GSPB_STRGN
ID GSPB_STRGN Reviewed; 3072 AA.
AC Q939N5;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 23-FEB-2022, entry version 75.
DE RecName: Full=Platelet binding protein GspB;
DE AltName: Full=Adhesin GspB {ECO:0000305};
DE AltName: Full=Serine-rich adhesin for platelets;
DE AltName: Full=Serine-rich repeat protein GspB;
DE Flags: Precursor;
GN Name=gspB;
OS Streptococcus gordonii.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=M99;
RX PubMed=12010500; DOI=10.1046/j.1365-2958.2002.02949.x;
RA Bensing B.A., Sullam P.M.;
RT "An accessory sec locus of Streptococcus gordonii is required for export of
RT the surface protein GspB and for normal levels of binding to human
RT platelets.";
RL Mol. Microbiol. 44:1081-1094(2002).
RN [2]
RP S.GORDONII IN INFECTIVE ENDOCARDITIS.
RX PubMed=8366515; DOI=10.1099/00222615-39-3-179;
RA Douglas C.W., Heath J., Hampton K.K., Preston F.E.;
RT "Identity of viridans streptococci isolated from cases of infective
RT endocarditis.";
RL J. Med. Microbiol. 39:179-182(1993).
RN [3]
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=M99;
RX PubMed=14729688; DOI=10.1128/jb.186.3.638-645.2004;
RA Bensing B.A., Gibson B.W., Sullam P.M.;
RT "The Streptococcus gordonii platelet binding protein GspB undergoes
RT glycosylation independently of export.";
RL J. Bacteriol. 186:638-645(2004).
RN [4]
RP EXPORT VIA THE ACCESSORY SECA2/SECY2 SYSTEM.
RC STRAIN=M99;
RX PubMed=15049820; DOI=10.1111/j.1365-2958.2004.03978.x;
RA Takamatsu D., Bensing B.A., Sullam P.M.;
RT "Genes in the accessory sec locus of Streptococcus gordonii have three
RT functionally distinct effects on the expression of the platelet-binding
RT protein GspB.";
RL Mol. Microbiol. 52:189-203(2004).
RN [5]
RP GLYCOSYLATION OF SER-RICH REGIONS.
RC STRAIN=M99;
RX PubMed=15489421; DOI=10.1128/jb.186.21.7100-7111.2004;
RA Takamatsu D., Bensing B.A., Sullam P.M.;
RT "Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii
RT mediate the intracellular glycosylation of the platelet-binding protein
RT GspB.";
RL J. Bacteriol. 186:7100-7111(2004).
RN [6]
RP DISCUSSION OF SEQUENCE.
RX PubMed=19202081; DOI=10.1099/mic.0.025221-0;
RA Zhou M., Wu H.;
RT "Glycosylation and biogenesis of a family of serine-rich bacterial
RT adhesins.";
RL Microbiology 155:317-327(2009).
RN [7]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=M99;
RX PubMed=20714350; DOI=10.1371/journal.ppat.1001044;
RA Sanchez C.J., Shivshankar P., Stol K., Trakhtenbroit S., Sullam P.M.,
RA Sauer K., Hermans P.W., Orihuela C.J.;
RT "The pneumococcal serine-rich repeat protein is an intra-species bacterial
RT adhesin that promotes bacterial aggregation in vivo and in biofilms.";
RL PLoS Pathog. 6:E1001044-E1001044(2010).
RN [8]
RP INTERACTION WITH ASP2 AND ASP3.
RX PubMed=21531800; DOI=10.1128/jb.00057-11;
RA Yen Y.T., Seepersaud R., Bensing B.A., Sullam P.M.;
RT "Asp2 and Asp3 interact directly with GspB, the export substrate of the
RT Streptococcus gordonii accessory Sec System.";
RL J. Bacteriol. 193:3165-3174(2011).
RN [9]
RP GLYCOSYLATION OF SER-RICH REGIONS.
