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Review
. 2022 Oct 22;14(11):723.
doi: 10.3390/toxins14110723.

A Review of the Proteomic Profiling of African Viperidae and Elapidae Snake Venoms and Their Antivenom Neutralisation

Affiliations
Review

A Review of the Proteomic Profiling of African Viperidae and Elapidae Snake Venoms and Their Antivenom Neutralisation

Benedict C Offor et al. Toxins (Basel). .

Abstract

Snakebite envenoming is a neglected tropical disease (NTD) that results from the injection of snake venom of a venomous snake into animals and humans. In Africa (mainly in sub-Saharan Africa), over 100,000 envenomings and over 10,000 deaths per annum from snakebite have been reported. Difficulties in snakebite prevention and antivenom treatment are believed to result from a lack of epidemiological data and underestimated figures on snakebite envenoming-related morbidity and mortality. There are species- and genus-specific variations associated with snake venoms in Africa and across the globe. These variations contribute massively to diverse differences in venom toxicity and pathogenicity that can undermine the efficacy of adopted antivenom therapies used in the treatment of snakebite envenoming. There is a need to profile all snake venom proteins of medically important venomous snakes endemic to Africa. This is anticipated to help in the development of safer and more effective antivenoms for the treatment of snakebite envenoming within the continent. In this review, the proteomes of 34 snake venoms from the most medically important snakes in Africa, namely the Viperidae and Elipdae, were extracted from the literature. The toxin families were grouped into dominant, secondary, minor, and others based on the abundance of the protein families in the venom proteomes. The Viperidae venom proteome was dominated by snake venom metalloproteinases (SVMPs-41%), snake venom serine proteases (SVSPs-16%), and phospholipase A2 (PLA2-17%) protein families, while three-finger toxins (3FTxs-66%) and PLA2s (16%) dominated those of the Elapidae. We further review the neutralisation of these snake venoms by selected antivenoms widely used within the African continent. The profiling of African snake venom proteomes will aid in the development of effective antivenom against snakebite envenoming and, additionally, could possibly reveal therapeutic applications of snake venom proteins.

Keywords: antivenom; elapids; proteomics; snake venom; toxins; venomics; viperids.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Snake venom bottom-up proteomics workflow through decomplexation strategy. Venom is collected through milking, lyophilised and the protein fractions are separated by chromatography and SDS-PAGE. The fractions are digested and analysed by LC-MS/MS, followed by protein identification. The venom proteome information is useful in the production of vaccines and other therapeutics. The decomplexation strategy was adapted from Tan et al. [72,80].
Figure 2
Figure 2
The proportion of the major families of the Viperidae (A) and Elapidae (B) snake venom protein components. Protein abundance values were averaged from the number of snake species studied. Abbreviations: PLA2 = phospholipase A2; SVMP = snake venom metalloproteinase; SVSP = snake venom serine protease; CTL = C-type lectin; DIS = disintegrin; LAAO = L-amino acid oxidase; KUN = Kunitz-type peptides; CRISP = cysteine-rich secretary protein; VEGF = vascular endothelial growth factor; CYS = cystatin; 3FTxs = three-finger toxins; CVF = cobra venom factor; PDE = endonucleases/phosphodiesterases.
Figure 3
Figure 3
Production of antivenom. Animals are hyper-immunised with snake venoms, and the plasma is fractionated and purified to generate antivenoms in the form of intact immunoglobulin (IgG) or immunoglobulin fragments (Fab or F(ab)2). There are quality control steps in the antivenom production pipeline to ensure that it is of high quality and safe before usage (adapted from WHO, [100]).

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