ProGP99 (PilE (pilin))
Home -> ProGPdb -> Search ProGP -> Display data
| ProGP ID | ProGP99 (PilE (pilin)) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Neisseria meningitidis serogroup B strain C311#3/ MC58 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Betaproteobacteria Orders : Neisseriales Family : Neisseriaceae Genus : Neisseria Species : meningitidis Strain : C311#3/ MC58 |
| Taxonomic ID (NCBI) | 491 |
| Genome Information | |
| 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 Name | pilE (NMB0018) |
| NCBI Gene ID | 902121 |
| GenBank Gene Sequence | NC_003112 |
| Protein Information | |
| Protein Name | PilE (pilin) |
| UniProtKB/SwissProt ID | P05431 |
| NCBI RefSeq | WP_010980743.1 |
| EMBL-CDS | AAF40497.1 |
| 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 Location | Surface |
| 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 Protein | S63 |
| 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 Detection | Rapid 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 ID | 20030 |
| GlyTouCan | G45609TX |
| 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 Name | PglL |
| OST ProGT ID | ProGT17 ProGT21 |
| 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 ID | ProGT17.1, ProGT17.2, Pro |
| Additional Comment | MS11 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 modfications are found on a fexible-loop region within the globular domain of the protein. |
| Literature | |
| Year of Identification | 1993 |
| Year of Identification Month Wise | 1993.12 |
| Year of Validation | 1998 |
| Reference | Chamot-Rooke, J., Rousseau, B., Lanternier, F., Mikaty, G., Mairey, E., Malosse, C., Bouchoux, G., Pelicic, V., Camoin, L., Nassif, X. and Duménil, G., 2007. Alternative Neisseria spp. type IV pilin glycosylation with a glyceramido acetamido trideoxyhexose residue. Proceedings of the National Academy of Sciences, 104(37), pp.14783-14788. |
| Corresponding Author | Duménil G |
| Contact | Polytechnic School, Reaction Mechanisms Laboratory, Department of Chemistry, F-91128 Palaiseau, France. |
| Reference | Power, 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. Biochemical and biophysical research communications, 347(4), pp.904-908. |
| Corresponding Author | Michael P Jennings |
| Contact | School 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 meningitidisThe GenBank accession number for the sequence determined in this work is AF014804. Microbiology, 146(4), pp.967-979. |
| Corresponding Author | Michael P Jennings |
| Contact | School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Qld 4072, Australia. |
| Reference | Marceau, M., Forest, K., Béretti, 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. Molecular microbiology, 27(4), pp.705-715. |
| Corresponding Author | Xavier Nassif |
| Contact | INSERM U411, Laboratoire de Microbiologie, Faculté de Médecine 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. Annals of the New York Academy of Sciences, 797, pp.53-64. |
| Corresponding Author | Mumtaz Virji |
| Contact | Department of Paediatrics, 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. and Blench, I., 1995. Meningococcal pilin: a glycoprotein substituted with digalactosyl 2, 4‐diacetamido‐2, 4, 6‐trideoxyhexose. Molecular microbiology, 17(6), pp.1201-1214. |
| Corresponding Author | Mumtaz Virji |
| Contact | Department of Paediatrics, University of Oxford, John Radcliffe Hospital, UK. |
| Reference | Hadjineophytou, C., Anonsen, J.H., Svingerud, T., Mortimer, T.D., Grad, Y.H., Scott, N.E. and Koomey, M., 2022. Sculpting the Bacterial O-Glycoproteome: Functional Analyses of Orthologous Oligosaccharyltransferases with Diverse Targeting Specificities. Mbio, pp.e03797-21. |
| Corresponding Author | Michael Koomey |
| Contact | Department of Biosciences, Section for Genetics and Evolutionary Biology, University of Oslo, Oslo, Norway Department of Biosciences, Centre for Ecological and Evolutionary Synthesis, University of Oslo, Oslo, Norway Norwegian Research Centre AS, Randaberg, Norway. |