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- W1980292889 abstract "Opa (opacity associated) proteins from Neisseria gonorrhoeae (NG) and Neisseria meningitides (NM) induce phagocytosis of the bacterium by non-phagocytic cells such as epithelial cells. There are eleven NG and four NM Opa alleles that undergo phase-variation expression to the outer membrane. The protein products are nearly identical in sequence, but vary in three extracellular loop regions that determine the host receptor specificity. Opa proteins bind to carcinoembryonic antigen-like cellular adhesion molecules (CEACAMs) or to heparansulfate proteoglycan receptors (HSPGs), thus subdividing Opa proteins into two classes, OpaCEA and OpaHS, respectively. Mutational and chimeric experiments have not revealed the sequence determinants of the hypervariable regions that are responsible for receptor recognition. The goal of this study is to investigate the structure, dynamics, and receptor interactions of OpaI, a 27 kDa, 238 amino acid OpaCEA from NG MS11. OpaI was over-expressed in E. coli, purified, and refolded in dodecylphosphocholine. Two-dimensional 15N, 1H- TROSY spectra, CD, and SDS-PAGE gel mobility of the protein-detergent complex indicate that the protein is folded and well-suited for NMR studies Using TROSY-based pulse sequences, methyl labeling, and specific amino acid labeling, a suitable backbone assignment was achieved and an initial low-resolution structural calculation with H-bond and NOE-derived restraints is presented." @default.
- W1980292889 created "2016-06-24" @default.
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- W1980292889 date "2011-02-01" @default.
- W1980292889 modified "2023-10-18" @default.
- W1980292889 title "NMR Backbone Assignment of Opai: A Mediator of Host:Neisseria Interactions" @default.
- W1980292889 doi "https://doi.org/10.1016/j.bpj.2010.12.2290" @default.
- W1980292889 hasPublicationYear "2011" @default.
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