ProGP119 (Fimbrial protein (pilin))
Home -> ProGPdb -> Search ProGP -> Display data
| ProGP ID | ProGP119 (Fimbrial protein (pilin)) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Neisseria gonorrhoeae N400/MS11 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Betaproteobacteria Orders : Neisseriales Family : Neisseriaceae Genus : Neisseria Species : gonoorrhoeae Strain : N400/MS11 |
| Taxonomic ID (NCBI) | 485 |
| Genome Information | |
| GenBank | AH000912.2 |
| EMBL | K02078 |
| Organism Additional Information | Neisseria gonorrhoeae is the etiologic agent of the human disease gonorrhoea. It is equipped with a variety of adherence factors that helps it in the colonization of diverse microenvironments in the human host. The property of phase and antigenic variation displayed by its type IV pilin enables it to avoid immune system thereby initiating the disease. |
| Gene Information | |
| Gene Name | pilE1 |
| Protein Information | |
| Protein Name | Fimbrial protein (pilin) |
| UniProtKB/SwissProt ID | P02974 |
| EMBL-CDS | AAA25466.1 |
| UniProtKB Sequence | >sp|P02974|FMM1_NEIGO Fimbrial protein OS=Neisseria gonorrhoeae GN=pilE1 PE=1 SV=2 MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLN HGKWPENNTSAGVASPPSDIKGKYVKEVEVKNGVVTATMLSSGVNNEIKGKKLSLWARRE NGSVKWFCGQPVTRTDDDTVADAKDGKEIDTKHLPSTCRDNFDAK |
| Sequence length | 165 AA |
| Subcellular Location | Surface |
| Function | Major pilin subunit protein of the type IV pilus (Tfp) colonization factor. Type IV pili (Tfp) are proteinaceous polymeric filaments that serve critical roles in disease pathogenesis and prokaryotic cell biology in many Gram-negative species. These multifunctional virulence factors are involved in adhesion to host cell surfaces, modulation of target cell specificity, twitching motility, bacteriophage adsorption and pilus retraction. |
| Protein Structure | |
| PDB ID | 2HI2, 2HIL, 2PIL, 1AY2 |
| 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|P02974|FMM1_NEIGO Fimbrial protein OS=Neisseria gonorrhoeae GN=pilE1 PE=1 SV=2 MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLN HGKWPENNTS*(70)AGVASPPSDIKGKYVKEVEVKNGVVTATMLSSGVNNEIKGKKLSLWARRE NGSVKWFCGQPVTRTDDDTVADAKDGKEIDTKHLPSTCRDNFDAK |
| Sequence Around Glycosites (21 AA) | NHGKWPENNTSAGVASPPSDI |
| Technique(s) used for Glycosylation Detection | Crystallographic analysis (electron density maps) |
| Technique(s) used for Glycosylated Residue(s) Detection | Crystallographic analysis (electron density maps) |
| Protein Glycosylation- Implication | Recently, using primary, human, cervical epithelial (i.e. pex) cells, pilin glycan has been shown to mediate productive cervical infection. For the first time, direct role of the protein-associated bacterial glycan in pathogenesis has been demonstrated (Ref. no. 1). Pilin glycan helps gonococci in binding to the compliment receptor 3 (CR3) I-domain expressed by pex cells when it is in a closed, low-affinity conformation. This leads to the active state of CR3. |
| Glycan Information | |
| Glycan Annotation | Linkage: Bac/DATDH-Ser. Disaccharide composed of a hexose residue linked to a proximal 2,4-diacetamido-2,4,6-trideoxyhexose sugar (HexDATDH). Various X-ray diffraction studies have identified α-D-galactopyranosyl-(1→3)-2,4-diacetamido-2,4-dideoxy-β-D-glucopyranoside (bacillosamine, Bac); Gal-DADDGlc; and GlcNAc-α1,3-Gal, as glycans. DADDGlc has a second acetamido group at C4 of the proximal glucose in place of the hydroxyl group. DADDGlc thus resembles DATDH. However, DATDH lacks the C6 hydroxyl group. This O-linked glycan may be present as a di- or monosaccharide because of phase variation of select pilin glycosylation genes like pglA. Gal-Gal-DATDH has been shown to be present in some strains. |
| BCSDB ID | 29194 |
| GlyTouCan | G27236WI |
| Technique(s) used for Glycan Identification | Crystallographic analysis (electron density maps) and mass spectrometry (MS/MS) |
| Protein Glycosylation linked (PGL) gene(s) | |
| OST Gene Name | PglO |
| OST ProGT ID | 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. PglE has a relaxed substrate specificity. In the majority of the gonococcal strains, PglE is switched off. |
| Accessory Gene(s)Progt ID | ProGT21.1, ProGT21.2, Pro |
| Additional Comment | Replacing the pglB1 allele with the pglB2 allele from the N. meningitidis 8013 strain results in the synthesis of glycan with GATDH (2-acetamido 4-glyceramido 2,4,6-trideoxyhexose). Glycan formation is phase variable. Sequon feature: S/T plus low complexity region, the glycan modifications are found on a fexible-loop region within the globular domain of the protein. |
| Literature | |
| Year of Identification | 1995 |
| Year of Identification Month Wise | 1995.11.01 |
| Year of Validation | 1995 |
| Reference | Jennings, M.P., Jen, F.E.C., Roddam, L.F., Apicella, M.A. and Edwards, J.L., 2011. Neisseria gonorrhoeae pilin glycan contributes to CR3 activation during challenge of primary cervical epithelial cells. Cellular microbiology, 13(6), pp.885-896. |
| Corresponding Author | Jennifer L. Edwards |
| Contact | The Center for Microbial Pathogenesis, The Research Institute at Nationwide Children's Hospital and The Department of Pediatrics, The Ohio State University, Columbus, Ohio 43205, USA |
| Reference | Aas, F.E., Vik, Å., Vedde, J., Koomey, M. and Egge‐Jacobsen, W., 2007. Neisseria gonorrhoeae O‐linked pilin glycosylation: functional analyses define both the biosynthetic pathway and glycan structure. Molecular microbiology, 65(3), pp.607-624. |
| Corresponding Author | Wolfgang Egge-Jacobsen |
| Contact | Centre for Molecular Biology and Neuroscience, Unversity of Oslo, 0316 Oslo, Norway. |
| 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 | Guillaume Dumenil |
| Contact | Ecole Polytechnique, Laboratoire des Mécanismes Réactionnels, Département de Chimie, F-91128 Palaiseau, France |
| Reference | Craig, L., Volkmann, N., Arvai, A.S., Pique, M.E., Yeager, M., Egelman, E.H. and Tainer, J.A., 2006. Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions. Molecular cell, 23(5), pp.651-662. |
| Corresponding Author | John A. Tainer |
| Contact | Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037 |
| Reference | Hegge, F.T., Hitchen, P.G., Aas, F.E., Kristiansen, H., Løvold, C., Egge-Jacobsen, W., Panico, M., Leong, W.Y., Bull, V., Virji, M. and Morris, H.R., 2004. Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili. Proceedings of the National Academy of Sciences, 101(29), pp.10798-10803. |
| Corresponding Author | Michael Koomey |
| Contact | Department of Molecular Biosciences,University of Oslo, 0316 Oslo, Norway |
| Reference | Forest, K.T., Dunham, S.A., Koomey, M. and Tainer, J.A., 1999. Crystallographic structure reveals phosphorylated pilin from Neisseria: phosphoserine sites modify type IV pilus surface chemistry and fibre morphology. Molecular microbiology, 31(3), pp.743-752. |
| Corresponding Author | John A. Tainer |
| Contact | Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA. |