ProGP99

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ProGP ID ProGP99
Validation Status Characterized
Organism Information
Organism NameNeisseria meningitidis serogroup B strain C3113/ MC58
Domain Bacteria
Classification Family: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 491
Genome Sequence(s)
GenBank AE002098.2
EMBL AE002098
Organism Additional Information Neisseria meningitidis (Gram-negative bacterium) is the causative agent of cerebrospinal meningitis. Sometimes, it crosses the epithelium using its pili to enter the bloodstream. After rapid proliferation, this leads to septicemia. It also crosses the blood-brain barrier to proliferate in the brain.
Gene Information
Gene NamepilE (NMB0018)
NCBI Gene ID 902121
GenBank Gene Sequence 902121
Protein Information
Protein NamePilE (pilin)
UniProtKB/SwissProt ID P05431
NCBI RefSeq NP_273084.1
EMBL-CDSAAF40497.1
UniProtKB Sequence >sp|P05431|FMM1_NEIMB Fimbrial protein OS=Neisseria meningitidis serogroup B GN=pilE PE=1 SV=2 MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLN HGEWPGNNTSAGVATSSEIKGKYVKSVEVKNGVVTAQMASSNVNNEIKGKKLSLWAKRQN GSVKWFCGQPVTRDKAKAANDDVTAAAAANGKKIDTKHLPSTCRDASDAS
Sequence length 170 AA
Subcellular LocationSurface
Function Major structural subunit of class 1 pili. Crucial role in both colonization of the host and adhesion to host cells.
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Propeptide: 1-7) S70
Experimentally Validated Glycosite(s ) in Mature ProteinS63
Glycosite(s) Annotated Protein Sequence >sp|P05431|FMM1_NEIMB Fimbrial protein OS=Neisseria meningitidis serogroup B GN=pilE PE=1 SV=2 MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLN HGEWPGNNTS*(70)AGVATSSEIKGKYVKSVEVKNGVVTAQMASSNVNNEIKGKKLSLWAKRQN GSVKWFCGQPVTRDKAKAANDDVTAAAAANGKKIDTKHLPSTCRDASDAS
Sequence Around Glycosites (21 AA) NHGEWPGNNTSAGVATSSEIK
Technique(s) used for Glycosylation DetectionRapid migration after deglycosylation, mass shift detected on SDS-polyacrylamide gel and biotin-hydrazide labelling
Technique(s) used for Glycosylated Residue(s) Detection Gas-phase Edman sequencing and site-directed mutagenesis (S63A)
Protein Glycosylation- Implication 5NβOHC47NfmPse has the same basic structure common to the sialic acid family of sugars, which have been postulated to function as biological masks protecting sensitive protein structures. Therefore, the presence of the pilin glycan may protect the pili from complement binding and phagocytosis or protect potential epitopes from the host B-cell response. Further, the glycosylation helps in the solubilization of the pilin monomers and/or individual pilus fibres (of strain 8013).
Glycan Information
Glycan Annotation Linkage: DATDH-Ser.
Unusual trisaccharide molecule, Gal(β1-4)Gal(α1-3)2,4-diacetimido-2,4,6-trideoxyhexose [Gal(β1-4)Gal(α1-3)DATDH].
In N. meningitidis 8013 strain, 2-glyceramido 4-acetamido 2,4,6-trideoxyhexose (GATDH) has been found in place of DATDH.
BCSDB ID20030
Technique(s) used for Glycan Identification GC-MS of alditol acetates obtained by trifluoro acetic acid (TFA) hydrolysis of permethylated HPLC fractions, and GC-MS after trimethylsilyl ether derivatization of oligosaccharides reductively eliminated from the peptide.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NamePglL
OST ProGT IDProGT15
Characterized Accessory Gene(s)PglA, PglB2, PglE. Galactosyltransferase PglA transfers the galactose to DATDH. PglE catalyzes the attachment of the terminal galactose to the glycan. PglBCD enzymes are essential for biosynthesis of DATDH from GlcNAc. PglB (B1) also catalyzes transfer of DATDH onto the lipid carrier. PglF is the flippase. PglB2 is a glyceramido transferase that synthesizes GATDH and transfers it onto the lipid carrier.
Accessory Gene(s)Progt IDProGT15.1-ProGT15.6
Additional CommentMS11 strain containing the pglB2 allele from the 8013 strain expresses a pilin modified with a GATDH (2-acetamido 4-glyceramido 2,4,6-trideoxyhexose).
Sequone feature: S/T plus low complexity region, the glycan modifications are found on a flexible-loop region within the globular domain of the protein.
