%0 Journal Article %1 frosch_conserved_1992 %A Frosch, M %A Müller, D %A Bousset, K %A Müller, A %D 1992 %J Infection and Immunity %K Acid Amino Animals, Antibodies, Bacterial Base C, Conformation Data, Epitopes, Inbred Membrane Mice, Molecular Monoclonal, Neisseria Outer Protein Proteins, Sequence Sequence, meningitidis, {BALB} %N 3 %P 798--803 %T Conserved outer membrane protein of Neisseria meningitidis involved in capsule expression %U http://www.ncbi.nlm.nih.gov/pubmed/1371768 %V 60 %X In Neisseria meningitidis, translocation of capsular polysaccharides to the cell surface is mediated by a transport system that fits the characteristics of ABC (ATP-binding cassette) transporters. One protein of this transport system, termed CtrA, is located in the outer membrane. By use of a CtrA-specific monoclonal antibody, we could demonstrate that CtrA occurs exclusively in N. meningitidis and not in other pathogenic or nonpathogenic Neisseria species. Nucleotide sequence comparison of the ctrA gene from different meningococcal serogroups indicated that CtrA is strongly conserved in all meningococcal serogroups, independent of the chemical composition of the capsular polysaccharide. Secondary structure analysis revealed that CtrA is anchored in the outer membrane by eight membrane-spanning amphipathic beta strands, a structure of proteins that function as porins.

@article{frosch_conserved_1992, abstract = {In Neisseria meningitidis, translocation of capsular polysaccharides to the cell surface is mediated by a transport system that fits the characteristics of {ABC} {(ATP-binding} cassette) transporters. One protein of this transport system, termed {CtrA,} is located in the outer membrane. By use of a {CtrA-specific} monoclonal antibody, we could demonstrate that {CtrA} occurs exclusively in N. meningitidis and not in other pathogenic or nonpathogenic Neisseria species. Nucleotide sequence comparison of the {ctrA} gene from different meningococcal serogroups indicated that {CtrA} is strongly conserved in all meningococcal serogroups, independent of the chemical composition of the capsular polysaccharide. Secondary structure analysis revealed that {CtrA} is anchored in the outer membrane by eight membrane-spanning amphipathic beta strands, a structure of proteins that function as porins.}, added-at = {2011-03-11T10:05:34.000+0100}, author = {Frosch, M and Müller, D and Bousset, K and Müller, A}, biburl = {https://www.bibsonomy.org/bibtex/2921b2c6e5d5cb2cd6f80d1b54b1344d4/jelias}, interhash = {eac77e052e9316318e713130cd16db62}, intrahash = {921b2c6e5d5cb2cd6f80d1b54b1344d4}, issn = {0019-9567}, journal = {Infection and Immunity}, keywords = {Acid Amino Animals, Antibodies, Bacterial Base C, Conformation Data, Epitopes, Inbred Membrane Mice, Molecular Monoclonal, Neisseria Outer Protein Proteins, Sequence Sequence, meningitidis, {BALB}}, month = mar, note = {{PMID:} 1371768}, number = 3, pages = {798--803}, timestamp = {2011-03-11T10:06:24.000+0100}, title = {Conserved outer membrane protein of Neisseria meningitidis involved in capsule expression}, url = {http://www.ncbi.nlm.nih.gov/pubmed/1371768}, volume = 60, year = 1992 }