecules belong to fucophlorethol class of phlorotannins. DPPH assay of the HPLC-purified, phlorotannin-enriched fraction possesses significant free radical-scavenging activity. Cell viability assay indicated that phlorotannin concentration ranging from 1.5 to 50.0 μg mL−1 is non-toxic to THP-1 cell lines. Anti-inflammatory assay performed through gelatin zymography confirmed that phlorotannins ameliorated high-glucose-induced pro-MMP-9 expression in a dose-dependent manner whereas the level of pro-MMP-2 remains unaltered. The antimicrobial assays carried out using both the crude and HPLC-purified phlorotannin fraction showed its anti-MRSA potential.
Keywords	2,2-diphenyl-1-picrylhydrazyl ; antioxidant activity ; cell lines ; cell viability ; coasts ; dose response ; free radical scavengers ; gelatin ; liquid chromatography ; macroalgae ; mass spectrometry ; Padina ; polymerization ; viability assays ; India
Language	English
Dates of publication	2019-10
Size	p. 3131-3141.
Publishing place	Springer Netherlands
Document type	Article
ZDB-ID	1002324-0
ISSN	1573-5176 ; 0921-8971
ISSN (online)	1573-5176
ISSN	0921-8971
DOI	10.1007/s10811-019-01792-y
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Article ; Online: Mass spectrometry-assisted venom profiling of Hypnale hypnale found in the Western Ghats of India incorporating de novo sequencing approaches.

Vanuopadath, Muralidharan / Sajeev, Nithin / Murali, Athira Radhamony / Sudish, Nayana / Kangosseri, Nithya / Sebastian, Ivy Rose / Jain, Nidhi Dalpatraj / Pal, Amit / Raveendran, Dileepkumar / Nair, Bipin Gopalakrishnan / Nair, Sudarslal Sadasivan

International journal of biological macromolecules

2018 Volume 118, Issue Pt B, Page(s) 1736–1746

Abstract: Hypnale hypnale (hump-nosed pit viper) is considered to be one among the medically important venomous snake species of India and Sri Lanka. In the present study, venom proteome profiling of a single Hypnale hypnale from Western Ghats of India was ... ...

Abstract	Hypnale hypnale (hump-nosed pit viper) is considered to be one among the medically important venomous snake species of India and Sri Lanka. In the present study, venom proteome profiling of a single Hypnale hypnale from Western Ghats of India was achieved using SDS-PAGE based protein separation followed by LC-MS/MS analysis. The identities of the proteins that were not established using the Mascot search were determined through de novo sequencing tools such as Novor followed by MS-BLAST based sequence similarity search algorithm and PEAKS proteomics software. The combined proteomics analysis revealed a total of 37 proteins belonging to nine different snake venom families, in which 7 proteins were exclusively identified through de novo strategies. The enzymatic and non-enzymatic venom protein families identified include serine proteases, metalloproteases, phospholipase A
MeSH term(s)	Amino Acid Sequence ; Chromatography, Liquid ; India ; Proteome ; Proteomics/methods ; Snake Venoms/analysis ; Snake Venoms/chemistry ; Tandem Mass Spectrometry
Chemical Substances	Proteome ; Snake Venoms
Language	English
Publishing date	2018-07-07
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2018.07.016
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