ObjectiveTo search and analyze nitric oxide synthase (NOS) and similar proteins from Plasmodium berghei(Pb).MethodsThe structure and function of nitric oxide synthase and similar proteins from Plasmodium berghei were ...ObjectiveTo search and analyze nitric oxide synthase (NOS) and similar proteins from Plasmodium berghei(Pb).MethodsThe structure and function of nitric oxide synthase and similar proteins from Plasmodium berghei were analyzed and predicted by bioinformatics.ResultsPbNOS were not available, but nicotinamide adenine dinucleotide 2′–phosphate reduced tetrasodium (NADPH)–cytochrome p450 reductase(CPR) were gained. PbCPR was in the nucleus of Plasmodium berghei, while 134aa–229aa domain was localize in nucleolar organizer. The amino acids sequence of PbCPR had the closest genetic relationship with Plasmodium vivax showing a 73% homology. The tertiary structure of PbCPR displayed the forcep–shape with wings, but no wings existed in the tertiary structure of its' host, Mus musculus(Mm). 137aa–200aa, 201aa–218aa, 220aa–230aa, 232aa–248, 269aa–323aa, 478aa–501aa and 592aa–606aa domains of PbCPR showed no homology with MmCPRs', and all domains were exposed on the surface of the protein.ConclusionsNOS can't be found in Plasmodium berghei and other Plasmodium species. PbCPR may be a possible resistance site of antimalarial drug, and the targets of antimalarial drug and vaccine. It may be also one of the mechanisms of immune evasion. This study on Plasmodium berghei may be more suitable to Plasmodium vivax. And 137aa–200aa, 201aa–218aa, 220aa–230aa, 232aa–248, 269aa–323aa, 478aa–501aa and 592aa–606aa domains of PbCPR are more ideal targets of antimalarial drug and vaccine.展开更多
基金Supported in part by the Research Program in Higher Educational Institutes of the Education Department in Hainan(No.Hjkj2009-50)Scientific Research Funds of Hainan Medical University in 2011(No.2010-014)
文摘ObjectiveTo search and analyze nitric oxide synthase (NOS) and similar proteins from Plasmodium berghei(Pb).MethodsThe structure and function of nitric oxide synthase and similar proteins from Plasmodium berghei were analyzed and predicted by bioinformatics.ResultsPbNOS were not available, but nicotinamide adenine dinucleotide 2′–phosphate reduced tetrasodium (NADPH)–cytochrome p450 reductase(CPR) were gained. PbCPR was in the nucleus of Plasmodium berghei, while 134aa–229aa domain was localize in nucleolar organizer. The amino acids sequence of PbCPR had the closest genetic relationship with Plasmodium vivax showing a 73% homology. The tertiary structure of PbCPR displayed the forcep–shape with wings, but no wings existed in the tertiary structure of its' host, Mus musculus(Mm). 137aa–200aa, 201aa–218aa, 220aa–230aa, 232aa–248, 269aa–323aa, 478aa–501aa and 592aa–606aa domains of PbCPR showed no homology with MmCPRs', and all domains were exposed on the surface of the protein.ConclusionsNOS can't be found in Plasmodium berghei and other Plasmodium species. PbCPR may be a possible resistance site of antimalarial drug, and the targets of antimalarial drug and vaccine. It may be also one of the mechanisms of immune evasion. This study on Plasmodium berghei may be more suitable to Plasmodium vivax. And 137aa–200aa, 201aa–218aa, 220aa–230aa, 232aa–248, 269aa–323aa, 478aa–501aa and 592aa–606aa domains of PbCPR are more ideal targets of antimalarial drug and vaccine.
