Table I

Summary of confirmed identifications of cell surface-associated protein spots

Spot namea,bProtein functionCell wall fractioncMr (kDa)dpIdHyphal inductioneNo. matched peptidesfPercentage of sequence coveragegAccession numberb
I. Classical CWPs
 Bgl2pβ-1,3-Glucosyltransferase135–374.3820CA1541
 Hsp150p/Pir2p150-kDa heat shock glycoprotein, member of the Pir-CWP family2,3,41503.5–5.1MS/MSh,i,j
 PhrpGPI-anchored pH-responsive glycosyl transferase (homologue of S. cerevisiae Gas1p)1,3,4130–1453.5–5.1MS/MSh,i,j
 10–11Putative β-1,3-glucanasek335–373.4–4.2MS/MSh,i,k
II. Heat shock and chaperone proteins
 Hsp90p90-kDa heat shock protein1824.7+2639CA4959
 Ssa1pMember of the HSP70 family1744.7–4.86–1413–37CA2857
 Ssa4pMember of the HSP70 family1714.8–4.98–1714–30CA1230
1694.9–5.1+9–2119–39
 Ssb1pMember of the HSP70 family1664.9–5.111–2625–36CA3534
 Ssd1p/Kar2pMember of the HSP70 family174–784.613–1623–32CA0915
 Ssz1p/Pdr13pMember of the HSP70 family1664.6822CA4844
 Hsp104p104-kDa heat shock protein1995.3–5.516–2721–33CA5135
III. Folding proteins
 Pdi1pProtein disulfide isomerase1734.4+1423CA1755
1704.41222
IV. Elongation factors
 Eft3pTranslation elongation factor 311165.3–5.516–3114–28CA3081
 Eft2pTranslation elongation factor 21936.3–6.512–1516–24CA2810
 Tef1pTranslation elongation factor 1α1517.6–8.91130CA0362
 Efb1pTranslation elongation factor 1β1354.1MS/MSh,lCA4862
V. Glycolytic and fermentation enzymes
 Fba1pFructose-bisphosphate aldolase1395.8+1745CA5180
2405.9725
4405.9+930
 Tpi1pTriose phosphate isomerase1305.6729CA5950
 Gap1pGlyceraldehyde-3-phosphate1356.4–7.7+4–1313–50CA5892
 dehydrogenase2356.9–7.56–1122–42
3357.1–7.75–916–31
4357.0–7.4+4–617–31
 Pgk1pPhosphoglycerate kinase1465.8–6.0+4–915–22CA1691
2465.8–6.06–717–19
3465.9–6.1+5–813–20
4465.8–6.0+4–615–17
 Gpm1pPhosphoglycerate mutase1305.7935CA4671
 Eno1pEnolase1485.4–5.6+6–1310–37CA3874
2485.4–5.56–1118–28
3485.4–5.5+9–1224–30
4485.3–5.4+7–2024–52
 Cdc19pPyruvate kinase1606.4–6.7+13–1528–39CA3483
2606.4–6.710–1218–38
 Pdc11pPyruvate decarboxylase1625.1–5.2+10–1217–20CA2474
2635.0–5.27–915–17
4635.0–5.1+11–1320–33
 Adh1pAlcohol dehydrogenase1455.6–5.7+4–89–14CA4765
2455.7–5.84–67–13
VI. Miscellaneous
 Csp37p37-kDa cell surface protein1357.1923CA1075
 Psa1pGDP-mannose pyrophosphorylase1415.7–5.9+13–1735–47CA3208
 Ino1pmyo-Inositol-1-phosphate synthase1585.1–5.2+6–1218–30CA5986
 Cdc48pMember of the ATPases associated with diverse cellular activities (AAA) superfamily1974.8–4.81418CA3333
 Bmh2pHomolog of mammalian 14-3-3 protein1344.5830CA5050
VII. Unknown function proteins and others
 ORF6713Unknown function1334.7+630CA4220
1334.8734
 4–5NDm245–573.7–4.3sMS/MSh,i,j
 17ND21604.2MS/MSh,i,j
 6ND3100–1755.7MS/MSh,i,j
 8ND3764.1MS/MSh,i,j
 15ND4325.2sMS/MSh,i,j,l
 16ND4215.8sMS/MSh,i,j,l
  • a Spot name as given on the Fig. 3–6.

  • b Protein name and accession number according to CandidaDB (genolist.pasteur.fr/CandidaDB).

  • c Cell wall fractions obtained from isolated walls by SDS and DTT (fraction 1), NaOH (fraction 2), Quantazyme (fraction 3), and exochitinase (fraction 4) treatment.

  • d Experimental Mr and pI (Melanie 3.0).

  • e Specific (s), up-regulated (+), or down-regulated (−) proteins after germ tube induction.

  • f Number of peptide masses matching the top hit from MS-Fit peptide mass fingerprinting. For several isoforms of a single protein, the minimum and maximum numbers of peptides matched are only given.

  • g Amino acid sequence coverage for the identified protein. For several isoforms of a single protein, the minimum and maximum percentages of sequence coverage are only given.

  • h Proteins analyzed by tandem mass spectrometry using a MALDI-TOF/TOF mass spectrometer.

  • i Spots in-gel deglycosylated with PNGase F before trypsin digestion.

  • j Peptide sequences that failed to match against C. albicans databases or partial short amino acid sequences that did not enable their positive identification.

  • k Two of its peptides were identified as the sequences ESTVAGFLVGSEALYR and NDLTASQLSDKINDVR from S. cerevisiae Bgl2p, but not from C. albicans Bgl2p, notwithstanding the fact that C. albicans Bgl2p is present in databases and we have identified it here by peptide mass fingerprinting. It might be a protein of the same family hitherto unannotated in C. albicans databases.

  • l Low molecular weight proteins with only few tryptic fragments present in their peptide mass fingerprinting.

  • m ND, not determined.