Disease relevance of CWP2

• Here bacterial carboxylesterase EstA from Burkholderia gladioli was covalently anchored into the cell wall of Saccharomyces cerevisiae by in-frame fusion to the endogenous yeast proteins Kre1p, Cwp2p, and Flo1p [1].

High impact information on CWP2

• Tip1p was found only in mother cells, whereas Cwp2p was incorporated in small-to-medium-sized buds [2].
• However, the plasma membrane protein Gas1p still receives its glycosyl-phosphatidylinositol anchor in pmt1 cells, and in this mutant strain an alpha-galactosidase-Cwp2 fusion protein was found linked to the cell wall but devoid of beta1,6-glucan side-chain, indicating an alternative mechanism of cell wall anchorage [3].
• Reciprocally, GST fused to EBNA-LPR1 or EBNA-LPR2 pulled down hERR1 transiently expressed in COS-7 cells [4].
• Finally, in yeast mutants with impaired cell wall structure, expression of both CWP1 and CWP2 was modified [5].
• Here we show that of the single cell wall protein knockouts, a Cwp2p-deficient mutant is most sensitive to nisin [5].

Biological context of CWP2

• To begin to understand why sphingolipids seem to be necessary for coping with low-pH stress, we screened a genomic library and selected a suppressor gene, CWP2 (cell wall protein 2), that when present in multiple copies partially compensates for the lack of sphingolipids and enhances survival at low pH [6].
• Attempts to clone the LPR suppressor gene were not successful, but they led to the isolation of the CWP2 gene, which encodes a major mannoprotein component of the outer cell wall [7].
• Dominant suppressor mutation bypasses the sphingolipid requirement for growth of Saccharomyces cells at low pH: role of the CWP2 gene [7].
• In contrast, the cells were most resistant to nisin after a peak in expression of the mRNA of cell wall protein 2 (Cwp2p), which coincided with the G2 phase of the cell cycle [5].

Anatomical context of CWP2

• Kic1-deficient cells also became highly resistant to the cell wall-degrading enzyme mixture Zymolyase, and exhibited higher transcript levels of the cell wall protein-encoding genes CWP2 and SED1 [8].

Associations of CWP2 with chemical compounds

• The cwp2 deletion mutant displayed an increased sensitivity to Congo red, calcofluor white, and Zymolyase [9].
• Four were full phenotypic revertants showing both low pH resistance and hygromycin B sensitivity [10].

Other interactions of CWP2

• Depletion of Cwp1p or Tip1p also caused increased sensitivities to Congo red and calcofluor white, but the effects were less pronounced than for cwp2 delta [9].
• A 80-kDa mannoprotein was identified as the product of the TIP1 gene, and a 180-kDa mannoprotein corresponded to the product of the ORF YKL444, which we named CWP2 [9].
• The highest proportion of cell wall incorporation was achieved with Cwp2p, Ag alpha 1p, or Sed1p as an anchor [11].
• Neither the number of positive cells within the population nor the distribution of the fusion at the single-cell level were negatively affected by replacing the "heterologous" Kre1p leader by the "native" Cwp2p leader [12].

Analytical, diagnostic and therapeutic context of CWP2

• Western analysis of a yeast strain producing c-myc epitope tagged Cwp2p revealed that this protein is only detectable if fatty acid chains are present on the protein, indicating that the lack of recognition of Cwp2p by an anti beta-1,6-glucan antiserum is caused by a blotting artefact of the mature protein [13].

References