%0 Journal Article %1 schmitt_functional_2007 %A Schmitt, Corinna %A Turner, David %A Boesl, Maria %A Abele, Marion %A Frosch, Matthias %A Kurzai, Oliver %D 2007 %J Journal of Bacteriology %K Adhesion, Bacterial Cell Cells, Epithelial Humans, Line, Neisseria Phylogeny Proteins, ag_kurzai meningitidis, %N 22 %P 7968--7976 %R 10.1128/JB.00851-07 %T A functional two-partner secretion system contributes to adhesion of Neisseria meningitidis to epithelial cells %U http://www.ncbi.nlm.nih.gov/pubmed/17873034 %V 189 %X Neisseria meningitidis is a frequent commensal of the human nasopharynx causing severe invasive infections in rare cases. A functional two-partner secretion (TPS) system in N. meningitidis, composed of the secreted effector protein HrpA and its cognate transporter HrpB, is identified and characterized in this study. Although all meningococcal strains harbor at least one TPS system, the hrpA genes display significant C-terminal sequence variation. Meningococcal genes encoding the TPS effector proteins and their transporters are closely associated and transcribed into a single mRNA. HrpA proteins are translocated across the meningococcal outer membrane by their cognate transporters HrpB and mainly released into the environment. During this process, HrpA is proteolytically processed to a mature 180-kDa form. In contrast to other known TPS systems, immature HrpA proteins are stable in the absence of HrpB and accumulate within the bacterial cell. A small percentage of mature HrpA remains associated with the bacteria and contributes to the interaction of meningococci with epithelial cells.

@article{schmitt_functional_2007, abstract = {Neisseria meningitidis is a frequent commensal of the human nasopharynx causing severe invasive infections in rare cases. A functional two-partner secretion {(TPS)} system in N. meningitidis, composed of the secreted effector protein {HrpA} and its cognate transporter {HrpB,} is identified and characterized in this study. Although all meningococcal strains harbor at least one {TPS} system, the {hrpA} genes display significant C-terminal sequence variation. Meningococcal genes encoding the {TPS} effector proteins and their transporters are closely associated and transcribed into a single {mRNA.} {HrpA} proteins are translocated across the meningococcal outer membrane by their cognate transporters {HrpB} and mainly released into the environment. During this process, {HrpA} is proteolytically processed to a mature {180-kDa} form. In contrast to other known {TPS} systems, immature {HrpA} proteins are stable in the absence of {HrpB} and accumulate within the bacterial cell. A small percentage of mature {HrpA} remains associated with the bacteria and contributes to the interaction of meningococci with epithelial cells.}, added-at = {2011-04-07T15:44:20.000+0200}, author = {Schmitt, Corinna and Turner, David and Boesl, Maria and Abele, Marion and Frosch, Matthias and Kurzai, Oliver}, biburl = {https://www.bibsonomy.org/bibtex/2b6003d5910e56035cbc58fbbaf784581/hymi}, doi = {10.1128/JB.00851-07}, interhash = {047dba5040bcfc521f551906ac900405}, intrahash = {b6003d5910e56035cbc58fbbaf784581}, issn = {1098-5530}, journal = {Journal of Bacteriology}, keywords = {Adhesion, Bacterial Cell Cells, Epithelial Humans, Line, Neisseria Phylogeny Proteins, ag_kurzai meningitidis,}, month = nov, note = {{PMID:} 17873034}, number = 22, pages = {7968--7976}, timestamp = {2011-04-07T16:35:57.000+0200}, title = {A functional two-partner secretion system contributes to adhesion of Neisseria meningitidis to epithelial cells}, url = {http://www.ncbi.nlm.nih.gov/pubmed/17873034}, volume = 189, year = 2007 }