Suppr超能文献

伯氏疟原虫甘氨酸裂解系统T蛋白对于寄生虫在脊椎动物和无脊椎动物宿主中的存活并非必需。

Plasmodium berghei glycine cleavage system T-protein is non-essential for parasite survival in vertebrate and invertebrate hosts.

作者信息

Varadarajan Nandan Mysore, Sundaram Balamurugan, Subramani Pradeep Annamalai, Kalappa Devaiah Monnanda, Ghosh Susanta Kumar, Nagaraj Viswanathan Arun

机构信息

Department of Biochemistry, Indian Institute of Science, Bangalore 560 012, India.

National Institute of Malaria Research (Field Unit), Nirmal Bhawan, ICMR Complex, Poojanahalli, Off NH-7, Kannamangala Post, Bangalore 562 110, India.

出版信息

Mol Biochem Parasitol. 2014 Oct;197(1-2):50-5. doi: 10.1016/j.molbiopara.2014.10.003. Epub 2014 Oct 24.

Abstract

T-protein, an aminomethyltransferase, represents one of the four components of glycine cleavage system (GCS) and catalyzes the transfer of methylene group from H-protein intermediate to tetrahydrofolate (THF) forming N(5), N(10)-methylene THF (CH2-THF) with the release of ammonia. The malaria parasite genome encodes T-, H- and L-proteins, but not P-protein which is a glycine decarboxylase generating the aminomethylene group. A putative GCS has been considered to be functional in the parasite mitochondrion despite the absence of a detectable P-protein homologue. In the present study, the mitochondrial localization of T-protein in the malaria parasite was confirmed by immunofluorescence and its essentiality in the entire parasite life cycle was studied by targeting the T-protein locus in Plasmodium berghei (Pb). PbT knock out parasites did not show any growth defect in asexual, sexual and liver stages indicating that the T-protein is dispensable for parasite survival in vertebrate and invertebrate hosts. The absence of P-protein homologue and the non-essentiality of T protein suggest the possible redundancy of GCS activity in the malaria parasite. Nevertheless, the H- and L-proteins of GCS could be essential for malaria parasite because of their involvement in α-ketoacid dehydrogenase reactions.

摘要

T蛋白是一种氨基甲基转移酶,是甘氨酸裂解系统(GCS)的四个组成部分之一,催化亚甲基从H蛋白中间体转移至四氢叶酸(THF),形成N(5), N(10)-亚甲基四氢叶酸(CH2-THF)并释放氨。疟原虫基因组编码T蛋白、H蛋白和L蛋白,但不编码作为产生氨基亚甲基基团的甘氨酸脱羧酶的P蛋白。尽管没有可检测到的P蛋白同源物,但推测GCS在寄生虫线粒体中具有功能。在本研究中,通过免疫荧光证实了疟原虫中T蛋白的线粒体定位,并通过靶向伯氏疟原虫(Pb)中的T蛋白基因座研究了其在整个寄生虫生命周期中的必要性。敲除PbT的寄生虫在无性、有性和肝脏阶段均未表现出任何生长缺陷,这表明T蛋白对于疟原虫在脊椎动物和无脊椎动物宿主中的存活并非必需。P蛋白同源物的缺失以及T蛋白的非必要性表明疟原虫中GCS活性可能存在冗余。然而,GCS的H蛋白和L蛋白可能对疟原虫至关重要,因为它们参与α-酮酸脱氢酶反应。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验