Isolation and characterization of functional Leishmania major virulence factor UDP-galactopyranose mutase.
Isolation and characterization of functional Leishmania major virulence factor UDP-galactopyranose mutase.
复制标题
功能性利什曼原虫主要毒力因子 UDP-吡喃半乳糖变位酶的分离和表征。
DOI：
10.1016/j.bbrc.2011.03.057
复制
发表时间：
2011
影响因子：
3.1
通讯作者：
Sobrado,Pablo
中科院分区：
文献类型：
--
作者：
Oppenheimer,Michelle;Valenciano,AnaL;Sobrado,Pablo
利什曼原虫属的人类寄生虫病原体是皮肤、粘膜和内脏利什曼病的病原体。目前，有数百万人感染这些疾病，每年有5万多人死亡。最近，有研究表明黄素依赖性酶udp -半乳糖氨基糖突变酶（UGM）是利什曼原虫的一个毒力因子。UGM催化udp -半乳糖葡萄糖转化为udp -半乳糖呋喃糖。该产物udp -半乳糖呋喃糖是存在于该寄生虫细胞表面的半乳糖呋喃糖的唯一来源，并被认为对宿主-寄生虫相互作用很重要。该酶的重组形式以可溶性和活性形式获得。这种酶被证明只有在还原的状态下才有活性。以udp -半乳糖呋喃糖为底物，kcato值为5±0.2s−1，kcato值为87±11μM。与二聚体细菌和四聚体真菌的UGMs不同，这种寄生酶作为单体发挥作用。
Human parasitic pathogens of the genus Leishmania are the causative agents of cutaneous, mucocutaneous, and visceral leishmaniasis. Currently, there are millions of people infected with these diseases and over 50,000 deaths occur annually. Recently, it was shown that the flavin-dependent enzyme UDP-galactopyranose mutase (UGM) is a virulence factor in Leishmania major. UGM catalyzes the conversion of UDP-galactopyranose to UDP-galactofuranose. The product, UDP-galactofuranose, is the only source of galactofuranose which is present on the cell surface of this parasite and has been implicated to be important for host-parasite interactions. The recombinant form of this enzyme was obtained in a soluble and active form. The enzyme was shown to be active only in the reduced sate. A kcatvalue of 5±0.2s−1and a KMvalue of 87±11μM were determined with UDP-galactofuranose as substrate. Different from the dimeric bacterial and tetrameric fungal UGMs, this parasitic enzyme functions as a monomer.