Search results for "Cell wall"

The Candida albicans cell wall-associated glyceraldehyde-3-phosphate dehydrogenase activity increases in response to starvation and temperature upshi…

2002

We have determined the effect of environmental factors (mild thermal upshift and starvation) on the Candida albicans cell wall-associated glyceraldehyde-3-phosphate dehydrogenase (cwGAPDH) activity. Temperature upshift (from 28 to 37 degrees C) and/ or starvation (at 28 or 37 degrees C in water) of exponentially growing yeast cells caused an increase in cwGAPDH activity (3 to 5-, and 7 to 8-fold, respectively). This increase in activity did not correlate with an increase in the amount of cwGAPDH protein present, as determined by flow cytometry, immunoelectron microscopy and Western-blotting. These results indicate that thermal upshift and starvation cause an activation of the cwGAPDH in C. …

Possible Roles of Mannoproteins in the Construction of Candida Albicans Cell Wall

1993

The shape of Candida albicans cells depends on their cell walls and some of their mannoproteins may act as modulators of the final molecular architecture. If that were the case, the wall mannoproteins might form part of what could be called a “morphogenetic code”.

α-L-rhamnosidases: Old and New Insights

2007

L-Rhamnose is a component of plant cell wall pectic polysaccharides (Mutter et al., 1994; Ridley et al., 2001), glycoproteins (Haruko and Haruko, 1999) and secondary metabolites such as anthocyanins (Renault et al., 1997), flavonoids (Bar-Peled et al., 1991) and triterpenoids (Friedman and McDonald, 1997). It has also been found in bacterial heteropolysaccharides (Hashimoto and Murata, 1998), rhamnolipids (Ochsner et al., 1994) and in the repeating units of the O-antigen structure of the lipopolysaccharide component of bacterial outer membranes (Chua et al., 1999). Some rhamnosides are important bioactive compounds, e.g. cytotoxic saponins (Bader et al., 1998; Yu et al., 2002), antifungal p…

Patterns of wall synthesis inSaccharomyces cerevisiae

1979

Wall formation inSaccharomyces cerevisiae seems to be the result of two main patterns of wall material deposition: (i) around the whole periphery of the cell in nonbudding ones, and (ii) mainly at the tip of the daughter cell or at the cross wall that separates dividing cells. This interpretation has been obtained following experiments in which RNA or protein synthesis has been inhibited. Under these conditions, glucan formation takes place, and wall thickening is probably due to the accumulation of this polysaccharide. Furthermore, once a pattern of wall deposition has been established, it is not modified by inhibition of RNA or protein synthesis.

Relationships Between Dimorphism, Cell Wall Structure, and Surface Activities in Candida albicans

1991

Most cells are covered with a complex network of interacting molecules that form the extracellular matrix. These molecules (proteins and polysaccharides) are secreted locally and interact among themselves to form an organized structure outside the cell plasma membrane. In unicellular eukaryotic organisms and plant cells, this structure is reinforced to withstand osmotic changes in the external environment, giving rise to the so-called cell wall.

Role of glycosylation in the incorporation of intrinsic mannoproteins into cell walls of Saccharomyces cerevisiae.

1989

Cell wall mannoproteins from Saccharomyces cerevisiae are completely or partially incorporated into their final location when N-glycosylation is inhibited by tunicamycin. These include a 90–100 kDa species still containing O-linked oligomannose chains, derived from a N-glycosylated material larger than 120 kDa; and a 30.5 kDa peptide lacking mannose residues, derived from a 33 kDa species. For both species, the growth temperature influences the level of incorporation of the non N-glycosylated molecules. Secretion of the peptides lacking N-linked saccharide chains follows the route defined by sec mutants.

Translational fusion to the Pir4 cell wall protein as a general and efficient method for cell surface immobilization or growth medium secretion of re…

2008

Synthesis and Assembly of Wall Polymers on Regenerating Yeast Protoplasts

1983

Accumulation of chitin and glucan on S. cerevisiae and C. albicans protoplasts begins shortly after resuspension in the regeneration medium, and mannoprotein molecules also appear retained by the regenerating wall after 30–60 minutes in S. cerevisiae or after a longer lag period in C. albicans. Nevertheless, a considerable fraction of the synthesized mannoproteins, which in SDS-acrylamide gels exhibit a different pattern from that of wall mannoproteins of cells, are still released to the growth medium during at least eight hours. De novo synthesis of chitin synthase, but not of glucan synthase, is observed in S. cerevisiae from about 30 minutes after initiation of the regeneration process. …

Chitin: A Structural Biopolysaccharide

2009

Chitin is a naturally occurring fibre-forming polymer that plays a protective role in many lower eukaryotes similar to that of cellulose in plants. Chemically it is a long-chain unbranched polysaccharide made of N-acetylglucosamine residues; it is the second most abundant organic compound in nature, after cellulose. Taking into account the structural role played by chitin, its metabolism (synthesis and degradation) is essential for different morphogenetic events. Absent in vertebrates and plants, chitin represents a parasite-specific target for chemotherapeutic attack and also plays a role in host immune responses. Because of its abundance in nature and its properties, biotechnological appl…

Wall mannoproteins of the yeast and mycelial cells of Candida albicans: nature of the glycosidic bonds and polydispersity of their mannan moieties.

1988

SUMMARY: Zymolyase released between 20 and 25% of the total protein from purified walls of yeast (Y) and mycelial (M) cells of Candida albicans. The material released contained 92% carbohydrate (86% mannose and 6% glucose) and 7:< protein. Over 85% of the carbohydrate was N-glycosidically linked to the protein and the rest (less than 15%) was linked O-glycosidically. Highly polydisperse, high molecular mass mannoproteins, resolved by electrophoresis as four defined bands in Y cells and two bands in M cells, had both types of sugar chains. A 34 kDa species found in both types of cells had a single 2.5 kDa N-glycosidically linked sugar chain and a 3 1.5 kDa protein moiety. Polydispersity in t…