Literature
Year of Identification1993
Year of Identification Month Wise1993.12
Year of Validation 1998
ReferenceChamot-Rooke J, Rousseau B, Lanternier F, Mikaty G, Mairey E, Malosse C, Bouchoux G, Pelicic V, Camoin L, Nassif X, Duménil G. (2007) Alternative Neisseria spp. type IV pilin glycosylation with a glyceramido acetamido trideoxyhexose residue. Proc Natl Acad Sci U S A, 104, 14783-14788. [PubMed: 17804791]
AuthorChamot-Rooke J, Rousseau B, Lanternier F, Mikaty G, Mairey E, Malosse C, Bouchoux G, Pelicic V, Camoin L, Nassif X, Duménil G.
Research GroupEcole Polytechnique, Laboratory of Reaction Mechanisms, Department of Chemistry, F-91128 Palaiseau, France.
Corresponding Author Duménil G.
ContactEcole Polytechnique, Laboratory of Reaction Mechanisms, Department of Chemistry, F-91128 Palaiseau, France.
ReferencePower, P.M., Seib, K.L. and Jennings, M.P. (2006) Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli. Biochem Biophys Res Commun, 347, 904-908. [PubMed: 16870136]
Author Power, P.M., Seib, K.L. Jennings, M.P.
Research GroupSchool of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Qld 4072, Australia.
Corresponding Author Jennings, M.P.
ContactSchool of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Qld 4072, Australia.
Reference Power, P.M., Roddam, L.F., Dieckelmann, M., Srikhanta, Y.N., Tan, Y.C., Berrington, A.W. and Jennings, M.P. (2000) Genetic characterization of pilin glycosylation in Neisseria meningitidis. Microbiology, 146 ( Pt 4), 967-979. [PubMed: 10784055]
Author Power, P.M., Roddam, L.F., Dieckelmann, M., Srikhanta, Y.N., Tan, Y.C., Berrington, A.W. Jennings, M.P.
Research GroupDepartment of Microbiology and Parasitology, The University of Queensland, Brisbane, Australia.
Corresponding Author Jennings, M.P.
ContactDepartment of Microbiology and Parasitology, The University of Queensland, Brisbane, Australia.
Reference Marceau, M., Forest, K., Beretti, J.L., Tainer, J. and Nassif, X. (1998) Consequences of the loss of O-linked glycosylation of meningococcal type IV pilin on piliation and pilus-mediated adhesion. Mol Microbiol, 27, 705-715. [PubMed: 9515697]
Author Marceau, M., Forest, K., Beretti, J.L., Tainer, J. Nassif, X.
Research GroupINSERM U411, Laboratory of Microbiology, Faculty of Medicine Necker-Enfants Malades, Paris, France.
Corresponding Author Nassif, X.
ContactINSERM U411, Laboratory of Microbiology, Faculty of Medicine Necker-Enfants Malades, Paris, France.
Reference Virji, M., Stimson, E., Makepeace, K., Dell, A., Morris, H.R., Payne, G., Saunders, J.R. and Moxon, E.R. (1996) Posttranslational modifications of meningococcal pili. Identification of a common trisaccharide substitution on variant pilins of strain C311. Ann N Y Acad Sci, 797, 53-64. [PubMed: 8993351]
Author Virji, M., Stimson, E., Makepeace, K., Dell, A., Morris, H.R., Payne, G., Saunders, J.R. Moxon, E.R.
Research GroupDepartment of Peadiatrics, University of Oxford, John Radcliffe Hospital, UK
Corresponding Author Moxon, E.R
ContactDepartment of Peadiatrics, University of Oxford, John Radcliffe Hospital, UK
Reference Stimson, E., Virji, M., Makepeace, K., Dell, A., Morris, H.R., Payne, G., Saunders, J.R., Jennings, M.P., Barker, S., Panico, M. et al. (1995) Meningococcal pilin: a glycoprotein substituted with digalactosyl 2,4-diacetamido-2,4,6-trideoxyhexose. Mol Microbiol, 17, 1201-1214. [PubMed: 8594338]
Author Stimson, E., Virji, M., Makepeace, K., Dell, A., Morris, H.R., Payne, G., Saunders, J.R., Jennings, M.P., Barker, S., Panico, M. et al
Research GroupDepartment of Paediatrics, University of Oxford, John Radcliffe Hospital, UK.
Corresponding Author Stimson, E.
ContactDepartment of Paediatrics, University of Oxford, John Radcliffe Hospital, UK.
Reference Virji, M., Saunders, J.R., Sims, G., Makepeace, K., Maskell, D. and Ferguson, D.J. (1993) Pilus-facilitated adherence of Neisseria meningitidis to human epithelial and endothelial cells: modulation of adherence phenotype occurs concurrently with changes in primary amino acid sequence and the glycosylation status of pilin. Mol Microbiol, 10, 1013-1028. [PubMed: 7934852]
Author Virji, M., Saunders, J.R., Sims, G., Makepeace, K., Maskell, D. and Ferguson, D.J.
Research GroupDepartment of Paediatrics, University of Oxford, John Radcliffe Hospital, UK
Corresponding Author Ferguson, D.J
ContactDepartment of Paediatrics, University of Oxford, John Radcliffe Hospital, UK