Division of Hematology, Department of Medicine, Faculty of Medicine, Chulalongkorn University, Bangkok 10330, Thailand.
Toxicon. 2011 Apr;57(5):772-80. doi: 10.1016/j.toxicon.2011.02.011. Epub 2011 Feb 17.
Molecular cloning and functional characterization of P-III snake venom metalloproteinases (SVMPs) will give us deeper insights in the pathogenesis of viper bites. This may lead to novel therapy for venom-induced local tissue damages, the complication refractory to current antivenom. The aim of this study was to elucidate the in vitro activities of a new SVMP from the green pit viper (GPV) using recombinant DNA technology. We report, here, a new cDNA clone from GPV (Cryptelytrops albolabris) venom glands encoding 614 amino acid residues P-III SVMP, termed albocollagenase. The conceptually translated protein comprised a signal peptide and prodomain, followed by a metalloproteinase domain containing a zinc-binding motifs, HEXGHXXGXXH-CIM and 9 cysteine residues. The disintegrin-like and cysteine-rich domains possessed 24 cysteines and a DCD (Asp-Cys-Asp) motif. The albocollagenase deduced amino acid sequence alignments showed approximately 70% identity with other P-III SVMPs. Notably, the prodomain was highly conserved, while the metalloproteinase, disintegrin-like and cysteine-rich domains contained several differences. Albocollagenase without the signal peptide and prodomain was expressed in Pichia pastoris with an N-terminal six-histidine tag. After affinity purification from the supernatant of methanol-induced media, SDS-PAGE and Western blot analysis in both reducing and non-reducing conditions showed a protein band of approximately 62 kDa. The recombinant albocollagenase could digest human type IV collagen from human placenta basement membrane within 1 min. After 10-min incubation, it also inhibited collagen-induced platelet aggregation with 50% inhibitory concentration (IC₅₀) of 70 nM. This is the first report of the active recombinant SVMP enzymes expressed in P. pastoris. The results suggest the significant roles of P-III SVMP in local and systemic pathology of envenomated patients. Inhibitors of this SVMP will be investigated in further studies to find a better treatment for viper bites.
分子克隆和功能表征 P-III 型蛇毒金属蛋白酶(SVMPs)将使我们更深入地了解毒蛇咬伤的发病机制。这可能为毒液引起的局部组织损伤提供新的治疗方法,目前的抗蛇毒血清对此类并发症无效。本研究的目的是利用重组 DNA 技术阐明来自绿林蝰蛇(GPV)的新型 SVMP 的体外活性。我们在此报告,从 GPV(Cryptelytrops albolabris)毒液腺中克隆得到一种新的 cDNA 克隆,编码 614 个氨基酸残基的 P-III SVMP,命名为 albocollagenase。该概念翻译的蛋白包含一个信号肽和前导肽,其后是一个金属蛋白酶结构域,含有锌结合基序 HEXGHXXGXXH-CIM 和 9 个半胱氨酸残基。解整合素样和富含半胱氨酸结构域含有 24 个半胱氨酸和一个 DCD(天冬氨酸-半胱氨酸-天冬氨酸)基序。albocollagenase 的推导氨基酸序列比对显示与其他 P-III SVMP 约有 70%的同一性。值得注意的是,前导肽高度保守,而金属蛋白酶、解整合素样和富含半胱氨酸结构域含有几个差异。没有信号肽和前导肽的 albocollagenase 在巴斯德毕赤酵母中表达,带有 N 端的六个组氨酸标签。在甲醇诱导的培养基上清液中经亲和纯化后,SDS-PAGE 和 Western blot 分析在还原和非还原条件下均显示约 62 kDa 的蛋白条带。重组 albocollagenase 可在 1 分钟内消化人胎盘基底膜的人 IV 型胶原。孵育 10 分钟后,它还能抑制胶原蛋白诱导的血小板聚集,其 50%抑制浓度(IC₅₀)为 70 nM。这是首次报道在巴斯德毕赤酵母中表达的活性重组 SVMP 酶。结果表明 P-III SVMP 在毒蛇咬伤患者的局部和全身病理中起重要作用。将进一步研究这种 SVMP 的抑制剂,以寻找更好的毒蛇咬伤治疗方法。