School of Chemistry and Molecular Biosciences and Australian Infectious Diseases Research Centre, The University of Queensland, St. Lucia, Queensland, Australia.
Center for Microbial Pathogenesis, The Abigail Wexner Research Institute at Nationwide Children's Hospital, Columbus, Ohio, USA.
J Infect Dis. 2020 Jan 14;221(3):449-453. doi: 10.1093/infdis/jiz468.
L-lactate is an abundant metabolite in a number of niches in host organisms and represents an important carbon source for bacterial pathogens such as Neisseria gonorrhoeae. In this study, we describe an alternative, iron-sulfur cluster-containing L-lactate dehydrogenase (LutACB), that is distinct from the flavoprotein L-lactate dehydrogenase (LldD). Expression of lutACB was found to be positively regulated by iron, whereas lldD was more highly expressed under conditions of iron-limitation. The functional role of LutACB and LldD was reflected in in vitro studies of growth and in the survival of N gonorrhoeae in primary cervical epithelial cells.
L-乳酸是宿主生物中许多生态位中丰富的代谢物，是淋病奈瑟菌等细菌病原体的重要碳源。在这项研究中，我们描述了一种替代的、含有铁硫簇的 L-乳酸脱氢酶 (LutACB)，它与黄素蛋白 L-乳酸脱氢酶 (LldD) 不同。发现 lutACB 的表达受铁的正向调节，而 lldD 在缺铁条件下表达更高。LutACB 和 LldD 的功能作用反映在淋病奈瑟菌体外生长和在原代宫颈上皮细胞中存活的研究中。
