中文摘要：

CVN（Cyanovirin-N）是一种高效的抗HIV蛋白. Cyanovirin-N（CVNH）家族是CVN的同源蛋白,具有与CVN的肽链折叠类型并且具有高度保守的抗HIV 的结构域.把水蕨Ceratopteris thalictroides野生型和突变型CtCVNH蛋白的编码序列分别克隆到真核表达载体pPICZαA,结果所有野生型wCtCVNH和突变型mCtCVNH基因分别产生两条带,Western blot确认大小分别为22 000和24 000.采用超滤离心和Ni-NTA亲和色谱法纯化蛋白质,糖基化检测证实wCtCVNH蛋白不存在N-糖基化位点,可能的原因是载体pPICZαA中α因子信号肽序列的不完全切割或存在一些非糖基化的其它翻译后修饰,为今后进一步研究CtCVNH的药代动力学和药效学奠定了坚实的基础.

英文摘要：

CVN （Cyanovirin-N） is a highly potent anti-HIV protein.Cyanovirin-N homology （CVNH） family is a homologous protein to CVN,which exhibits a common fold structure similar to CVN and possess a highly conserved anti-HIV CVN domain.In this study,DNA encoding sequences of the wild-type and mutant CtCVNH from Ceratopteris thalictroides were separately cloned into eukaryotic expression vector pPICZαA.All wCtCVNH and mutated mCtCVNH genes produced two bands corresponding to 22 000 and 24 000,which were validated by western blot.The proteins were purified by ultra-filtered centrifugation and Ni-NTA affinity chromatograph.Glycosylation assay further confirmed that no N-glycosylation site occurred in wCtCVNH protein.The possible reasons were ascribed to incomplete cleavage of the α-factor signal peptide sequence in vector pPICZαA or some other post-translational modifications rather than N-glycosylation.The study laid a solid foundation for further exploring the pharmacokinetics and pharmacodynamics of CtCVNH in future.