(1)H, (13)C and (15)N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii

Marta G Carneiro; Leonardus M I Koharudin; Christian Griesinger; Angela M Gronenborn; Donghan Lee

doi:10.1007/s12104-015-9600-8

(1)H, (13)C and (15)N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii

Biomol NMR Assign. 2015 Oct;9(2):317-9. doi: 10.1007/s12104-015-9600-8. Epub 2015 Feb 14.

Authors

Marta G Carneiro¹, Leonardus M I Koharudin², Christian Griesinger¹, Angela M Gronenborn², Donghan Lee³

Affiliations

¹ Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
² Department of Structural Biology, University of Pittsburgh School of Medicine, 1050 Biomedical Science Tower 3, 3501 5th Ave, Pittsburgh, PA, 15260, USA.
³ Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany. dole@nmr.mpibpc.mpg.de.

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 (1)H, (13)C and (15)N resonances of free OAA.

Keywords: Anti-HIV lectins; NMR assignment; Oscillatoria agardhii agglutinin.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Carbon-13 Magnetic Resonance Spectroscopy*
Lectins / chemistry*
Nitrogen Isotopes
Oscillatoria / chemistry*
Protein Structure, Secondary
Proton Magnetic Resonance Spectroscopy*

Substances

Lectins
Nitrogen Isotopes

Abstract

Publication types

MeSH terms

Substances

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