The pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductase
O-Glycosylation is emerging as a common posttranslational modification of surface exposed proteins in bacterial mucosal pathogens. In pathogenic Neisseria an O-glycosylation pathway modifies a single abundant protein, pilin, the subunit protein that forms pili. Here, we identify an additional outer...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2009-01, Vol.378 (1), p.84-89 |
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| creator | Ku, S.C. Schulz, B.L. Power, P.M. Jennings, M.P. |
| description | O-Glycosylation is emerging as a common posttranslational modification of surface exposed proteins in bacterial mucosal pathogens. In pathogenic
Neisseria an
O-glycosylation pathway modifies a single abundant protein, pilin, the subunit protein that forms pili. Here, we identify an additional outer membrane glycoprotein in pathogenic
Neisseria, the nitrite reductase AniA, that is glycosylated in its C-terminal repeat region by the pilin glycosylation pathway. To our knowledge, this is the first report of a general
O-glycosylation pathway in a prokaryote. We also show that AniA displays polymorphisms in residues that map to the surface of the protein. A frame-shift mutation abolishes AniA expression in 34% of
Neisseria meningitidis strains surveyed, however, all
Neisseria gonorrhoeae strains examined are predicted to express AniA, implying a crucial role for AniA in gonococcal biology. |
| doi_str_mv | 10.1016/j.bbrc.2008.11.025 |
| format | Article |
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Neisseria an
O-glycosylation pathway modifies a single abundant protein, pilin, the subunit protein that forms pili. Here, we identify an additional outer membrane glycoprotein in pathogenic
Neisseria, the nitrite reductase AniA, that is glycosylated in its C-terminal repeat region by the pilin glycosylation pathway. To our knowledge, this is the first report of a general
O-glycosylation pathway in a prokaryote. We also show that AniA displays polymorphisms in residues that map to the surface of the protein. A frame-shift mutation abolishes AniA expression in 34% of
Neisseria meningitidis strains surveyed, however, all
Neisseria gonorrhoeae strains examined are predicted to express AniA, implying a crucial role for AniA in gonococcal biology.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2008.11.025</identifier><identifier>PMID: 19013435</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; AniA ; Antigens, Bacterial - chemistry ; Antigens, Bacterial - genetics ; Antigens, Bacterial - immunology ; Antigens, Bacterial - metabolism ; Bacterial Outer Membrane Proteins - chemistry ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - immunology ; Bacterial Outer Membrane Proteins - metabolism ; Fimbriae Proteins - metabolism ; Glycosylation ; Molecular Sequence Data ; Neisseria gonorrhoeae ; Neisseria gonorrhoeae - enzymology ; Neisseria gonorrhoeae - immunology ; Neisseria gonorrhoeae - pathogenicity ; Neisseria meningitidis ; Neisseria meningitidis - enzymology ; Neisseria meningitidis - pathogenicity ; Neisseria meningitiis ; Nitrite reductase ; Nitrite Reductases - chemistry ; Nitrite Reductases - genetics ; Nitrite Reductases - immunology ; Nitrite Reductases - metabolism ; O-Glycosylation ; Protein Conformation ; Protein Processing, Post-Translational</subject><ispartof>Biochemical and biophysical research communications, 2009-01, Vol.378 (1), p.84-89</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-4ed260e819d24e217ab17db0451cc0a24bc8499c5554aaf16bc562f8cc2e196f3</citedby><cites>FETCH-LOGICAL-c385t-4ed260e819d24e217ab17db0451cc0a24bc8499c5554aaf16bc562f8cc2e196f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2008.11.025$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19013435$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ku, S.C.</creatorcontrib><creatorcontrib>Schulz, B.L.</creatorcontrib><creatorcontrib>Power, P.M.</creatorcontrib><creatorcontrib>Jennings, M.P.</creatorcontrib><title>The pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductase</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>O-Glycosylation is emerging as a common posttranslational modification of surface exposed proteins in bacterial mucosal pathogens. In pathogenic
Neisseria an
O-glycosylation pathway modifies a single abundant protein, pilin, the subunit protein that forms pili. Here, we identify an additional outer membrane glycoprotein in pathogenic
Neisseria, the nitrite reductase AniA, that is glycosylated in its C-terminal repeat region by the pilin glycosylation pathway. To our knowledge, this is the first report of a general
O-glycosylation pathway in a prokaryote. We also show that AniA displays polymorphisms in residues that map to the surface of the protein. A frame-shift mutation abolishes AniA expression in 34% of
Neisseria meningitidis strains surveyed, however, all
