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ProGlyProt ID
Organism Information
Organism Name
Neisseria gonorrhoeae N400 /MS11
Family: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)
Genome Sequence(s)
Organism Additional Information
Neisseria gonorrhoeae is the etiologic agent of the human disease gonorrhoea. It is equipped with a variety of adherence factors that help 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
Protein Information
Protein Name
Fimbrial protein (pilin)
UniProtKB/SwissProt ID
UniProtKB Sequence
Sequence length
165 AA
Subcellular Location
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 Protein
Glycosite(s) Annotated Protein Sequence
>sp|P02974|FMM1_NEIGO Fimbrial protein OS=Neisseria gonorrhoeae GN=pilE1 PE=1 SV
Sequence Around Glycosites (21 AA)
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 acive 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.
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
OST GenBank Gene Sequence
OST Protein Name
OST UniProtKB/ SwissProt ID
OST UniProtKB Sequence
OST Genome Context
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.
1) Jennings, M.P., Jen, F.E., 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. Cell Microbiol, 13, 885-896. [PubMed: 21371235]
2) Aas, F.E., Vik, A., 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. Mol Microbiol, 65, 607-624. [PubMed: 17608667]
3) Chamot-Rooke, J., Rousseau, B., Lanternier, F., Mikaty, G., Mairey, E., Malosse, C., Bouchoux, G., Pelicic, V., Camoin, L., Nassif, X. et al. (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]
4) 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. Mol Cell, 23, 651-662. [PubMed: 16949362]
5) Hegge, F.T., Hitchen, P.G., Aas, F.E., Kristiansen, H., Lovold, C., Egge-Jacobsen, W., Panico, M., Leong, W.Y., Bull, V., Virji, M. et al. (2004) Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili. Proc Natl Acad Sci U S A, 101, 10798-10803. [PubMed: 15249686]
6) 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. Mol Microbiol, 31, 743-752. [PubMed: 10048019]
7) Parge, H.E., Forest, K.T., Hickey, M.J., Christensen, D.A., Getzoff, E.D. and Tainer, J.A. (1995) Structure of the fibre-forming protein pilin at 2.6 A resolution. Nature, 378, 32-38. [PubMed: 7477282]
Additional Comments
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 flexible-loop region within the globular domain of the protein.
Year of Identification
Year of Validation
Copyright @ 2011 IMTECH
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