scholarly journals Length Specificity and Polymerization Mechanism of (1,3)-β-d-Glucan Synthase in Fungal Cell Wall Biosynthesis

Biochemistry ◽  
2020 ◽  
Vol 59 (5) ◽  
pp. 682-693 ◽  
Author(s):  
Abhishek Chhetri ◽  
Anna Loksztejn ◽  
Hai Nguyen ◽  
Kaila M. Pianalto ◽  
Mi Jung Kim ◽  
...  
Keyword(s):  
Cell Wall ◽  
Fungal Cell Wall ◽  
Cell Wall Biosynthesis ◽  
Fungal Cell ◽  
Glucan Synthase ◽  
Polymerization Mechanism

scholarly journals Protein Kinase A and High-Osmolarity Glycerol Response Pathways Cooperatively Control Cell Wall Carbohydrate Mobilization inAspergillus fumigatus

mBio ◽  
2018 ◽  
Vol 9 (6) ◽  
Author(s):  
Leandro José de Assis ◽  
Adriana Manfiolli ◽  
Eliciane Mattos ◽  
João H. T. Marilhano Fabri ◽  
Iran Malavazi ◽  
...  
Keyword(s):  
Cell Wall ◽  
Protein Kinase ◽  
Glycogen Synthesis ◽  
Fungal Cell Wall ◽  
Cell Wall Biosynthesis ◽  
Fungal Cell ◽  
Content Type ◽  
High Osmolarity ◽  
High Osmolarity Glycerol ◽  
Kinase A

ABSTRACTAspergillus fumigatusmitogen-activated protein kinases (MAPKs) are involved in maintaining the normal morphology of the cell wall and providing resistance against cell wall-damaging agents. Upon cell wall stress, cell wall-related sugars need to be synthesized from carbohydrate storage compounds. Here we show that this process is dependent on cAMP-dependent protein kinase A (PKA) activity and regulated by the high-osmolarity glycerol response (HOG) MAPKs SakA and MpkC. These protein kinases are necessary for normal accumulation/degradation of trehalose and glycogen, and the lack of these genes reduces glucose uptake and glycogen synthesis. Alterations in glycogen synthesis were observed for thesakAandmpkCdeletion mutants, which also displayed alterations in carbohydrate exposure on the cell wall. Carbohydrate mobilization is controlled by SakA interaction with PkaC1 and PkaR, suggesting a putative mechanism where the PkaR regulatory subunit leaves the complex and releases the SakA-PkaC1 complex for activation of enzymes involved in carbohydrate mobilization. This work reveals the communication between the HOG and PKA pathways for carbohydrate mobilization for cell wall construction.IMPORTANCEAspergillus fumigatusis an opportunistic human pathogen causing allergic reactions or systemic infections such as invasive pulmonary aspergillosis, especially in immunocompromised patients. The fungal cell wall is the main component responsible for recognition by the immune system, due to the specific composition of polysaccharide carbohydrates exposed on the surface of the fungal cell wall called pathogen-associated molecular patterns (PAMPs). Key enzymes in the fungal cell wall biosynthesis are a good target for fungal drug development. This report elucidates the cooperation between the HOG and PKA pathways in the mobilization of carbohydrates for fungal cell wall biosynthesis. We suggest that the reduced mobilization of simple sugars causes defects in the structure of the fungal cell wall. In summary, we propose that SakA is important for PKA activity, therefore regulating the availability and mobilization of monosaccharides for fungal cell wall biosynthesis during cell wall damage and the osmotic stress response.

Fungal cell wall biosynthesis: a view on biodiversity in fungi and application of ‘-omics’

Yeast ◽  
2007 ◽  
Vol 24 (4) ◽  
pp. 217-219 ◽  
Author(s):  
Sabine Strahl ◽  
Jürgen J. Heinisch
Keyword(s):  
Cell Wall ◽  
Fungal Cell Wall ◽  
Cell Wall Biosynthesis ◽  
Fungal Cell

scholarly journals A Novel Screening Method for Cell Wall Mutants in Aspergillus niger Identifies UDP-Galactopyranose Mutase as an Important Protein in Fungal Cell Wall Biosynthesis

Genetics ◽  
2008 ◽  
Vol 178 (2) ◽  
pp. 873-881 ◽  
Author(s):  
Robbert A. Damveld ◽  
Angelique Franken ◽  
Mark Arentshorst ◽  
Peter J. Punt ◽  
Frans M. Klis ◽  
...  
Keyword(s):  
Cell Wall ◽  
Aspergillus Niger ◽  
Screening Method ◽  
Fungal Cell Wall ◽  
Cell Wall Biosynthesis ◽  
Fungal Cell ◽  
Important Protein

The structure of neopeptins, inhibitors of fungal cell wall biosynthesis

1984 ◽  
Vol 25 (4) ◽  
pp. 423-426 ◽  
Author(s):  
Makoto Ubukata ◽  
Masakazu Uramoto ◽  
Kiyoshi Isono
Keyword(s):  
Cell Wall ◽  
Fungal Cell Wall ◽  
Cell Wall Biosynthesis ◽  
Fungal Cell

ChemInform Abstract: Novel Nikkomycin Analogues: Inhibitors of the Fungal Cell Wall Biosynthesis Enzyme Chitin Synthase.

ChemInform ◽  
2000 ◽  
Vol 31 (41) ◽  
pp. no-no
Author(s):  
Kikoh Obi ◽  
Jun-ichiro Uda ◽  
Kazuhiko Iwase ◽  
Osamu Sugimoto ◽  
Hiroyuki Ebisu ◽  
...  
Keyword(s):  
Cell Wall ◽  
Fungal Cell Wall ◽  
Chitin Synthase ◽  
Cell Wall Biosynthesis ◽  
Fungal Cell

scholarly journals Preliminary Structural Elucidation of β-(1,3)-glucan Synthase from Candida glabrata Using Cryo-Electron Tomography

2021 ◽  
Vol 7 (2) ◽  
pp. 120
Author(s):  
Cristina Jiménez-Ortigosa ◽  
Jennifer Jiang ◽  
Muyuan Chen ◽  
Xuyuan Kuang ◽  
Kelley R. Healey ◽  
...  
Keyword(s):  
Cell Wall ◽  
Candida Glabrata ◽  
Structural Information ◽  
Electron Tomography ◽  
Fungal Cell Wall ◽  
Therapeutic Drug ◽  
Candida Spp ◽  
Fungal Cell ◽  
Glucan Synthase ◽  
Cryo Electron Tomography

Echinocandin drugs have become a front-line therapy against Candida spp. infections due to the increased incidence of infections by species with elevated azole resistance, such as Candida glabrata. Echinocandins target the fungal-specific enzyme ß-(1,3)-glucan synthase (GS), which is located in the plasma membrane and catalyzes the biosynthesis of ß-(1,3)-glucan, the major component of the fungal cell wall. However, resistance to echinocandin drugs, which results from hotspot mutations in the catalytic subunits of GS, is an emerging problem. Little structural information on GS is currently available because, thus far, the GS enzyme complex has resisted homogenous purification, limiting our understanding of GS as a major biosynthetic apparatus for cell wall assembly and an important therapeutic drug target. Here, by applying cryo-electron tomography (cryo-ET) and subtomogram analysis, we provide a preliminary structure of the putative C. glabrata GS complex as clusters of hexamers, each subunit with two notable cytosolic domains, the N-terminal and central catalytic domains. This study lays the foundation for structural and functional studies of this elusive protein complex, which will provide insight into fungal cell wall synthesis and the development of more efficacious antifungal therapeutics.

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