Backbone and side-chain assignment of the lipidated and non-lipidated forms of the meningococcal outer membrane protein LP2086

A Mascioni; J Jacob; F Moy; D Dilts; P Fink; K Malakian; S Sigethy; Y Wen; E Novikova; G W Zlotnick; D H H Tsao

doi:10.1007/s12104-009-9153-9

Backbone and side-chain assignment of the lipidated and non-lipidated forms of the meningococcal outer membrane protein LP2086

Biomol NMR Assign. 2009 Jun;3(1):111-3. doi: 10.1007/s12104-009-9153-9. Epub 2009 Mar 5.

Authors

A Mascioni¹, J Jacob, F Moy, D Dilts, P Fink, K Malakian, S Sigethy, Y Wen, E Novikova, G W Zlotnick, D H H Tsao

Affiliation

¹ Wyeth Research, Structural Biology and Computational Chemistry, 200 Cambridge Park Drive, 02140, Cambridge, MA, USA. [email protected]

PMID: 19636959
DOI: 10.1007/s12104-009-9153-9

Abstract

LP2086 is a lipidated outer membrane protein from Neisseria meningitidis that elicits bactericidal antibodies and represents a promising vaccine candidate against meningococcal infections. Here we report the backbone and side-chain assignment for two forms of LP2086: non-lipidated in aqueous buffer and the lipidated protein in micellar solution.

MeSH terms

Amino Acid Sequence
Antigens, Bacterial / chemistry*
Bacterial Proteins / chemistry*
Carbon Isotopes / chemistry
Magnetic Resonance Spectroscopy / methods*
Membrane Lipids / chemistry*
Micelles
Molecular Sequence Data
Nitrogen Isotopes / chemistry
Protein Structure, Tertiary
Protein Subunits
Protons

Substances

Antigens, Bacterial
Bacterial Proteins
Carbon Isotopes
Membrane Lipids
Micelles
Nitrogen Isotopes
Protein Subunits
Protons
factor H-binding protein, Neisseria meningitidis