Meningococcus adhesins nada, app and orf 40
a technology of meningococcus and adhesins, applied in the field of biochemistry, can solve the problems that do not reveal everything about this pathogen, and achieve the effect of preventing the attachment of a neisserial cell
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NadA Homology
[0195]NadA shows homology to (a) YadA of enteropathogenic Yersinia, a non-pilus associated adhesin implicated in virulence [Cornelis (1998) Microbiol. Mol. Biol. Rev. 62:1315-1352.] and (b) UspA2 of Moraxella catarrhalis, a protein involved in serum resistance and a protective antigen [Chen et al. (1999) Infect. Immun. 67:1310-1316.]. Sequence similarity is mainly clustered in the carboxyl terminal region (56-63% identity in the last 70 amino acids). Outside this region the level of identity drops to 23-25%.
[0196]YadA and UspA2 have been identified as adhesins [Hoiczyk et al. (2000) EMBO J 19:5989-5999]. Both proteins form very stable and difficult-to-dissociate high molecular weight oligomers (150-200 kDa) anchored to the outer membrane. NadA has also been found to form very stable high molecular weight aggregates on the outer membrane of meningococcus.
[0197]The amino acid sequence of NadA was analysed [Nielsen et al. (1997) Protein Engineering 10:1-6; Levin & Garner (...
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