Sequence Diversity, Predicted Two-Dimensional Protein Structure, and Epitope Mapping of Neisserial Opa Proteins Export

@article{citeulike:3938792, abstract = {The sequence diversity of 45 Opa outer membrane proteins from Neisseria meningitidis, Neisseria gonorrhoeae, Neisseria sicca, and Neisseria flava indicates that horizontal genetic exchange of opa alleles has been rare between these species. A two-dimensional structural model containing four surface-exposed loops was constructed based on rules derived from porin crystal structure and on conservation of sequence homology within transmembrane [beta]-strands. The minimal continuous epitopes recognized by 23 monoclonal antibodies were mapped to loops 2 and 3. Some of these epitopes are localized on the bacterial cell surface, in support of the model.}, author = {Malorny, Burkhard and Morelli, Giovanna and Kusecek, Barica and Kolberg, Jan and Achtman, Mark}, citeulike-article-id = {3938792}, citeulike-linkout-0 = {http://jb.asm.org/cgi/content/abstract/180/5/1323?ijkey=3305f0d8f84d1a830523b6ca62ec87df844516ad}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/9495774}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=9495774}, day = {1}, journal = {J. Bacteriol.}, keywords = {dimer, membrane, opa, protein, secondary, structure}, month = {March}, number = {5}, pages = {1323--1330}, posted-at = {2009-01-25 18:26:44}, priority = {2}, title = {Sequence Diversity, Predicted Two-Dimensional Protein Structure, and Epitope Mapping of Neisserial Opa Proteins}, url = {http://jb.asm.org/cgi/content/abstract/180/5/1323?ijkey=3305f0d8f84d1a830523b6ca62ec87df844516ad}, volume = {180}, year = {1998} }

TY - JOUR ID - citeulike:3938792 L3 - citeulike-article-id:3938792 N2 - The sequence diversity of 45 Opa outer membrane proteins from Neisseria meningitidis, Neisseria gonorrhoeae, Neisseria sicca, and Neisseria flava indicates that horizontal genetic exchange of opa alleles has been rare between these species. A two-dimensional structural model containing four surface-exposed loops was constructed based on rules derived from porin crystal structure and on conservation of sequence homology within transmembrane [beta]-strands. The minimal continuous epitopes recognized by 23 monoclonal antibodies were mapped to loops 2 and 3. Some of these epitopes are localized on the bacterial cell surface, in support of the model. IS - 5 JF - J. Bacteriol. EP - 1330 TI - Sequence Diversity, Predicted Two-Dimensional Protein Structure, and Epitope Mapping of Neisserial Opa Proteins VL - 180 SP - 1323 KW - dimer KW - membrane KW - opa KW - protein KW - secondary KW - structure AU - Malorny, Burkhard AU - Morelli, Giovanna AU - Kusecek, Barica AU - Kolberg, Jan AU - Achtman, Mark PY - 1998/03/01/ UR - http://jb.asm.org/cgi/content/abstract/180/5/1323?ijkey=3305f0d8f84d1a830523b6ca62ec87df844516ad ER -