ProGP76 (Cell surface lipoprotein MPB83 (25/23-kDa antigen))

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ProGP ID ProGP76 (Cell surface lipoprotein MPB83 (25/23-kDa antigen))
Validation Status Characterized
Organism Information
Organism NameMycobacterium bovis AN5
Domain Bacteria
Classification Phylum : Actinobacteria
Class : Actinomycetia
Orders : Corynebacteriales
Family : Mycobacteriaceae
Genus : Mycobacterium
Species : bovis
Strain : AN5
Taxonomic ID (NCBI) 1765
Genome Information
GenBank LT708304.1
EMBL BX248344
Organism Additional Information Mycobacterium bovis is the etiologic agent of bovine tuberculosis.
Gene Information
Gene Namempb83 (Mb2898)
NCBI Gene ID 1092210
GenBank Gene Sequence NC_002945
Protein Information
Protein NameCell surface lipoprotein MPB83 (25/23-kDa antigen)
UniProtKB/SwissProt ID P0CAX7
NCBI RefSeq WP_003414630.1
EMBL-CDSEU683972
UniProtKB Sequence >sp|P0CAX7|MP83_MYCBO Cell surface lipoprotein MPB83 OS=Mycobacterium bovis GN=mpb83 PE=4 SV=1 MINVQAKPAAAASLAAIAIAFLAGCSSTKPVSQDTSPKPATSPAAPVTTAAMADPAADLI GRGCAQYAAQNPTGPGSVAGMAQDPVATAASNNPMLSTLTSALSGKLNPDVNLVDTLNGG EYTVFAPTNAAFDKLPAATIDQLKTDAKLLSSILTYHVIAGQASPSRIDGTHQTLQGADL TVIGARDDLMVNNAGLVCGGVHTANATVYMIDTVLMPPAQ
Sequence length 220 AA
Subcellular LocationSurface (membrane associated)
Function Major immunodominant antigen.
Glycosylation Status
Glycosylation Type O- (Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinT48, T49
Experimentally Validated Glycosite(s ) in Mature ProteinT48, T49
Glycosite(s) Annotated Protein Sequence >sp|P0CAX7|MP83_MYCBO Cell surface lipoprotein MPB83 OS=Mycobacterium bovis GN=mpb83 PE=4 SV=1 MINVQAKPAAAASLAAIAIAFLAGCSSTKPVSQDTSPKPATSPAAPVT*(48)T*(49)AAMADPAADLI GRGCAQYAAQNPTGPGSVAGMAQDPVATAASNNPMLSTLTSALSGKLNPDVNLVDTLNGG EYTVFAPTNAAFDKLPAATIDQLKTDAKLLSSILTYHVIAGQASPSRIDGTHQTLQGADL TVIGARDDLMVNNAGLVCGGVHTANATVYMIDTVLMPPAQ
Sequence Around Glycosites (21 AA) KPATSPAAPVTTAAMADPAAD
PATSPAAPVTTAAMADPAADL
ProGP Web Logo
Technique(s) used for Glycosylation DetectionConcanavalin A (ConA)-binding, DIG glycan detection (labeling with digoxigenin-succinyl-epsilon-amidocaproic acid hydrazide and anti-DIG antibody after periodate oxidation)
Technique(s) used for Glycosylated Residue(s) Detection Q-TOF nanoelectrospray MS-MS (hybrid quadrupole orthogonal acceleration time of flight), deletion analysis and site-directed mutagenesis
Protein Glycosylation- Implication Glycosylation may function either as a signal for cleavage or as a means of preventing amino-terminal degradation of the protein following cleavage from its acylated anchor. This is because the 23-kDa form of MPB83 is generated by proteolytic cleavage immediately before Thr48 from the mature acylated 25-kDa form.
Glycan Information
Glycan Annotation Linkage: Man-Thr.
3 mannose units present with Man(1→3)Man linkage. The dominant glycoform identified for MPB83 is Thr48 substituted with a single mannose residue and Thr49 substituted with a Man(1→3)Man linkage. However, evidence for a heterogeneous array of glycoforms from Thr48(Man3) Thr49(Man0) through to Thr48(Man0)Thr49(Man3) has also been observed.
BCSDB ID 3436
Technique(s) used for Glycan Identification Dionex ion chromatography of sugars after their release by acid hydrolysis, FAB-MS (fast atom bombardment-mass spectrometry) of permethylated O-glycans after their release by reductive elimination, and GC-MS linkage analysis of the partially methylated alditol acetates, derived from the permethylated products of reductive elimination.
Protein Glycosylation linked (PGL) gene(s)
Additional Comment23-kDa is the predominant form of the antigen in the culture supernatant.
25/23-kDa antigen was misidentified as glycosylated form of MPB70. It is actually MPB83 antigen.
Literature
Year of Identification1991
Year of Identification Month Wise1991.03
Year of Validation 2003
ReferenceMichell, S.L., Whelan, A.O., Wheeler, P.R., Panico, M., Easton, R.L., Etienne, A.T., Haslam, S.M., Dell, A., Morris, H.R., Reason, A.J. and Herrmann, J.L., 2003. The MPB83 Antigen from Mycobacterium bovis ContainsO-Linked Mannose and (1→ 3)-Mannobiose Moieties. Journal of Biological Chemistry, 278(18), pp.16423-16432.
Corresponding Author Stephen L Michell
ContactTB Research Group, Department of Bacterial Diseases, Veterinary Laboratories Agency (Weybridge), New Haw, Addlestone, Surrey KT15 3NB, UK. slmichell@dstl.gov.uk
ReferenceFifis, T.H.E.O.D.O.R.A., Costopoulos, C.H.R.Y.S., Radford, A.J., Bacic, A.N.T.O.N.Y. and Wood, P.R., 1991. Purification and characterization of major antigens from a Mycobacterium bovis culture filtrate. Infection and immunity, 59(3), pp.800-807.
Corresponding Author Theodora Fifis
ContactCommonwealth Scientific and Industrial Research Organisation, Division of Animal Health, Parkville, Victoria Australia.