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ProGP ID ProGP190
Validation Status Characterized
Organism Information
Organism NameMycobacterium tuberculosis H37Rv
Domain Bacteria
Classification Family: Mycobacteriaceae
Suborder: Corynebacterineae
Order: Actinomycetales
Subclass: Actinobacteridae
Class: Actinobacteria
Division or phylum: "Actinobacteria"
Taxonomic ID (NCBI) 1773
Genome Sequence(s)
GenBank BX842578.1
EMBL BX842578
Gene Information
Gene NameApa (Rv1860) or modD
NCBI Gene ID 885896
GenBank Gene Sequence 885896
Protein Information
Protein NameAlanine and proline-rich secreted protein Apa (50/55-kDa or 45 kDa MPT 32)
UniProtKB/SwissProt ID P9WIR7
NCBI RefSeq YP_177849.1
EMBL-CDSCAE55438.1
UniProtKB Sequence >sp|P9WIR6|APA_MYCTO Alanine and proline-rich secreted protein Apa OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=apa PE=3 SV=1 MHQVDPNLTRRKGRLAALAIAAMASASLVTVAVPATANADPEPAPPVPTTAASPPSTAAA PPAPATPVAPPPPAAANTPNAQPGDPNAAPPPADPNAPPPPVIAPNAPQPVRIDNPVGGF SFALPAGWVESDAAHLDYGSALLSKTTGDPPFPGQPPPVANDTRIVLGRLDQKLYASAEA TDSKAAARLGSDMGEFYMPYPGTRINQETVSLDANGVSGSASYYEVKFSDPSKPNGQIWT GVIGSPAANAPDAGPPQRWFVVWLGTANNPVDKGAAKALAESIRPLVAPPPAPAPAPAEP APAPAPAGEVAPTPTTPTPQRTLPA
Sequence length 325 AA
Subcellular LocationSecreted
Function Immunodominant antigen. Elicits potent DTH (delayed-type hypersensitivity) responses in living-BCG-immunized guinea pigs..Stimulation of peripheral blood mononuclear cells from PPD positive individuals with Apa induces a Th1 type lymphoproliferative response with expansion of both CD4+ and CD8+ cells and increased IFN-γ production. 2) In Mtb, mannosylated nApa is a potential adhesin and has a role in host cell attachment, entry, and immune evasion, it induces a strong delayed-type hypersensitivity (DTH) in immunized animals, Elicits a mostly Th1 type of T-cell response in healthy humans; induces IFN-gamma production from CD4+ and CD8+ cells, Functions as an adhesin, binds to mouse macrophages via mannose residues
Glycosylation Status
Glycosylation Type O- (Thr) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Signal peptide: 1-39) T49, T57, T66, T316, T313,T315
Experimentally Validated Glycosite(s ) in Mature ProteinT10, T18, T27, T277
Glycosite(s) Annotated Protein Sequence >sp|Q50906|APA_MYCTU Alanine and proline-rich secreted protein apa OS=Mycobacterium tuberculosis GN=apa PE=1 SV=1 MHQVDPNLTRRKGRLAALAIAAMASASLVTVAVPATANADPEPAPPVPT*(49)TAASPPST*(57)AAA PPAPAT*(66)PVAPPPPAAANTPNAQPGDPNAAPPPADPNAPPPPVIAPNAPQPVRIDNPVGGF SFALPAGWVESDAAHFDYGSALLSKTTGDPPFPGQPPPVANDTRIVLGRLDQKLYASAEA TDSKAAARLGSDMGEFYMPYPGTRINQETVSLDANGVSGSASYYEVKFSDPSKPNGQIWT GVIGSPAANAPDAGPPQRWFVVWLGTANNPVDKGAAKALAESIRPLVAPPPAPAPAPAEP APAPAPAGEVAPTPTT*(316)PTPQRTLPA
Sequence Around Glycosites (21 AA) ADPEPAPPVPTTAASPPSTAA
VPTTAASPPSTAAAPPAPATP
STAAAPPAPATPVAPPPPAAA
PAGEVAPTPTTPTPQRTLPA
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionSchiff's staining, peroxidase-conjugated concanavalin A (ConA)-binding
Technique(s) used for Glycosylated Residue(s) Detection N-terminal amino acid sequencing coupled with fast atom bombardment-mass spectrometry (FAB-MS), Edman degradation on a gas-phase sequencer , FAB-MS
Protein Glycosylation- Implication The presence of the mannose residues on the Apa protein was essential for the antigenicity of the molecules in T-cell-dependent immune responses in vitro (proliferation assay) and in vivo (delayed type hypersensitivity or DTH reaction). The deglycosylated antigen was 10-fold less active than native molecules in eliciting DTH. Mannosylation of antigen leads to selective targeting and subsequent greater presentation by dendritic cells. 2) In Mtb,mannosylated nApa is a potential adhesin and has a role in host cell attachment, entry, and immune evasion
Glycan Information
Glycan Annotation Linkage: αMan-Thr.
34.6% sugar detected.
α-D-Manp(1→2)α-D-Manp (mannobiose), α-D-Manp (single mannose), α-D-Manp(1→2)α-D-Manp(1→2)α-D-Manp (mannotriose) are present. T10 and T18 are glycosylated with mannobiose, T27 with single mannose, and T277 with either of the three. The majority of the antigen species bear six, seven, or eight mannose residues (22, 24, and 17%, respectively), while others three, four, or five mannoses (5, 9, and 14%, respectively). Alpha-D-Man, mannobiose, or mannotriose, Thr residues at positions 10 and 18 were substituted a-D-Manp(132)a-D-Manp, position 27 was substituted with a single a-D-Manp, Thr-277 was substituted with either a-D-Manp, a-D-Manp(132)a-D-Manp, or a-D-Manp(132)a-D-Manp (132)a-D-Manp.
