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Backbone and side-chain assignment of the lipidated and non-lipidated forms of the meningococcal outer membrane protein LP2086 |
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| Authors: | 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 |
| Institution: | (1) Wyeth Research, Structural Biology and Computational Chemistry, 200 Cambridge Park Drive, 02140 Cambridge, MA, USA;(2) Wyeth Vaccines Research, 401 North Middletown Road, 10965 Pearl River, NY, USA |
| 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. Ethical standards All experiments described comply with the current laws of the United States of America. The authors declare that they have no conflict of interest |
| Keywords: | LP2086 Outer membrane lipoprotein Neisseria meningitidis |
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