1ys5
From Proteopedia
Solution structure of the antigenic domain of GNA1870 of Neisseria meningitidis
Structural highlights
FunctionFHBP_NEIMB A bacterial surface lipoprotein that binds host (human) complement factor H (fH, gene CFH), binding contributes to the avoidance of complement-mediated lysis by N.meningitidis. Binding of fH to the bacteria surface is independent of bacterial sialic acid moieties (PubMed:16751403). fH binding affinity is high enough that it may sequester plasma fH, depleting its circulating levels and de-regulating complement in the host (Probable). This protein induces high levels of bactericidal antibodies in mice (PubMed:12642606, PubMed:15039331, PubMed:15664958, PubMed:21753121, PubMed:23133374).[1] [2] [3] [4] [5] [6] [7] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGNA1870, a 28-kDa surface-exposed lipoprotein of Neisseria meningitidis recently discovered by reverse vaccinology, is one of the most potent antigens of Meningococcus and a promising candidate for a universal vaccine against a devastating disease. Previous studies of epitope mapping and genetic characterization identified residues critical for bactericidal response within the C-terminal domain of the molecule. To elucidate the conformation of protective epitopes, we used NMR spectroscopy to obtain the solution structure of the immunodominant 18-kDa C-terminal portion of GNA1870. The structure consists of an eight-stranded antiparallel beta-barrel overlaid by a short alpha-helix with an unstructured N-terminal end. Residues previously shown to be important for antibody recognition were mapped on loops facing the same ridge of the molecule. The sequence similarity of GNA1870 with members of the bacterial transferrin receptor family allows one to predict the folding of this class of well known bacterial antigens, providing the basis for the rational engineering of high affinity B cell epitopes. Solution structure of the immunodominant domain of protective antigen GNA1870 of Neisseria meningitidis.,Cantini F, Savino S, Scarselli M, Masignani V, Pizza M, Romagnoli G, Swennen E, Veggi D, Banci L, Rappuoli R J Biol Chem. 2006 Mar 17;281(11):7220-7. Epub 2005 Dec 31. PMID:16407174[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found References
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Categories: Large Structures | Neisseria meningitidis | Banci L | Cantini F | Masignani V | Pizza M | Rappuoli R | Romagnoli G | Savino S | Scarselli M | Swennen E | Veggi D