The 946;-1,3-glucanase ENG families of Aspergillus fumigatus are important for conidial cell wall morphogenesis

Ref ID: 19540

Author:

I Mouyna1*, L Hartl1,2, V Aimanianda1, L Muszkieta1, JP Latgé1

Author address:

1Aspergillus, Pasteur Institut, Paris, France
2Microsynth Austria GmbH, Vienna, Autriche

Full conference title:

6th Advances Against Aspergillosis 2014

Abstract:

Purpose:
Beta-1,3-glucan is produced by a variety of different organisms ranging from prokaryotes to
higher plants. In fungi it constitutes a major cell wall component being responsible for rigidity
of the cell wall structure. Softening of the cell wall is absolutely required during morphogenetic
events like germination and branching and would be under the dependence of cell wall specific
glycosylhydrolases such as endo-beta-1,3-glucanases and chitinases. We investigated a survey of all
potential endo-β -1,3-glucanases found in the A. fumigatus genome.
Methods:
Different fungal and bacterial glucanases were used as protein queries for BLAST searches to
identify possible homologs in the genome of the A. fumigatus strains Af293.
Results:
We have identified eight genes coding for potential endo-beta-1,3-glucanases that belongs
to 2 families. ENGL1 belongs to the family GH81 while ENG2 to ENG8 are GH16 hydrolytic
enzymes. While ENGL1 and ENG2 have already been cloned and characterised, here we report the
construction of the quadruple deletion strain Afeng2-5 depleted of four GH16_MLG1_glucanases.
All four genes were expressed in the wild-type strain during germination and also at later timepoints.
Additionally all four corresponding proteins are localised close to the cell wall. Eng2 is
bound to the plasma membrane by a GPI anchor, Eng4 and Eng5 by a transmembrane helix and
Eng3 is secreted, allowing it direct contact with cell wall glucans.
Conclusion:
The quadruple mutant showed fragile conidia. As there is still glucanases activities in the quadruple
mutant, the quintuple Afengl1/eng2-5 is currently constructed.

Abstract Number: 67

Conference Year: 2014

Link to conference website: http://www.AAA2014.org

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