Neisseria gonorrhoeae strains examined are predicted to express AniA, implying a crucial role for AniA in gonococcal biology.</description><subject>Amino Acid Sequence</subject><subject>AniA</subject><subject>Antigens, Bacterial - chemistry</subject><subject>Antigens, Bacterial - genetics</subject><subject>Antigens, Bacterial - immunology</subject><subject>Antigens, Bacterial - metabolism</subject><subject>Bacterial Outer Membrane Proteins - chemistry</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - immunology</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Fimbriae Proteins - metabolism</subject><subject>Glycosylation</subject><subject>Molecular Sequence Data</subject><subject>Neisseria gonorrhoeae</subject><subject>Neisseria gonorrhoeae - enzymology</subject><subject>Neisseria gonorrhoeae - immunology</subject><subject>Neisseria gonorrhoeae - pathogenicity</subject><subject>Neisseria meningitidis</subject><subject>Neisseria meningitidis - enzymology</subject><subject>Neisseria meningitidis - pathogenicity</subject><subject>Neisseria meningitiis</subject><subject>Nitrite reductase</subject><subject>Nitrite Reductases - chemistry</subject><subject>Nitrite Reductases - genetics</subject><subject>Nitrite Reductases - immunology</subject><subject>Nitrite Reductases - metabolism</subject><subject>O-Glycosylation</subject><subject>Protein Conformation</subject><subject>Protein Processing, Post-Translational</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQhy0EotvCC3BAPnEiYcaxk1jisqqgIFX0UiRuluNMul7lz2I7RXkE3posu1JvcJrR6JufRvMx9gYhR8Dywz5vmuByAVDniDkI9YxtEDRkAkE-ZxsAKDOh8ccFu4xxD4AoS_2SXaAGLGShNuz3_Y74wfd-5HfZQ7-4KS69TX4a-cGm3S-78Kn7204PNHrHv5GPkYK33Edu-TqkYHsel5ho4GlnE3-Koci3o9--53bk05wo8IGGJtiR-OhT8Il4oHZ2yUZ6xV50to_0-lyv2PfPn-6vv2S3dzdfr7e3mStqlTJJrSiBatStkCSwsg1WbQNSoXNghWxcLbV2SilpbYdl41Qputo5QajLrrhi7065hzD9nCkmM_joqO_Xq6Y5mrKshBaF_i-IWlUCKrWC4gS6MMUYqDOH4AcbFoNgjqbM3hxNmaMpg2hWU-vS23P63AzUPq2c1azAxxNA6zMePQUTnafRUesDuWTayf8r_w_AIacQ</recordid><startdate>20090102</startdate><enddate>20090102</enddate><creator>Ku, S.C.</creator><creator>Schulz, B.L.</creator><creator>Power, P.M.</creator><creator>Jennings, M.P.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20090102</creationdate><title>The pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductase</title><author>Ku, S.C. ; Schulz, B.L. ; Power, P.M. ; Jennings, M.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-4ed260e819d24e217ab17db0451cc0a24bc8499c5554aaf16bc562f8cc2e196f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>AniA</topic><topic>Antigens, Bacterial - chemistry</topic><topic>Antigens, Bacterial - genetics</topic><topic>Antigens, Bacterial - immunology</topic><topic>Antigens, Bacterial - metabolism</topic><topic>Bacterial Outer Membrane Proteins - chemistry</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial Outer Membrane Proteins - immunology</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Fimbriae Proteins - metabolism</topic><topic>Glycosylation</topic><topic>Molecular Sequence Data</topic><topic>Neisseria gonorrhoeae</topic><topic>Neisseria gonorrhoeae - enzymology</topic><topic>Neisseria gonorrhoeae - immunology</topic><topic>Neisseria gonorrhoeae - pathogenicity</topic><topic>Neisseria meningitidis</topic><topic>Neisseria meningitidis - enzymology</topic><topic>Neisseria meningitidis - pathogenicity</topic><topic>Neisseria meningitiis</topic><topic>Nitrite reductase</topic><topic>Nitrite Reductases - chemistry</topic><topic>Nitrite Reductases - genetics</topic><topic>Nitrite Reductases - immunology</topic><topic>Nitrite Reductases - metabolism</topic><topic>O-Glycosylation</topic><topic>Protein Conformation</topic><topic>Protein Processing, Post-Translational</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ku, S.C.</creatorcontrib><creatorcontrib>Schulz, B.L.</creatorcontrib><creatorcontrib>Power, P.M.</creatorcontrib><creatorcontrib>Jennings, M.P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ku, S.C.</au><au>Schulz, B.L.</au><au>Power, P.M.</au><au>Jennings, M.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2009-01-02</date><risdate>2009</risdate><volume>378</volume><issue>1</issue><spage>84</spage><epage>89</epage><pages>84-89</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>O-Glycosylation is emerging as a common posttranslational modification of surface exposed proteins in bacterial mucosal pathogens. In pathogenic
Neisseria an
O-glycosylation pathway modifies a single abundant protein, pilin, the subunit protein that forms pili. Here, we identify an additional outer membrane glycoprotein in pathogenic
Neisseria, the nitrite reductase AniA, that is glycosylated in its C-terminal repeat region by the pilin glycosylation pathway. To our knowledge, this is the first report of a general
O-glycosylation pathway in a prokaryote. We also show that AniA displays polymorphisms in residues that map to the surface of the protein. A frame-shift mutation abolishes AniA expression in 34% of
Neisseria meningitidis strains surveyed, however, all
Neisseria gonorrhoeae strains examined are predicted to express AniA, implying a crucial role for AniA in gonococcal biology.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>19013435</pmid><doi>10.1016/j.bbrc.2008.11.025</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2009-01, Vol.378 (1), p.84-89 |
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| subjects | Amino Acid Sequence AniA Antigens, Bacterial - chemistry Antigens, Bacterial - genetics Antigens, Bacterial - immunology Antigens, Bacterial - metabolism Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - immunology Bacterial Outer Membrane Proteins - metabolism Fimbriae Proteins - metabolism Glycosylation Molecular Sequence Data Neisseria gonorrhoeae Neisseria gonorrhoeae - enzymology Neisseria gonorrhoeae - immunology Neisseria gonorrhoeae - pathogenicity Neisseria meningitidis Neisseria meningitidis - enzymology Neisseria meningitidis - pathogenicity Neisseria meningitiis Nitrite reductase Nitrite Reductases - chemistry Nitrite Reductases - genetics Nitrite Reductases - immunology Nitrite Reductases - metabolism O-Glycosylation Protein Conformation Protein Processing, Post-Translational |
| title | The pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductase |
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