Fibronectin-, vitronectin- and laminin-binding proteins at the cell walls of Candida parapsilosis and Candida tropicalis pathogenic yeasts

Kozik, Andrzej; Karkowska-Kuleta, Justyna; Zajac, Dorota; Bochenska, Oliwia; Kedracka-Krok, Sylwia; Jankowska, Urszula; Rapala-Kozik, Maria

doi:10.1186/s12866-015-0531-4

Table 1 Mass spectrometric identification of fibronectin-, vitronectin- and laminin-binding C. parapsilosis and C. tropicalis cell wall-associated proteins

From: Fibronectin-, vitronectin- and laminin-binding proteins at the cell walls of Candida parapsilosis and Candida tropicalis pathogenic yeasts

C. parapsilosis
NCBI protein database accession number	Protein	Molecular mass [kDa]	Scores	Number of peptides	Sequence coverage [%]	Method of extraction from fungal cell wall		Method of identification
NCBI protein database accession number	Protein	Molecular mass [kDa]	Scores	Number of peptides	Sequence coverage [%]	β-1,3-glucanase	β-1,6-glucanase	AFC	CL
Fibronectin-binding proteins
gi\|354547941	hypothetical protein CPAR2_404800 [C. parapsilosis], cell wall agglutinin, N-terminal, ligand sugar binding	143.6	736	13	14		+	+
gi\|354547939	hypothetical protein CPAR2_404780 [C. parapsilosis], cell wall agglutinin, N-terminal, ligand sugar binding	113.6	525	10	13		+	+
gi\|354546787	hypothetical protein CPAR2_211630 [C. parapsilosis], similar to C. albicans Eft2, elongation factor 2	93.8	259	11	14	+	+	+	+
gi\|354547813	hypothetical protein CPAR2_403510 [C. parapsilosis], similar to C. albicans Rbt1, cell wall protein with similarity to Hwp1, required for virulence	83.8	73	2	1		+		+
gi\|354545198	hypothetical protein CPAR2_804740 [C. parapsilosis], similar to C. albicans Tkl1, putative transketolase	74.6	166	6	8	+	+	+	+
gi\|354545113	hypothetical protein CPAR2_803890 [C. parapsilosis], similar to C. albicans Mls1, malate synthase	62.7	1434	32	72	+	+	+	+
gi\|354544475	hypothetical protein CPAR2_301880 [C. parapsilosis], putative amidase	61.7	938	18	38	+	+	+	+
gi\|354546116	hypothetical protein CPAR2_204880 [C. parapsilosis], similar to C. albicans Pgi1, putative glucose-6-phosphate isomerase	61.5	104	3	7		+	+
gi\|354545980	hypothetical protein CPAR2_203520 [C. parapsilosis], similar to C. albicans Gnd1, putative 6-phosphogluconate dehydrogenase	55.4	184	5	15	+	+		+
gi\|354546805	hypothetical protein CPAR2_211810 [C. parapsilosis], similar to C. albicans Gpm1, phosphoglycerate mutase	27.6	366	13	33		+		+
Vitronectin-binding proteins
gi\|8927048	elongation factor 2 [C. parapsilosis]	90.3	362	8	10	+	+	+	+
gi\|354545198	hypothetical protein CPAR2_804740 [C. parapsilosis], similar to C. albicans Tkl1, putative transketolase	74.6	146	3	4	+	+	+	+
gi\|354545113	hypothetical protein CPAR2_803890 [C. parapsilosis], similar to C. albicans Mls1, malate synthase	62.7	927	19	43		+	+	+
gi\|354544475	hypothetical protein CPAR2_301880 [C. parapsilosis], putative amidase	62.1	1452	25	45	+	+	+	+
gi\|354546116	hypothetical protein CPAR2_204880 [C. parapsilosis], similar to C. albicans Pgi1, putative glucose-6-phosphate isomerase	61.5	655	15	22		+	+
gi\|354545980	hypothetical protein CPAR2_203520 [C. parapsilosis], similar to C. albicans Gnd1, putative 6-phosphogluconate dehydrogenase	55.4	636	14	31	+	+	+	+
gi\|354546348	hypothetical protein CPAR2_207210 [C. parapsilosis], similar to C. albicans Eno1, enolase	47	229	4	13		+	+
gi\|354545888	hypothetical protein CPAR2_202600 [C. parapsilosis], similar to C. albicans Tal1, putative transaldolase	35.7	526	10	36		+	+
Laminin-binding proteins
gi\|354547939	hypothetical protein CPAR2_404780 [C. parapsilosis], cell wall agglutinin, N-terminal, ligand sugar binding	113.6	93	3	2		+	+
gi\|354545113	hypothetical protein CPAR2_803890 [C. parapsilosis], similar to C. albicans Mls1, malate synthase	62.7	425	9	20		+		+
gi\|354544475	hypothetical protein CPAR2_301880 [C. parapsilosis], putative amidase	61.7	1629	67	58	+	+		+
gi\|354546805	hypothetical protein CPAR2_211810 [C. parapsilosis], similar to C. albicans Gpm1, phosphoglycerate mutase	27.3	167	4	18	+			+
Fibronectin-binding proteins
gi\|255722852	predicted protein [C. tropicalis MYA-3404], hyphally regulated cell wall protein, N-terminal	194.6	202	6	4		+	+
gi\|255728333	malate synthase [C. tropicalis MYA-3404]	62.4	921	23	58		+	+	+
gi\|255727881	enolase 1 [C. tropicalis MYA-3404]	46.9	619	33	55		+	+	+
gi\|255732698	fructose-1,6-bisphosphatase [C. tropicalis MYA-3404]	40.5	134	4	14	+	+	+	+
gi\|255722021	transaldolase [C. tropicalis MYA-3404]	35.5	123	3	8		+	+
Vitronectin-binding proteins
gi\|255722852	predicted protein [C. tropicalis MYA-3404], hyphally regulated cell wall protein, N-terminal	194.6	107	3	2		+	+
gi\|240134900	elongation factor 2 [Candida tropicalis MYA-3404]	90.2	378	10	11		+	+
gi\|255728333	malate synthase [C. tropicalis MYA-3404]	62.4	529	12	25		+		+
gi\|255727881	enolase 1 [C. tropicalis MYA-3404]	46.9	157	5	18	+		+
gi\|255732698	fructose-1,6-bisphosphatase [C. tropicalis MYA-3404]	40.5	320	7	25	+	+	+	+
gi\|255722021	transaldolase [C. tropicalis MYA-3404]	35.5	513	10	28		+		+
Laminin-binding proteins
gi\|255722852	predicted protein [C. tropicalis MYA-3404], hyphally regulated cell wall protein, N-terminal	194.6	103	2	1		+	+
gi\|240134900	elongation factor 2 [Candida tropicalis MYA-3404]	90.2	259	7	8		+	+
gi\|255728333	malate synthase [C. tropicalis MYA-3404]	62.4	337	10	22		+	+	+
gi\|240132975	peroxisomal catalase [Candida tropicalis MYA-3404]	55.1	104	3	5		+	+
gi\|255727881	enolase 1 [C. tropicalis MYA-3404]	46.9	189	4	12		+	+
gi\|255732698	fructose-1,6-bisphosphatase [C. tropicalis MYA-3404]	40.5	136	4	15	+		+
gi\|255722021	transaldolase [C. tropicalis MYA-3404]	35.5	487	12	44		+	+

