Carneiro Marta G, Koharudin Leonardus M I, Griesinger Christian, Gronenborn Angela M, Lee Donghan
Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Department of Structural Biology, University of Pittsburgh School of Medicine, 1050 Biomedical Science Tower 3, 3501 5th Ave, Pittsburgh, PA, 15260, USA.
Biomol NMR Assign. 2015 Oct;9(2):317-9. doi: 10.1007/s12104-015-9600-8. Epub 2015 Feb 14.
Lectins from different sources are known to interfere with HIV infection. The anti-viral activity is mediated by binding to high mannose sugars present on the viral envelope, thereby inhibiting cell entry. The lectin from Oscillatoria agardhii agglutinin (OAA) specifically recognizes a unique substructure of high mannose sugars and exhibits broad anti-HIV activity. Here we report the assignment of backbone and side-chain (1)H, (13)C and (15)N resonances of free OAA.
已知来自不同来源的凝集素会干扰HIV感染。抗病毒活性是通过与病毒包膜上存在的高甘露糖糖结合来介导的,从而抑制细胞进入。来自颤藻凝集素(OAA)的凝集素特异性识别高甘露糖糖的独特亚结构,并表现出广泛的抗HIV活性。在此,我们报告了游离OAA的主链和侧链氢、碳-13和氮-15共振的归属。