Technique(s) used for Glycan Identification GC-MS of partially methylated alditol acetates obtained by trifluoro acetic acid (TFA) hydrolysis of permethylated oligoglycosyl alditols which are released by β-elimination of the glycopeptides.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameProtein O mannosyltransferase
OST ProGT IDProGT10
Characterized Accessory Gene(s)Polyprenol-phosphate-mannose (PPM) synthase, Ppm1, is present. A second type of Ppm synthase (Rv3779 gene product) exclusive to slow-growing mycobacteria, is a membrane glycosyltransferase. It mannosylates polyprenyl-phosphates directly from GDP-mannose.
Accessory Gene(s)Progt IDProGT10.1
Literature
ReferenceMengele, R. and Sumper, M. (1992) Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles. J Biol Chem, 267, 8182-8185.
AuthorMengele, R. and Sumper, M
Research GroupChair of Biochemistry, University of Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M
ContactChair of Biochemistry, University of Regensburg, Federal Republic of Germany
Reference Lechner, J. and Sumper, M. (1987) The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J Biol Chem, 262, 9724-9729. [PubMed: 3036870]
Author Lechner, J. and Sumper, M.
Research GroupInstitute of Biochemistry, Genetics and Microbiology, Uniuersitat Regensburg, Uniuersitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Genetics and Microbiology, Uniuersitat Regensburg, Uniuersitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany
Reference Lechner, J. and Sumper, M. (1987) The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J Biol Chem, 262, 9724-9729. [PubMed: 3036870]
Author Lechner, J. Sumper, M.
Research GroupInstitute of Biochemistry, Genetics and Microbiology, Uniuersitat Regensburg, Uniuersitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Genetics and Microbiology, Uniuersitat Regensburg, Uniuersitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany
Reference Paul, G., Lottspeich, F. and Wieland, F. (1986) Asparaginyl-N-acetylgalactosamine. Linkage unit of halobacterial glycosaminoglycan. J Biol Chem, 261, 1020-1024. [PubMed: 3944078]
Author Paul, G., Lottspeich, F. Wiel
Research GroupInstitute for Biochemistry, University of Regensburg, Universitatsstraje 31, 8400 Regensburg andMax Planck Institute of Biochemistry, Gene Center, At the Klopferspitz, 8033 Martinsried, Federal Republic of Germany
ContactInstitute for Biochemistry, University of Regensburg, Universitatsstraje 31, 8400 Regensburg andMax Planck Institute of Biochemistry, Gene Center, At the Klopferspitz, 8033 Martinsried, Federal Republic of Germany
Reference Lechner, J., Wieland, F. and Sumper, M. (1985) Transient methylation of dolichyl oligosaccharides is an obligatory step in halobacterial sulfated glycoprotein biosynthesis. J Biol Chem, 260, 8984-8989. [PubMed: 4019460]
Author Lechner, J., Wieland, F. and Sumper, M.
Research GroupDepartment of Biochemistry, University of Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactDepartment of Biochemistry, University of Regensburg, Federal Republic of Germany
Reference Wieland, F., Paul, G. and Sumper, M. (1985) Halobacterial flagellins are sulfated glycoproteins. J Biol Chem, 260, 15180-15185. [PubMed: 3934156]
AuthorWieland, F., Paul, G. and Sumper, M.
Research GroupInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, 8400 Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, 8400 Regensburg, Federal Republic of Germany
Reference Wieland, F., Heitzer, R. and Schaefer, W. (1983) Asparaginylglucose: Novel type of carbohydrate linkage. Proc Natl Acad Sci U S A, 80, 5470-5474. [PubMed: 16593364]
Author Wieland, F., Heitzer, R. and Schaefer, W
Research GroupInstitute of Biochemistry, University of Regensburg, D-8400 Regensburg, Federal Republic of Germany.
Corresponding Author Schaefer, W
ContactInstitute of Biochemistry, University of Regensburg, D-8400 Regensburg, Federal Republic of Germany.
Reference Mescher, M.F. and Strominger, J.L. (1976) Purification and characterization of a prokaryotic glucoprotein from the cell envelope of Halobacterium salinarium. J Biol Chem, 251, 2005-2014. [PubMed: 1270419]
Author Mescher, M.F. and Strominger, J.L
Research GroupBiological Laboratories, Harvard University, Cambridge, Massachusetts 02138
Corresponding Author Strominger, J.L.
ContactBiological Laboratories, Harvard University, Cambridge, Massachusetts 02138
Reference Mescher, M.F., Strominger, J.L. and Watson, S.W. (1974) Protein and carbohydrate composition of the cell envelope of Halobacterium salinarium. J Bacteriol, 120, 945-954. [PubMed: 4455689]
Author Mescher, M.F., Strominger, J.L. and Watson, S.W.
Research GroupThe Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138, and Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543
Corresponding Author Watson, S.W
ContactThe Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138, and Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543
Reference Wieland, F., Dompert, W., Bernhardt, G. and Sumper, M. (1980) Halobacterial glycoprotein saccharides contain covalently linked sulphate. FEBS Lett, 120, 110-114. [PubMed: 7439381]
Author Wieland, F., Dompert, W., Bernhardt, G. and Sumper, M.
Research GroupInstitute of Biochemistry, Cenetics and Microbiology, Biochemistry I, Universitiit, 8400 Regensburg, FRG
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Cenetics and Microbiology, Biochemistry I, Universitiit, 8400 Regensburg, FRG