Protein O-mannosylation affects protein secretion, cell wall integrity and morphogenesis in Trichoderma reesei

2020 ◽  
Vol 144 ◽  
pp. 103440 ◽  
Author(s):  
Guangya Zhao ◽  
Yueqiang Xu ◽  
Haomiao Ouyang ◽  
Yuanming Luo ◽  
Shutao Sun ◽  
...  
Keyword(s):  
Cell Wall ◽  
Trichoderma Reesei ◽  
Protein Secretion ◽  
Cell Wall Integrity

scholarly journals Introduction of the Aspergillus fumigatus α-1,2-mannosidase MsdS into Trichoderma reesei leads to abnormal polarity and improves the ligno-cellulose degradation

2020 ◽  
Author(s):  
Prakriti Sharma Ghimire ◽  
Haomiao Ouyang ◽  
Guangya Zhao ◽  
Mingming Xie ◽  
Hui Zhou ◽  
...  
Keyword(s):  
Cell Wall ◽  
Aspergillus Fumigatus ◽  
Trichoderma Reesei ◽  
Protein Secretion ◽  
Cellulose Degradation ◽  
Fungal Cell ◽  
Wall Defect ◽  
New Strategy ◽  
Species Specific ◽  
First Time

ABSTRACTα-1,2-Mannosidase is an important enzyme essential for N-glycan processing and plays a significant role in the biosynthesis and organization of fungal cell wall. Lacking of α-1,2-mannosidase leads to cell wall defect in yeast and filamentous fungi. Trichoderma reesei is known to be non-toxic to human, and its N-glycan on secreted glycoprotein is Man8GlcNAc2. To evaluate the significance of the N-glycan processing in T. reesei, in this study Aspergillus fumigatus α-1, 2-mannosidase MsdS, an enzyme that cleaves N-linked Man8GlcNAc2 in Golgi to produce Man6GlcNAc2 on secreted glycoprotein, was introduced into T. reesei. The msdS-expressing strain Tr-MsdS produced a major glycoform of Man6GlcNAc2 on its secreted glycoproteins, instead of Man8GlcNAc2 in the parent strain. Although the cell wall content of msdS-expressing strain Tr-MsdS was changed, it appeared that the cell wall integrity was not affected. However, phenotypes such as increased conidiation, multiple budding and random branching were observed in strain Tr-MsdS. In addition, expression of MsdS into T. ressei also affected protein secretion and improved the ligno-cellulose degradation of T. reesei. Our results indicate that processing of the N-glycan is species-specific and plays an important role in protein secretion in T. reesei, specially cellulases. Also, our results provide a new strategy to improve cellulases production by interfering the N-glycan processing in T. reesei.ImportanceFor the first time, the N-glycan processing is shown to play an important role in polarized growth and protein secretion in T. reesei. In addition, our results show that alterated N-glycan processing enhances cellulose degradation, which provides a strategy to improve cellulases production in T. reesei.

scholarly journals Introduction of the Aspergillus fumigatus α-1,2-mannosidase MsdS into Trichoderma reesei improves the ligno-cellulose degradation

2020 ◽  
Author(s):  
Prakriti Sharma Ghimire ◽  
Haomiao Ouyang ◽  
Guangya Zhao ◽  
Mingming Xie ◽  
Hui Zhou ◽  
...  
Keyword(s):  
Cell Wall ◽  
Aspergillus Fumigatus ◽  
Trichoderma Reesei ◽  
Protein Secretion ◽  
Cellulose Degradation ◽  
Fungal Cell ◽  
Wall Defect ◽  
New Strategy ◽  
Species Specific ◽  
Important Enzyme

Abstract Background: a-1,2-Mannosidase is an important enzyme essential for N-glycan processing and plays a significant role in the biosynthesis and organization of fungal cell wall. Lacking of α-1,2-mannosidase leads to cell wall defect in yeast and filamentous fungi. In Trichoderma reesei, a fungus known to be non-toxic to human, its N-glycan on secreted glycoprotein is Man8GlcNAc2, which is different from that in Aspergillus fumigatus. To evaluate the significance of the N-glycan processing in T. reesei, in this study A. fumigatus α-1, 2-mannosidase MsdS, an enzyme that cleaves N-linked Man8GlcNAc2 in Golgi to produce Man6GlcNAc2 on secreted glycoprotein, was introduced into T. reesei.Results: The msdS-expressing strain Tr-MsdS produced a major glycoform of Man6GlcNAc2 on its secreted glycoproteins, instead of Man8GlcNAc2 in the parent strain. Although the cell wall content of msdS-expressing strain Tr-MsdS was changed, it appeared that the cell wall integrity was not affected. However, phenotypes such as increased conidiation, multiple budding and random branching were observed in strain Tr-MsdS. In addition, expression of MsdS into T. ressei also affected protein secretion and improved the ligno-cellulose degradation of T. reesei.Conclusions: Our results indicate that processing of the N-glycan is species-specific and plays an important role in protein secretion in T. reesei, specially cellulases. Also, our results provide a new strategy to improve cellulases production by interfering the N-glycan processing in T. reesei.

