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Abstract
Small serum proteins (SSPs) are low-molecular-weight proteins in snake serum with affinities for various venom proteins. Five SSPs, PfSSP-1 through PfSSP-5, have been reported in Protobothrops flavoviridis (“habu”, Pf) serum so far. Recently, we reported that the five genes encoding these PfSSPs are arranged in tandem on a single chromosome. However, the physiological functions and evolutionary origins of the five SSPs remain poorly understood. In a detailed analysis of the habu draft genome, we found a gene encoding a novel SSP, SSP-6. Structural analysis of the genes encoding SSPs and their genomic arrangement revealed the following: (1) SSP-6 forms a third SSP subgroup; (2) SSP-5 and SSP-6 were present in all snake genomes before the divergence of non-venomous and venomous snakes, while SSP-4 was acquired only by venomous snakes; (3) the composition of paralogous SSP genes in snake genomes seems to reflect snake habitat differences; and (4) the evolutionary emergence of SSP genes is probably related to the physiological functions of SSPs, with an initial snake repertoire of SSP-6 and SSP-5. SSP-4 and its derivative, SSP-3, as well as SSP-1 and SSP-2, appear to be venom-related and were acquired later.
Highlights
The bites of viperid snakes, including Protobothrops flavoviridis (Pf), cause a variety of symptoms, including bleeding, necrosis, edema, and neurotoxicity, and can be fatal in severe cases
We found a low-molecular-weight serum protein that binds to myotoxic [Lys49 ]PLA2 isozymes and revealed that this is a homolog of Small Serum Protein-2 (SSP-2), a human prostatic secretory protein superfamily of 94 amino acids (PSP94) [30]
Paralogs, (3) a relationship between arrays of SSP paralogs in the snake genome and environmental conditions, (4) relationships between SSP evolution and physiological functions of their products, suggesting an initial repertoire of SSP-6, SSP-5, and SSP-4, and the subsequent appearance of venom-related SSP-1, SSP-2, and SSP-3
Summary
The bites of viperid snakes, including Protobothrops flavoviridis (Pf), cause a variety of symptoms, including bleeding, necrosis, edema, and neurotoxicity, and can be fatal in severe cases. Recent transcriptomic and proteomic studies have identified multiple components of viperid venoms [1,2,3], including phospholipases A2 [4,5,6,7], metalloproteases (snake venom metalloproteases, SVMPs) [8,9,10,11], and serine proteases [12,13]. Many of these venom proteins have isoforms. From a detailed structural analysis, we propose: (1) a novel classification of SSPs, (2) an evolutionary scenario to explain SSP paralogs, (3) a relationship between arrays of SSP paralogs in the snake genome and environmental conditions, (4) relationships between SSP evolution and physiological functions of their products, suggesting an initial repertoire of SSP-6, SSP-5, and SSP-4, and the subsequent appearance of venom-related SSP-1, SSP-2, and SSP-3
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