RC STRAIN=M99;
RX PubMed=26884191; DOI=10.1073/pnas.1600494113;
RA Chen Y., Seepersaud R., Bensing B.A., Sullam P.M., Rapoport T.A.;
RT "Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis
RT of a bacterial adhesion protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E1190-E1199(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 245-604, FUNCTION, MUTAGENESIS OF
RP TYR-443; ARG-484 AND TYR-485, AND INTERACTION WITH HUMAN GP1BA.
RX PubMed=21765814; DOI=10.1371/journal.ppat.1002112;
RA Pyburn T.M., Bensing B.A., Xiong Y.Q., Melancon B.J., Tomasiak T.M.,
RA Ward N.J., Yankovskaya V., Oliver K.M., Cecchini G., Sulikowski G.A.,
RA Tyska M.J., Sullam P.M., Iverson T.M.;
RT "A structural model for binding of the serine-rich repeat adhesin GspB to
RT host carbohydrate receptors.";
RL PLoS Pathog. 7:E1002112-E1002112(2011).
CC -!- FUNCTION: Plays a role in virulence and host-pathogen interactions.
CC Mediates binding to human platelets via interaction with the human cell
CC surface glycoprotein GP1BA (PubMed:21765814). Plays a positive role in
CC biofilm formation, possibly by self-association via the basic region
CC (BR) (PubMed:20714350). {ECO:0000269|PubMed:20714350,
CC ECO:0000269|PubMed:21765814}.
CC -!- SUBUNIT: Both SSR domains in the unglycosylated protein bind to Asp2
CC and Asp3; glycosylated protein binds less well. Interacts with the
CC human cell surface glycoprotein GP1BA. {ECO:0000269|PubMed:21531800,
CC ECO:0000269|PubMed:21765814}.
CC -!- INTERACTION:
CC Q939N5; Q9AET8: asp2; NbExp=4; IntAct=EBI-6414561, EBI-6414583;
CC Q939N5; Q9AET7: asp3; NbExp=4; IntAct=EBI-6414561, EBI-6414568;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:12010500,
CC ECO:0000269|PubMed:14729688}; Peptidoglycan-anchor
CC {ECO:0000269|PubMed:12010500, ECO:0000269|PubMed:14729688}.
CC Note=Exported by the accessory SecA2/SecY2 protein translocation
CC apparatus. {ECO:0000269|PubMed:12010500}.
CC -!- DOMAIN: Has a short and long Ser-rich region with a basic region
CC between them. The SRR domains themselves are comprised of inexact
CC repeats of SASESASTSASV. SSR1 has 6 repeats, SSR2 has 200. The Ser-rich
CC regions are both glycosylated. The basic region (BR) binds to whole
CC cell lysates of wild-type but not bacteria deleted of this gene; it
CC also recognizes whole cell lysates of S.aureus strain ISP479C probably
CC via SraP, but not lysates of S.pneumoniae TIGR4 (PubMed:20714350). The
CC predicted pI of the basic region is 9.51 (PubMed:19202081).
CC {ECO:0000269|PubMed:20714350, ECO:0000303|PubMed:19202081}.
CC -!- PTM: Proteolytically cleaved by a metalloprotease. {ECO:0000250}.
CC -!- PTM: Both SSR1 and SSR2 domains are glycosylated (Probable). A
CC truncated derivative (residues 1-2062) contains 105 nmol per nmol of
CC protein, suggesting at least 10% of the apparent molecular weight is
CC due to carbohydrates (PubMed:14729688). Glucose and N-acetylglucosamine
CC are present in a ratio of 30:73 residues per truncated polypeptide, as
CC well as minor amounts of galactose and N-acetylgalactosamine
CC (PubMed:14729688). Glycosylation occurs intracellularly in the Ser-rich
CC regions SSR1 and SSR2 (PubMed:14729688, PubMed:15489421). Glycosylation
CC of SSR2 domain may be required to prevent aggregation of GspB
CC (Probable). It is probable that most of the Ser residues in SSR1 and
CC SSR2 are O-GlcNAcylated. Sequential glycosylation by sugar transferases
CC are able to generate complex sugar polymorphisms (By similarity).
