Abstract
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 1H, 13C and 15N resonances of free OAA.
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Acknowledgments
This work was supported by the Max Planck Society, the EU (ERC Grant agreement No. 233227 to CG), and the National Institute of Health Grant GM080642 (to AMG).
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The authors declare that they have no conflict of interest.
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Carneiro, M.G., Koharudin, L.M.I., Griesinger, C. et al. 1H, 13C and 15N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii . Biomol NMR Assign 9, 317–319 (2015). https://doi.org/10.1007/s12104-015-9600-8
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DOI: https://doi.org/10.1007/s12104-015-9600-8