Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis

Bacterial peptides are intensively present throughout the human proteome

“…myasthenia gravis, rheumatoid arthritis, insulin-dependent diabetes, ankylosing spondylitis, Guillain-Barré syndrome, autoimmune hepatitis and primary biliary cirrhosis, neurological diseases such as multiple sclerosis and other demyelinating pathologies, and even the atherosclerotic plaque. [8][9][10][11][12][13][14] In contrast, the results presented here are consistent with a number of other reports in which the elusive character of the molecular mimicry hypothesis has been underlined. [15][16][17][18][19][20][21][22][23][24][25][26][27] Our past 4,5 and present data tend to exclude a causal mechanistic role for molecular mimicry in the genesis of autoimmunity.…”

Molecular Mimicry and Primary Biliary Cirrhosis: Premises Not Promises

“…20 As mentioned previously, these cross-reactivities are not surprising, due to the structurally conserved nature of PDC-E2 among many species from eubacteria to mammals; interestingly, cross-reactivity to non-PDC-E2 bacterial counterparts has also been shown. 21 Although PDC-E2 is present in mitochondria, several bodies of evidence suggest that one component of the 2-oxo-acid dehydrogenase enzyme family, dihydrolipoyl dehydrogenase, is detectable in the membrane fraction of E. coli, 22 Neisseria meningitidis, 23 and Trypanosoma brucei. 24 It is also reported that the protein located in the membrane of N. meningitidis consists of 11 amino acid residues highly homologous with that of the lipoyl domain PDC-E2.…”

“…24 It is also reported that the protein located in the membrane of N. meningitidis consists of 11 amino acid residues highly homologous with that of the lipoyl domain PDC-E2. 23 Because it is believed that the origin of mitochondria in mammalian cells is intracellular organisms, it is not impossible that mitochondrial components, usually located in the mitochondrial inner membrane, are also detected in the membrane fraction of various organisms. Thus, the presence of these displayed proteins on the cell surface of bacteria may contribute to the breakdown of self-tolerance.…”

Metabolic Networking through Enzymatic Sensing, Signaling and Response to Homeostatic Fluctuations

“…The variations include the different architectures known for the complexes (Izard et al, 1999;De Kok et al, 1998), their different lipoate content and stoichiometries of catalytic components and different localization of the lipoate residues. Those may be incorporated not only in the established lipoate holder, the core-forming dihydrolipoyl acyltransferase component of the complexes, but also in the peripheral components (De Kok et al, 1998;De la Sierra et al, 1997). As discussed in Section 2.1.1, the catalytic selectivity of the complexes may differ between the species as well (Niebisch et al, 2006).…”