scholarly journals Disruption of the ESX-5 system of Mycobacterium tuberculosis causes loss of PPE protein secretion, reduction of cell wall integrity and strong attenuation

2012 ◽  
Vol 83 (6) ◽  
pp. 1195-1209 ◽  
Author(s):  
Daria Bottai ◽  
Mariagrazia Di Luca ◽  
Laleh Majlessi ◽  
Wafa Frigui ◽  
Roxane Simeone ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Protein Secretion ◽  
Cell Wall Integrity

The Regulatory Function of the Molecular Chaperone Hsp90 in the Cell Wall Integrity of Pathogenic Fungi

2018 ◽  
Vol 16 (1) ◽  
pp. 44-53
Author(s):  
Marina Campos Rocha ◽  
Camilla Alves Santos ◽  
Iran Malavazi
Keyword(s):  
Cell Wall ◽  
Antifungal Therapy ◽  
Molecular Chaperone ◽  
Regulatory Protein ◽  
Pathogenic Fungi ◽  
Antifungal Drugs ◽  
Cell Wall Integrity ◽  
Regulatory Function ◽  
Loss Of Function ◽  
Hsp90 Inhibition

Different signaling cascades including the Cell Wall Integrity (CWI), the High Osmolarity Glycerol (HOG) and the Ca2+/calcineurin pathways control the cell wall biosynthesis and remodeling in fungi. Pathogenic fungi, such as Aspergillus fumigatus and Candida albicans, greatly rely on these signaling circuits to cope with different sources of stress, including the cell wall stress evoked by antifungal drugs and the host’s response during infection. Hsp90 has been proposed as an important regulatory protein and an attractive target for antifungal therapy since it stabilizes major effector proteins that act in the CWI, HOG and Ca2+/calcineurin pathways. Data from the human pathogen C. albicans have provided solid evidence that loss-of-function of Hsp90 impairs the evolution of resistance to azoles and echinocandin drugs. In A. fumigatus, Hsp90 is also required for cell wall integrity maintenance, reinforcing a coordinated function of the CWI pathway and this essential molecular chaperone. In this review, we focus on the current information about how Hsp90 impacts the aforementioned signaling pathways and consequently the homeostasis and maintenance of the cell wall, highlighting this cellular event as a key mechanism underlying antifungal therapy based on Hsp90 inhibition.

scholarly journals Yeast Nap1-Binding Protein Nbp2p Is Required for Mitotic Growth at High Temperatures and for Cell Wall Integrity

Genetics ◽  
2003 ◽  
Vol 165 (2) ◽  
pp. 517-529
Author(s):  
Kentaro Ohkuni ◽  
Asuko Okuda ◽  
Akihiko Kikuchi
Keyword(s):  
Cell Death ◽  
Cell Wall ◽  
High Temperature ◽  
High Temperatures ◽  
Hybrid System ◽  
Mapk Pathway ◽  
Binding Protein ◽  
Cell Wall Integrity ◽  
Calcofluor White ◽  
Two Hybrid

AbstractNbp2p is a Nap1-binding protein in Saccharomyces cerevisiae identified by its interaction with Nap1 by a two-hybrid system. NBP2 encodes a novel protein consisting of 236 amino acids with a Src homology 3 (SH3) domain. We showed that NBP2 functions to promote mitotic cell growth at high temperatures and cell wall integrity. Loss of Nbp2 results in cell death at high temperatures and in sensitivity to calcofluor white. Cell death at high temperature is thought not to be due to a weakened cell wall. Additionally, we have isolated several type-2C serine threonine protein phosphatases (PTCs) as multicopy suppressors and MAP kinase-kinase (MAPKK), related to the yeast PKC MAPK pathway, as deletion suppressors of the nbp2Δ mutant. Screening for deletion suppressors is a new genetic approach to identify and characterize additional proteins in the Nbp2-dependent pathway. Genetic analyses suggested that Ptc1, which interacts with Nbp2 by the two-hybrid system, acts downstream of Nbp2 and that cells lacking the function of Nbp2 prefer to lose Mkk1, but the PKC MAPK pathway itself is indispensable when Nbp2 is deleted at high temperature.

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