2009
DOI: 10.2174/092986609788923293
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Venom-Sweet-Venom: N-Linked Glycosylation in Snake Venom Toxins

Abstract: Protein glycosylation represents one of the most important post-translational events, and is a mean of diversifying a protein without recourse to the genome. The venoms produced by snakes contain an abundance of glycoproteins with N-linked carbohydrates. N-linked glycosylation can ensure the correct folding of important functional domains. Characterization of carbohydrates structures aids in development of human therapeutics by snake venom toxins.

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Cited by 25 publications
(16 citation statements)
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“…Thus, accumulating evidence indicates that the glycan moieties in snake venom proteins appear to be formed by a common mammalian N-glycan core with biologically important carbohydrate terminals [24]. Since carbohydrate modification can easily enhance venom complexity without changing the genome and glycans are known to have a direct impact on immunogenicity and antibody recognition [22,27], the presence of complex glycans on geographic samples is equally worthy of investigation to understand snake venom biodiversity [28]. To the best of our knowledge, there is no report on the individual snake venom glycome.…”
Section: Introductionmentioning
confidence: 99%
“…Thus, accumulating evidence indicates that the glycan moieties in snake venom proteins appear to be formed by a common mammalian N-glycan core with biologically important carbohydrate terminals [24]. Since carbohydrate modification can easily enhance venom complexity without changing the genome and glycans are known to have a direct impact on immunogenicity and antibody recognition [22,27], the presence of complex glycans on geographic samples is equally worthy of investigation to understand snake venom biodiversity [28]. To the best of our knowledge, there is no report on the individual snake venom glycome.…”
Section: Introductionmentioning
confidence: 99%
“…D-amino acids are also present in toxins [19]. Phosphorylation of animal toxins has not been described in the literature so far, in contrast to glycosylation for which few articles were published [20]. Regarding only snake venoms, several high mass enzymes have been found to be glycosylated.…”
Section: Introductionmentioning
confidence: 99%
“…Regarding only snake venoms, several high mass enzymes have been found to be glycosylated. For example, L-amino acid oxidase from the venom of Malayan pit viper Calloselasma rhodostoma is remarkably homogeneously N-glycosylated at Asn172 and Asn361 [20,21]. Many of these glycosylated snake toxins belong to serine protease group.…”
Section: Introductionmentioning
confidence: 99%
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“…An abundance of glycoproteins with N-linked carbohydrates are contained in snake venoms. N-Linked glycosylation can ensure the correct folding of important functional domains and has considerable influence on the biological and toxicological functions of active proteins [1][2][3] . In recent years, an increasing number of proteomics studies have been carried out to explore the protein composition of snake venoms.…”
Section: Introductionmentioning
confidence: 99%