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

@article{Mascioni2009StructuralBF,
  title={Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086.},
  author={Alessandro Mascioni and Breagh E Bentley and Rosaria Camarda and Deborah A. Dilts and Pamela S. Fink and Viktoria Gusarova and Susan K Hoiseth and Jaison Jacob and Shuo Liang Lin and Karl Malakian and Lisa K Mcneil and Terri L Mininni and Franklin J. Moy and Ellen Murphy and Elena Novikova and Scott D Sigethy and Yingxia Wen and Gary W Zlotnick and D{\'e}sir{\'e}e H H Tsao},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 13},
  pages={8738-46}
}
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… CONTINUE READING

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