Proteomic analysis and antivenomics study of Western India<i>Naja naja</i>venom: correlation between venom composition and clinical manifestations of cobra bite in this region

Chanda, Abhishek; Kalita, Bhargab; Patra, Aparup; Senevirathne, W.D.S.T.; Mukherjee, Ashis K.

doi:10.1080/14789450.2019.1559735

Cited by 47 publications

(53 citation statements)

References 53 publications

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“…Though SDS-PAGE analysis (Figure 2a) reveal presence of low and high molecular mass proteins in SSV and HPV venoms, the western-blotting indicate that all the tested antivenoms bind less efficiently to low and high molecular mass proteins present in HPV venom than that in the SSV (Figure 2 bd). The inadequacy of polyvalent antivenoms in detecting low and high molecular mass proteins present in different snake species has been reported by various groups, which is in agreement with our finding [6][7][8][9][10]. Further, we have observed that the binding specificity of VINS and PSAV antivenoms (Figure 2b & c) were better than Virchow antivenom (Figure 2d) in detecting HPV venom epitopes.…”

Section: Resultssupporting

confidence: 92%

“…In India, the antivenom manufacturers solely depend on the Irula Snake Catchers Industrial Cooperative Society (Tamilnadu, South-India) for obtaining venoms used for the immunization process [4]. However, several in vitro preclinical studies indicate that the immuno-recognition potential of these antivenoms towards the venom toxins present even in the 'big four' snakes from different geographical locations seems to be varied [6][7][8][9]. Besides these, studies have shown that available Indian polyvalent antivenoms are not effective in neutralizing venom components present in the 'non-big four', yet medically-relevant snake species including Trimeresurus malabaricus, Naja kaouthia, Echis carinatus sochureki, Bungarus fasciatus and Bungarus sindanus [10,11].…”

Section: Introductionmentioning

confidence: 99%

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Evaluating the Immunological cross-reactivity of Indian polyvalent antivenoms towards the venom ofHypnale hypnale(hump-nosed pit viper) from the Western Ghats

Vanuopadath¹,

Dileepkumar

Nair³

et al. 2020

Preprint

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Hypnale hypnale (hump-nosed pit viper) is a venomous pit viper species found in the Western Ghats of India and Sri Lanka. Due to the severe life-threatening envenomation effects induced by its venom components, Hypnale hypnale has been classified under ″category 1″ of medically important snake species by the World Health Organization. Since there are no specific antivenoms available to combat its envenomation in India, the only option available is to administer Indian polyvalent antivenoms. However, the cross-neutralization potential of the commercially available polyvalent antivenoms on Indian Hypnale hypnale venom has not been explored so far. In the current study, in vitro immunological cross-reactivity of Hypnale hypnale venom towards various Indian polyvalent antivenoms were assessed using end point titration ELISA and Western blotting. A three to four-fold increase in EC50 values were obtained for Hypnale hypnale venom towards all the antivenoms tested. Observation of minimal binding specificities towards low and high molecular mass venom proteins are suggestive of the fact that commercially available polyvalent antivenoms failed to detect and bind to the antigenic epitopes of considerable number of proteins present in Hypnale hypnale venom. This highlights the importance of including Hypnale hypnale venom in the immunization mixture while raising antivenoms.

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Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Evaluating the Immunological cross-reactivity of Indian polyvalent antivenoms towards the venom ofHypnale hypnale(hump-nosed pit viper) from the Western Ghats

Vanuopadath¹,

Dileepkumar

Nair³

et al. 2020

Preprint

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“…The presence of Ras-like protein demonstrates the presence of extracellular vesicles in the venom of Naja naja. The comparison of our proteomic data with that of N. naja snake both from western and eastern India, reveals that such proteins were not identified in Indian N. naja , Further in Pakistani Naja naja snake we not could identify cholinesterase, butyrylcholinesterase, hyalurinidase and snaclec proteins which were previously reported in Indian N. naja venom [ 45 , 46 ].…”

Section: Resultsmentioning

confidence: 61%

“…In Table 1 , the protein families discovered and reported for the first time in terms of our investigations are shown with check mark (✓). Interestingly previous studies reported PLA 2 as the second most abundant protein family found in N. naja venom, and that SVMP was present in relatively low abundance [ 8 , 42 , 43 , 44 , 45 , 46 ]. In contrast, our data showed SVMP as the second most abundant protein family in N. naja.…”

Section: Resultsmentioning

confidence: 99%

“…These research groups performed pre fractionation of the venom sample either by reverse phase chromatography, 1-dimensional gel electrophoresis (1D gel) or 2-dimensional gel electrophoresis (2 D gel) or a combination of these methods. Further mass spectrometric analysis of peptide fragments obtained from in gel trypsin digestion, was carried out by MALDI TOF/TOF, ion trap or ESI MS. Chanda et al also reported the venom proteomics of N. naja , from Western and Eastern parts of India [ 45 , 46 ]. In their study of the venom sample from East India, they pre fractionated the crude venom by 1D gel prior to LTQ orbitrap analysis.…”

Section: Introductionmentioning

confidence: 99%

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Proteomic Investigations of Two Pakistani Naja Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles

Manuwar

Dreyer

Böhmert

et al. 2020

Toxins

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Latest advancement of omics technologies allows in-depth characterization of venom compositions. In the present work we present a proteomic study of two snake venoms of the genus Naja i.e., Naja naja (black cobra) and Naja oxiana (brown cobra) of Pakistani origin. The present study has shown that these snake venoms consist of a highly diversified proteome. Furthermore, the data also revealed variation among closely related species. High throughput mass spectrometric analysis of the venom proteome allowed to identify for the N. naja venom 34 protein families and for the N. oxiana 24 protein families. The comparative evaluation of the two venoms showed that N. naja consists of a more complex venom proteome than N. oxiana venom. Analysis also showed N-terminal acetylation (N-ace) of a few proteins in both venoms. To the best of our knowledge, this is the first study revealing this posttranslational modification in snake venom. N-ace can shed light on the mechanism of regulation of venom proteins inside the venom gland. Furthermore, our data showed the presence of other body proteins, e.g., ankyrin repeats, leucine repeats, zinc finger, cobra serum albumin, transferrin, insulin, deoxyribonuclease-2-alpha, and other regulatory proteins in these venoms. Interestingly, our data identified Ras-GTpase type of proteins, which indicate the presence of extracellular vesicles in the venom. The data can support the production of distinct and specific anti-venoms and also allow a better understanding of the envenomation and mechanism of distribution of toxins. Data are available via ProteomeXchange with identifier PXD018726.

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The application of laboratory‐based analytical tools and techniques for the quality assessment and improvement of commercial antivenoms used in the treatment of snakebite envenomation

Patra

Herrera

Gutiérrez

et al. 2021

Drug Testing and Analysis

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Snakebite envenomation is a public health problem of high impact, particularly for the developing world. Antivenom, which contains whole or protease‐digested immunoglobulin G, purified from the plasma of hyper‐immunized animals (mainly horses), is the mainstay for the treatment of snakebite envenomation. The success of antivenom therapy depends upon its ability to abrogate or reduce the local and systemic toxicity of envenomation. In addition, antivenom administration must be safe for the patients. Therefore, antivenom manufacturers must ensure that these products are effective and safe in the treatment of envenomations. Antivenom efficacy and safety are determined by the physicochemical characteristics of formulations, purity of the immunoglobulin fragments and antibodies, presence of protein aggregates, endotoxin burden, preservative load, and batch to batch variation, as well as on the ability to neutralize the most important toxins of the venoms against which the antivenom is designed. In this context, recent studies have shown that laboratory‐based simple analytical techniques, for example, size exclusion chromatography, sodium dodecyl sulphate polyacrylamide gel electrophoresis, mass spectrometry, immunological profiling including immuno‐turbidimetry and enzyme‐linked immunosorbent assays, Western blotting, immune‐chromatographic technique coupled to mass spectrometry analysis, reverse‐phase high performance liquid chromatography, spectrofluorometric analysis, in vitro neutralization of venom enzymatic activities, and other methodologies, can be applied for the assessment of antivenom quality, safety, stability, and efficacy. This article reviews the usefulness of different analytical techniques for the quality assessment of commercial antivenoms. It is suggested that these tests should be applied for screening the quality of commercial antivenoms before their preclinical and clinical assessment.

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Proteomic analysis and antivenomics study of Western IndiaNaja najavenom: correlation between venom composition and clinical manifestations of cobra bite in this region

Cited by 47 publications

References 53 publications

Evaluating the Immunological cross-reactivity of Indian polyvalent antivenoms towards the venom ofHypnale hypnale(hump-nosed pit viper) from the Western Ghats

Evaluating the Immunological cross-reactivity of Indian polyvalent antivenoms towards the venom ofHypnale hypnale(hump-nosed pit viper) from the Western Ghats

Proteomic Investigations of Two Pakistani Naja Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles

The application of laboratory‐based analytical tools and techniques for the quality assessment and improvement of commercial antivenoms used in the treatment of snakebite envenomation

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