Snake C-Type Lectins Potentially Contribute to the Prey Immobilization in <i>Protobothrops mucrosquamatus</i> and <i>Trimeresurus stejnegeri</i> Venoms
Huiwen Tian,
Ming Liu,
Jiameng Li,
Runjia Xu,
Chengbo Long,
Hao Li,
James Mwangi,
Qiumin Lu,
Ren Lai,
Chuanbin Shen
Affiliations
Huiwen Tian
Life Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China
Ming Liu
Department of Molecular and Cell Biology, School of Life Sciences, University of Science and Technology of China, Anhui 230027, Hefei, China
Jiameng Li
Life Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China
Runjia Xu
Key Laboratory of Bioactive Peptides of Yunnan Province/Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China
Chengbo Long
Key Laboratory of Bioactive Peptides of Yunnan Province/Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China
Hao Li
Key Laboratory of Bioactive Peptides of Yunnan Province/Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China
James Mwangi
Key Laboratory of Bioactive Peptides of Yunnan Province/Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China
Qiumin Lu
Key Laboratory of Bioactive Peptides of Yunnan Province/Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China
Ren Lai
Life Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China
Chuanbin Shen
Key Laboratory of Bioactive Peptides of Yunnan Province/Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China
Snake venoms contain components selected to immobilize prey. The venoms from Elapidae mainly contain neurotoxins, which are critical for rapid prey paralysis, while the venoms from Viperidae and Colubridae may contain fewer neurotoxins but are likely to induce circulatory disorders. Here, we show that the venoms from Protobothrops mucrosquamatus and Trimeresurus stejnegeri are comparable to those of Naja atra in prey immobilization. Further studies indicate that snake C-type lectin-like proteins (snaclecs), which are one of the main nonenzymatic components in viper venoms, are responsible for rapid prey immobilization. Snaclecs (mucetin and stejnulxin) from the venoms of P. mucrosquamatus and T. stejnegeri induce the aggregation of both mammalian platelets and avian thrombocytes, leading to acute cerebral ischemia, and reduced animal locomotor activity and exploration in the open field test. Viper venoms in the absence of snaclecs fail to aggregate platelets and thrombocytes, and thus show an attenuated ability to cause cerebral ischemia and immobilization of their prey. This work provides novel insights into the prey immobilization mechanism of Viperidae snakes and the understanding of viper envenomation-induced cerebral infarction.
