Center of Advanced Study in Crystallography & Biophysics, University of Madras, Chennai 600025, India.
Department of Chemistry and Chemical Biology, Indiana University Purdue University, Indianapolis, IN 46202, USA.
Molecules. 2022 Feb 9;27(4):1167. doi: 10.3390/molecules27041167.
A 24 kDa leucine-rich protein from ion exchange fractions of , which has anti-bacterial activity against both the Gram-negative and Gram-positive bacteria has been purified. In this study, mass spectrometry analysis identified the leucine richness and found a luminal binding protein (LBP). Circular dichroism suggests that the protein was predominantly composed of α- helical contents of its secondary structure. Scanning electron microscopy visualized the characteristics and morphological and structural changes in LBP-treated bacterium. Further in vitro studies confirmed that mannose-, trehalose- and raffinose-treated LBP completely inhibited the hemagglutination ability towards rat red blood cells. Altogether, these studies suggest that LBP could bind to sugar moieties which are abundantly distributed on bacterial surface which are essential for maintaining the structural integrity of bacteria. Considering that is a well-known medicinal and edible plant, in order to shed light on its ancient usage in this work, an efficient anti-microbial protein was isolated, characterized and its in vitro functional study against human pathogenic bacteria was evaluated.
已从离子交换部分纯化出一种 24 kDa 的亮氨酸丰富蛋白，该蛋白对革兰氏阴性菌和革兰氏阳性菌均具有抗菌活性。在这项研究中，质谱分析鉴定了亮氨酸的丰富度，并发现了一种腔结合蛋白（LBP）。圆二色性表明该蛋白主要由其二级结构的α-螺旋组成。扫描电子显微镜观察到 LBP 处理细菌的特征和形态结构变化。进一步的体外研究证实，经甘露糖、海藻糖和棉子糖处理的 LBP 完全抑制了对大鼠红细胞的血凝能力。总的来说，这些研究表明 LBP 可以与大量分布在细菌表面的糖基结合，这些糖基对维持细菌的结构完整性至关重要。考虑到 是一种众所周知的药用和食用植物，为了阐明其在这项工作中的古老用途，我们分离、鉴定了一种有效的抗菌蛋白，并对其针对人类致病菌的体外功能进行了评估。
