Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086.

ABSTRACT: LP2086 is a family of outer membrane lipoproteins from Neisseria meningitidis, which elicits bactericidal antibodies and are currently undergoing human clinical trials in a bivalent formulation where each antigen represents one of the two known LP2086 subfamilies. Here we report the NMR structure of the recombinant LP2086 variant B01, a representative of the LP2086 subfamily B. The structure reveals a novel fold composed of two domains: a "taco-shaped" N-terminal beta-sheet and a C-terminal beta-barrel connected by a linker. The structure in micellar solution is consistent with a model of LP2086 anchored to the outer membrane bilayer through its lipidated N terminus. A long flexible chain connects the folded part of the protein to the lipid anchor and acts as spacer, making both domains ac

SUBMITTER: Mascioni A 

PROVIDER: S-EPMC2659232 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature