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. 2008 Sep 19;7(11):1951–1964. doi: 10.1128/EC.00284-08

TABLE 2.

Covalently bound C. glabrata CWPs identified by LC/MS/MSa

Category and protein name ORF no. Properties and proposed functionb MS/MS result
Conserved functional domain(s)d Closest S. cerevisiae homolog (SGD namee) Closest C. albicans homolog (CGD namee) Reference for C. glabrata protein name
Sequence coverage (%) No. of peptides identifiedc
Carbohydrate-active enzymes
    Crh1 CAGL0G09449g SP, GPI, 452 aa. GH16 transglycosidase, involved in chitin incorporation 22 11 GH16: 34-240 Crh1f Crh11f 67
    Utr2 CAGL0C02211g SP, GPI, 481 aa. GH16 transglycosidase, involved in chitin incorporation 6 2 CBM 18: 23-64; GH16: 93-303 Utr2f Utr2f 67
    Gas1 CAGL0G00286g SP, GPI, 559 aa. GH72 transglycosidase, elongation of 1,3-β-glucan 8 1 (+ 2) GH72: 25-329; X8: 377-459 Gas1f Phr2,f Phr1f 66
    Gas2 CAGL0M13849g SP, GPI, 565 aa. GH72 transglycosidase, elongation of 1,3-β-glucan 10 2 (+ 2) GH72: 26-330; X8: 378-460 Gas1f Phr2,f Phr1f 66
    Gas4 CAGL0F03883g SP, GPI, 480 aa. GH72 transglycosidase, elongation of 1,3-β-glucan 12 3 GH 2: 20-350 Gas3f Phr3, Pga4f
    Gas5 CAGL0F01287g SP, GPI, 523 aa. GH72 transglycosidase, elongation of 1,3-β-glucan 24 10 GH72: 27-331 Gas5f Pga4f
    Scw4 CAGL0G00308g SP, no GPI, 374 aa. GH17 transglycosidase, modification of 1,3-β-glucan 28 8 GH17: 118-372 Scw4f MP65/Scw1f
Other enzymatic activity
    Plb2 CAGL0J11748g SP, GPI, 695 aa. phospholipase 10 6 PLAc: 33-550 Plb2f Plb3
Nonenzymatic CWPs
    Cwp1.1 CAGL0F07601g SP, GPI, 218 aa. structural mannoprotein 53 13 (+ 26) None Cwp1f None 67
    Cwp1.2 CAGL0F07579g SP, GPI, 212 aa. structural mannoprotein 55 4 (+ 26) None Cwp1f none 67
    Ssr1 CAGL0H06413g SP, GPI, 212 aa. contains CFEM domain 27 6 CFEM: 22-81 Ccw14f Ssr1f
    Tir1 CAGL0F01463g SP, GPI, 221 aa. mannoprotein of the Srp1p/Tip1p family 12 2 None Tir1f None
    Pir1 CAGL0I06204g SP, no GPI, 349 aa. conserved 4-cysteine domain 21 1 (+ 9) 4× Cys: 252-349 Pir1-4f Pir1f 67
    Pir2 CAGL0I06182g SP, no GPI, 340 aa. conserved 4-cysteine domain 26 2 (+ 10) 4× Cys: 243-340 Pir1-4f Pir1f 67
    Pir3 CAGL0M08492g SP, no GPI, 335 aa. conserved 4-cysteine domain 20 11 (+ 2) 4× Cys: 238-335 Pir1-4f Pir1f 67
    Pir4 CAGL0I06160g SP, no GPI, 233 aa. conserved 4-cysteine domain 43 11 4× Cys: 136-233 Pir1-4f Pir1f 67
Unknown proteins
    Ecm33 CAGL0M01826g SP, GPI, 421 aa. unknown role in cell wall biosynthesis 18 7 Unknown Ecm33f, Pst1f Ecm33f, Ecm331
    Pst1 CAGL0E04620g SP, GPI, 429 aa. unknown role in cell wall biosynthesis 6 3 Unknown Ecm33f, Pst1f Ecm33f, Ecm331
Adhesin-like wall proteinsh
    Awp1 CAGL0J02508g SP, GPI, 870 aa. putative adhesin 6 4 Unknown Awa1, Hpf1, Hpf1′ None
    Awp2 CAGL0K00110g SP, GPI, 832 aa. putative adhesin 8 5 Unknown Awa1, Hpf1, Hpf1′ Iff family, Hyr1
    Awp3 CAGL0J11902g- CAGL0J11924g SP, GPI, unknown size putative adhesin 6g 2 Unknown None None
    Awp4 CAGL0J11990-CAGL0J12056g SP, GPI, unknown size putative adhesin 11 + 13g 2 (+ 3) Unknown None Iff family, Hyr1
    Epa6 CAGL0C00110g SP, GPI, 715 aa. adhesin 15 5 (+ 1) PA14: 139-247 Flocculins None 4
a

For mass spectrometric details, see Table S1 in the supplemental material.

b

Predicted signal peptides for secretion (SP) (http://www.cbs.dtu.dk/services/SignalP/) and C-terminal signatures for GPI anchoring (http://mendel.imp.ac.at/gpi/fungi_server.html) are indicated; see also reference 67. Conserved functional domains were identified using CDD v2.03 (http://www.ncbi.nlm.nih.gov/structure/cdd/cdd.shtml), CAZy (http://www.cazy.org/), and reference 15. GH, glycoside hydrolase; aa, amino acids.

c

Numbers in parentheses indicate nonunique peptides.

d

Identified as outlined in footnote b.

e

SGD, Saccharomyces Genome Database (http://www.yeastgenome.org/); CGD, Candida Genome Database (http://www.candidagenome.org/).

f

Identified as covalently bound cell wall protein using LC/MS/MS (13, 58, 70, 72).

g

Sequence coverage of identified ORF fragments.

h

Not identified in ATCC 90876 cells that were grown in YEPD to mid-log phase.