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ProGlyProt ID
BC159
Organism Information
Organism Name
Neisseria meningitidis serogroup B strain C311#3/ MC58
Domain
Bacteria
Classification
Family: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
GenBank
EMBL
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
GenBank Gene Sequence
 
 
Protein Information
Protein Name
PilE (pilin)
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence
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.
 
 
Protein Structure
Homology Model
Homology Model File
 
 
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 GSVKW
FCGQPVTRDKAKAANDDVTAAAAANGKKIDTKHLPSTCRDASDAS
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
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 NCBI Gene ID
OST GenBank Gene Sequence
OST Protein Name
PglL
OST UniProtKB/ SwissProt ID
OST NCBI RefSeq
OST EMBL-CDS
OST UniProtKB Sequence
OST EC Number (BRENDA)
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.
PGL Additional Links
 
 
Literature
Reference(s)
1) 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]
2) 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. Biochem Biophys Res Commun, 347, 904-908. [PubMed: 16870136]
3) 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]
4) 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]
5) 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]
6) 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]
7) 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]
Additional Comments
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).
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
1993
Year of Validation
1998
 
 
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