ProGP119 (Fimbrial protein (pilin))

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ProGP ID ProGP119 (Fimbrial protein (pilin))
Validation Status Characterized
Organism Information
Organism NameNeisseria 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 NamepilE1
Protein Information
Protein NameFimbrial protein (pilin)
UniProtKB/SwissProt ID P02974
Sequence length 165 AA
Subcellular LocationSurface
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
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
Sequence Around Glycosites (21 AA) NHGKWPENNTSAGVASPPSDI
Technique(s) used for Glycosylation DetectionCrystallographic 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 NamePglO
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 IDProGT21.1, ProGT21.2, Pro
Additional CommentReplacing 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.
Year of Identification1995
Year of Identification Month Wise1995.11.01
Year of Validation 1995
ReferenceJennings, 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
ContactThe 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
ReferenceAas, 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
ContactCentre for Molecular Biology and Neuroscience, Unversity of Oslo, 0316 Oslo, Norway.
ReferenceChamot-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
ContactEcole Polytechnique, Laboratoire des Mécanismes Réactionnels, Département de Chimie, F-91128 Palaiseau, France
ReferenceCraig, 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
ContactDepartment of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037
ReferenceHegge, 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
ReferenceForest, 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
ContactDepartment of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.