Cell wall-associated proteins were extracted from C. parapsilosis and C. tropicalis pseudohyphae, using either β-1,3-glucanase (+β-mercaptoethanol) or β-1,6-glucanase. Subsets of ECMP-binding proteins were isolated from the whole cell wall protein mixtures, using affinity chromatography (AFC) or cross-linking (CL) methods. After SDS-PAGE electrophoresis, specific protein bands were excised and digested using trypsin. Peptides were analyzed using the UltiMate 3000 RSLCnano System coupled to a micrOTOF-QII mass spectrometer and Apollo Source ESI nano-sprayer (for AFC-isolated proteins) or an Dionex Ultimate 3000 UHPLC system coupled to an HCT Ultra ETDII mass spectrometer equipped with an ESI ion source (for CL-isolated proteins). The obtained lists of peaks were searched against the NCBI protein database using an in-house Mascot server. The data represent a combination of results obtained for the extracts of cell wall-associated proteins, prepared from three independent yeast cultures. For a given extraction method (β-1,3-glucanase vs. β-1,6-glucanase) and ECMP-binder isolation method (AFC vs. CL), only those proteins are listed that were found on the analysis of all three yeast cultures. Hence, each “+” sign means that a given protein was found at least three times. The best Mascot parameters (scores, number of identified peptides and sequence coverage) ever recorded for a given protein are specified; the proteins identified with a score > 70 and a number of identified peptides ≥ 2 are only listed

Back to article page

ISSN: 1471-2180

Contact us

General enquiries: journalsubmissions@springernature.com

BMC Microbiology

Contact us