CC {ECO:0000250|UniProtKB:A0A0H2URK1, ECO:0000269|PubMed:14729688,
CC ECO:0000269|PubMed:15489421, ECO:0000305|PubMed:14729688,
CC ECO:0000305|PubMed:15489421, ECO:0000305|PubMed:26884191}.
CC -!- DISRUPTION PHENOTYPE: Loss of adherence to human platelet cells
CC (PubMed:12010500). Decrease in early biofilm formation
CC (PubMed:20714350). {ECO:0000269|PubMed:12010500,
CC ECO:0000269|PubMed:20714350}.
CC -!- MISCELLANEOUS: S.gordonii, a commensal oral cavity bacteria, is among
CC the bacteria most frequently identified as being the primary
CC etiological agents of subacute infective endocarditis (found in 13% of
CC cases). {ECO:0000269|PubMed:8366515}.
CC -!- SIMILARITY: Belongs to the serine-rich repeat protein (SRRP) family.
CC {ECO:0000305}.
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DR EMBL; AY028381; AAL13053.1; -; Genomic_DNA.
DR PDB; 3QC5; X-ray; 1.40 A; X=245-604.
DR PDB; 3QC6; X-ray; 1.90 A; X=245-604.
DR PDB; 5IUC; X-ray; 1.25 A; A/B=399-521.
DR PDB; 6EF7; X-ray; 1.03 A; A=399-521.
DR PDB; 6EF9; X-ray; 1.30 A; A=398-521.
DR PDB; 6EFA; X-ray; 1.60 A; A=399-601.
DR PDBsum; 3QC5; -.
DR PDBsum; 3QC6; -.
DR PDBsum; 5IUC; -.
DR PDBsum; 6EF7; -.
DR PDBsum; 6EF9; -.
DR PDBsum; 6EFA; -.
DR SMR; Q939N5; -.
DR IntAct; Q939N5; 2.
DR UniLectin; Q939N5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR044024; aRib.
DR InterPro; IPR022263; KxYKxGKxW.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR026465; Ser_adhes_glycop.
DR Pfam; PF18938; aRib; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR TIGRFAMs; TIGR04224; ser_adhes_Nterm; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; Glycoprotein; Peptidoglycan-anchor;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..85
FT /evidence="ECO:0000255"
FT CHAIN 86..3041
FT /note="Platelet binding protein GspB"
FT /id="PRO_0000414192"
FT PROPEP 3042..3072
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000414193"
FT REGION 117..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..236
FT /note="Ser-rich region 1 (SSR1)"
FT REGION 182..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..603
FT /note="Basic region (BR)"
FT REGION 604..3028
FT /note="Ser-rich region 2 (SSR2)"
FT REGION 876..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..2085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2106..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2173..2223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2250..2595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2625..2967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3014..3045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3038..3042
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 182..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3014..3044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 443
FT /note="Important for interaction with host glycoprotein and
FT virulence"
FT SITE 484
FT /note="Important for interaction with host glycoprotein and
FT virulence"
FT SITE 485
FT /note="Important for interaction with host glycoprotein and
FT virulence"
FT MOD_RES 3041
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 443
FT /note="Y->F: Strongly reduced interaction with GP1BA
FT carbohydrate chains."
FT /evidence="ECO:0000269|PubMed:21765814"
FT MUTAGEN 484
FT /note="R->E: Strongly reduced interaction with GP1BA
FT carbohydrate chains. Strongly reduced platelet binding."
FT /evidence="ECO:0000269|PubMed:21765814"
FT MUTAGEN 485
FT /note="Y->F: Strongly reduced interaction with GP1BA
FT carbohydrate chains."
