The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase

Winram, Scott B.; Lottenberg, Richard

doi:10.1099/13500872-142-8-2311

Cited by 156 publications

(129 citation statements)

References 30 publications

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“…pez-Ribot et al, 1996 ;Lo! pez-Ribot & Chaffin, 1996 ;Modun & Williams, 1999 ;Pancholi & Fischetti, 1992, 1998Winram & Lottenberg, 1996). All these observations favour the idea of the involvement of a nonconventional secretion mechanism for these cell-wall-associated proteins.…”

Section: Discussionmentioning

confidence: 52%

“…mansoni has been associated with human resistance to schistosomiasis (Charrier-Ferrara et al, 1992 ;Goudot-Crozel et al, 1989). In group A streptococci and in Staphylococcus aureus a cell-surface GAPDH is involved in the interaction with host cells and ligands (Modun & Williams, 1999 ;Pancholi & Fischetti, 1992, 1993, 1997Winram & Lottenberg, 1996, 1998. Also eukaryotic micro-organisms contain a cell-wall-associated GAPDH ; in Kluyveromyces marxianus cellular flocculation depends on the expression of a cell-surface GAPDH (Falcao Moreira et al, 1998 ;Fernandes et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

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The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall proteins

et al. 2001

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The authors show that the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Saccharomyces cerevisiae, previously thought to be restricted to the cell interior, is also present in the cell wall. GAPDH activity, proportional to cell number and time of incubation, was detected in intact wild-type yeast cells. Intact cells of yeast strains containing insertion mutations in each of the three structural TDH genes (tdh1, tdh2 and tdh3) and double mutants (tdh1 tdh2 and tdh1 tdh3) also displayed a cell-wall-associated GAPDH activity, in the range of parental wild-type cells, although with significant differences among strains. A cell wall location of GAPDH was further confirmed in wild-type and tdh mutants by indirect immunofluorescence and flow cytometry analysis with a polyclonal antibody against S. cerevisiae GAPDH. By immunoelectron microscopy, the GAPDH protein was detected at the outer surface of the cell wall of wild-type cells, as well as in the cytoplasm. Western immunoblot analysis of cell wall extracts and cytosol showed that Tdh2 and Tdh3 polypeptides are present in the cell wall, as well as in the cytosol, of exponentially growing cells. Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts. The results incorporate the GAPDH of S. cerevisiae, encoded by TDH1-3, into the newly emerging family of multifunctional cell-wall-associated GAPDHs which retain their catalytic activity.

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Section: Discussionmentioning

confidence: 52%

Section: Introductionmentioning

confidence: 99%

The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall proteins

et al. 2001

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“…GAPDH has also been associated with a surface location and different functions in microbial species. First, the enzyme has been reported as a major surface protein on group A streptococci (Streptococcus pyogenes), where it is enzymatically active, binds various mammalian proteins such as lysozyme, fibronectin, actin, myosin, and plasmin (40,57), and also acts as an ADP-ribosylating enzyme (41). Second, in Kluyveromyces marxianus, the same enzyme protein has been identified as a constitutive protein of cell wall putatively involved in the interactions between cells leading to flocculation (15,16).…”

Section: Resultsmentioning

confidence: 99%

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

et al. 1997

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A gt11 cDNA library from Candida albicans ATCC 26555 was screened by using pooled sera from two patients with systemic candidiasis and five neutropenic patients with high levels of anti-C. albicans immunoglobulin M antibodies. Seven clones were isolated from 60,000 recombinant phages. The most reactive one contained a 0.9-kb cDNA encoding a polypeptide immunoreactive only with sera from patients with systemic candidiasis. The whole gene was isolated from a genomic library by using the cDNA as a probe. The nucleotide sequence of the coding region showed homology (78 to 79%) to the Saccharomyces cerevisiae TDH1 to TDH3 genes coding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and their amino acid sequences showed 76% identity; thus, this gene has been named C. albicans TDH1. A rabbit polyclonal antiserum against the purified cytosolic C. albicans GAPDH (polyclonal antibody [PAb] anti-CA-GAPDH) was used to identify the GAPDH in the ␤-mercaptoethanol extracts containing cell wall moieties. Indirect immunofluorescence demonstrated the presence of GAPDH at the C. albicans cell surface, particularly on the blastoconidia. Semiquantitative flow cytometry analysis showed the sensitivity of this GAPDH form to trypsin and its resistance to be removed with 2 M NaCl or 2% sodium dodecyl sulfate. The decrease in fluorescence in the presence of soluble GAPDH indicates the specificity of the labelling. In addition, a dose-dependent GAPDH enzymatic activity was detected in intact blastoconidia and germ tube cells. This activity was reduced by pretreatment of the cells with trypsin, formaldehyde, and PAb anti-CA-GAPDH. These observations indicate that an immunogenic, enzymatically active cell wall-associated form of the glycolytic enzyme GAPDH is found at the cell surface of C. albicans cells.

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“…Antibodies against the surface GAPDH of S. mansoni have been associated with human resistance to schistosomiasis (Argiro et al, 2000;Charrier-Ferrara et al, 1992;Goudot-Crozel et al, 1989). In group A streptococci and in Staphylococcus aureus a cell surface GAPDH is involved in the interaction with host cells and ligands (Modun and Williams, 1999;Fischetti, 1992, 1997;Taylor and Heinrichs, 2002;Winram and Lottenberg, 1996). Also, eukaryotic microorganisms contain a cell wall-associated GAPDH; in Kluyveromyces marxianus cellular flocculation depends on the expression of a cell surface GAPDH (Falcao Moreira et al, 1998Fernandes et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Candida albicans TDH3 gene promotes secretion of internal invertase when expressed in Saccharomyces cerevisiae as a glyceraldehyde‐3‐phosphate dehydrogenase‐invertase fusion protein

Delgado

Gil

Gozalbo

2003

Yeast

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We have checked the ability of the Candida albicans GAPDH polypeptide, which lacks a conventional N-terminal signal peptide, to reach the cell wall in Saccharomyces cerevisiae by using an intracellular form of the yeast invertase as a reporter protein.A hybrid TDH3-SUC2 gene containing the C. albicans TDH3 promoter sequences and a coding region encoding a fusion protein formed by the C. albicans GAPDH polypeptide, fused at its C-terminus with the yeast internal invertase, was constructed in a centromer derivative plasmid and transformed into a Suc − S. cerevisiae strain. Transformants displayed invertase activity measured in intact whole cells, and were able to grow on sucrose as the sole fermentable carbon source. Northern blot analysis with both TDH3 and SUC2 probes detected a single mRNA species of the expected size (about 2.7 kb), and Western immunoblot analysis of cell-free extracts, using a monoclonal antibody (mAb49) against a C. albicans GAPDH epitope, showed the presence of a 90 kDa polypeptide corresponding to the GAPDH-invertase fusion protein. This indicates that the TDH3 gene is able to direct part of the encoded gene product to the cell wall, and that any putative motifs for this targeting should be within the GAPDH amino acid sequence. Further analysis, using the same approach, of a panel of seven N-and C-terminal GAPDH truncates revealed that the region required for the cell wall targeting is located within the N-terminal half of the protein.

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The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase

Cited by 156 publications

References 30 publications

The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall proteins

The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall proteins

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

Candida albicans TDH3 gene promotes secretion of internal invertase when expressed in Saccharomyces cerevisiae as a glyceraldehyde‐3‐phosphate dehydrogenase‐invertase fusion protein

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