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On the Indian subcontinent, almost all snakebite deaths have traditionally been attributed to the Big Four, consisting of the Russell's viper, Indian cobra, saw-scaled viper, and the common krait. However, studies have shown that the hump-nosed viper, previously considered essentially harmless and misidentified as the saw-scaled viper, is capable of delivering a fatal bite. In regions of Kerala, India, it may be responsible for nearly 10% of venomous bites. Commonly used antivenoms in India do not appear to be effective against hump-nosed viper bites.[26][27] According to the most conservative estimates, at least 81,000 snake envenomings and 11,000 fatalities occur in India each year, making it the most heavily affected country in the world.[1] The Malayan pit viper and banded krait are two other species involved in a significant number of venomous bites.
Reports of large man-eating pythons are common in Southeast Asia, although the threat is typically exaggerated. However, in the Philippines, more than a quarter of Aeta men (a modern forest-dwelling hunter-gatherer group) have reported surviving a reticulated python attack. Pythons are nonvenomous ambush predators, and both the Aeta and pythons hunt deer, wild pigs, and monkeys, making them competitors and prey.

Throughout Western Asia, the species responsible for the majority of bites tend to be more venomous than European snakes, but deaths are infrequent. Studies estimate that perhaps 100 fatal bites occur each year. The Palestine viper and Lebetine viper are the most important species. While larger and more venomous elapids, such as the Egyptian cobra, are also found throughout the Middle East, these species inflict fewer bites.
दोस्तों स्नेक रेस्क्यू टीम में हम 3 सदस्य है अमित मिश्रा अक्षय मिश्रा मनोज कुमार ।
अगर आप यह संदेश पढ़ रहे है तो आपको यूट्यूब के माध्यम से पता चला ही होगा कि हमारी टीम निःशुल्क 24 घण्टे सेवा के ये तत्पर रहती है।
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Snake venom is a blend of bioactive compounds that interferes in various physiological systems and can lead to debilitation of the victim or death. Among a variety of enzymes encountered in snake venoms, metalloproteinases are considered to represent the key toxins in venom-induced pathogenesis . These enzymes are synthesized as precursors in the cytoplasm of secretory cells and undergo proteolytic processing during the release of mature secretory vesicle contents into the venom gland lumen .

Snake venom metalloproteinases (SVMPs) range from 20 to 100 kDa and have been grouped into 4 classes taking into account their primary structure and domain organization: P-I class encompasses the enzymes that only contain a zinc-dependent catalytic domain; P-II class members contain a disintegrin domain in addition to the catalytic domain; P-III class includes the P-II enzyme and the cysteine-rich domain; and P-IV class has an additional lectin-like domain linked by disulfide bonds to a P-III SVMP . A novel classification has been proposed based on the ability of P-II and P-III SVMPs to form dimers and they are considered to belong to the P-I, P-IIa and P-IIb, P-IIIa and PIIIb, and P-IV classes

Most SVMPs display hemorrhagic activity due to their proteolytic action on all major proteins of the extracellular matrix (ECM) , and there exists a positive correlation between the proteolytic activity and their hemorrhagic potencies. Typically, SVMPs belonging to class IV are more potent than other classes.

Despite the fact that P-I class SVMPs contain only the catalytic domain, these toxins display a wide variety of physiological effects; many interfere either directly or indirectly with the proper functioning of the hemostatic system.

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