FT /evidence="ECO:0000269|PubMed:21765814"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:3QC5"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:3QC6"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 351..364
FT /evidence="ECO:0007829|PDB:3QC5"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:3QC6"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3QC5"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 386..395
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 418..426
FT /evidence="ECO:0007829|PDB:6EF7"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 480..487
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:6EF7"
FT HELIX 499..508
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:6EF7"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:3QC5"
FT HELIX 541..554
FT /evidence="ECO:0007829|PDB:3QC5"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:3QC5"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:3QC5"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:3QC5"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:3QC5"
FT STRAND 598..601
FT /evidence="ECO:0007829|PDB:3QC5"
SQ SEQUENCE 3072 AA; 285769 MW; 0B148372697CF7F2 CRC64;
MFFKRQKGQY HEVERVTRFK LIKSGKHWLR AATSQFGLLR LMKGSDVSST EVKVVEEQSV
EKSGLNYLKG IIATGAVLGG AVVTSSSVYA EEEQAHEKVI DTRDVLATRG EAVLSEEAAT
TLSSTEANPV ESLSDTLSAS ESTSASSSVS TSISVSESFS VSGSLSYSTS LSQSVSASAS
ASESLSVSSS ASDSVSASTS TSASASQSVS ASQKSTISTS ESTRSESSQQ STEASSQTGR
RRTRRAVTES APNVEYHDVK GDMIQSVTTS FDDTSRLLTW TINLTPRQVK SNLGALVSIS
GNQETRTVTI NGKNAANGGV YNSGGAWNLY TGESVNNNVL RITTQVNDTG GEVKLGLRLV
TSDKKITKTN LPLEFSQVAA TTNGSWDKAG YNTTIVEKDT ERPVVNVPSE ITVYRGESFE
YFATVTDNSN AFDLAKTVVR WLYNNQPGRG TEWLQYSVTQ VGNQLKVRIF GNVPIDTTIG
DYTRYVVATD AAGNVNATQT EMGNAAVDKT SVNGQFKLII RFRIKTPENT VFVNNPNQLT
EVEKNLVREA VKKSNPDLRA QDVLNSNYVT GITVSNNGTT TITYRDGRKD IIDGSKFIDT
RAGSISKSQS TSNSISVSLS KSESASASLV TSKLNSISSS ASVSASTSIS TSGSVSASES
ASTSSSVSAS ESASTSASVS ASESASTSAS VSASTSASTS ASVSASTSAS TSASTSASKS
ASTSASVSAS TSASTSASVS ASESASTSAS VSASTSASTS ASVSASTSAS TSASVSASES
ASTSASVSAS TSASTSASVS ASESASTSAS VSASTSASTS ASVSASASAS TSASVSASTS
ASTSASVSAS ASASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS ESASTSASVS ASTSASTSAS VSASTSASTS ASVSASTSAS TSASVSASTS
ASTSASVSAS ESASTSASVS ASESASTSAS VSASTSASTS ASVSASESAS TSASVSASES
ASTSASESAS ESASTSASVS ASESASTSAS VSASESSSTS ASVSASESSS TSASVSASES
ASTSASVSAS ESASTSASES ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS
ASTSASVSAS ESASTSTSVS TSTSASTSAS VSASESASTS ASVSASESAS TSASVSASTS
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS TSTSTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASKS
ASTSESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESVSTSASVS ASDSASISAS
VLASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSSSVS ASESASTSAS
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS
VSASESASTS ASVSSSESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
VSASESASTS ASVSASESAS TSASVSASMS ASTSASVSVS ESTSTSASVS ANESASTSAS
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS
VSANESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
VSASTSASTS ASVSANESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
VSASESASTS ASVSASTSAS TSASVSASES ASTSASASAS ESASTSASVS ASESASTSAS
VSASESASTS ASVSASESAS TNASVSVSES MSVSESLSLS ISTSVLHSQL NDIYESELYS
LSLSESLSAS QSLSQSLSES QSSSASQSMH DRISKGQLPR TGESENKASI LALGLGALGL
AFKKRKKNES ED
