How a fungus escapes the water to grow into the air

  title={How a fungus escapes the water to grow into the air},
  author={Han A. B. W{\"o}sten and M. A. van Wetter and Luis G Lugones and Henny C. Mei and Henk J. Busscher and Joseph G. H. Wessels},
  journal={Current Biology},

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Surface-active proteins enable microbial aerial hyphae to grow into the air.

Although filamentous bacteria and filamentous fungi belong to different kingdoms that diverged early in evolution, they adopted similar life styles and both groups form aerial structures from which (a)sexual spores can develop.

Hydrophobin Rodlets on the Fungal Cell Wall.

The conidia of airborne fungi are protected by a hydrophobic protein layer that coats the cell wall polysaccharides and renders the spores resistant to wetting and desiccation, aiding host interactions in symbiotic relationships and increasing infectivity in pathogenic fungi.

Structural proteins involved in emergence of microbial aerial hyphae.

Although the erection of aerial hyphae in both filamentous fungi and filamentous bacteria is dependent upon (poly)peptides that are structurally unrelated, they can, at least partially, functionally substitute for each other.

An extracellular matrix glues together the aerial‐grown hyphae of Aspergillus fumigatus

This is the first analysis of the three dimensional structure of a mycelial colony, and knowledge of this multicellular organization will impact the future understanding of the pathobiology of aerial mold pathogens.

Hydrophobins in wood biology and biotechnology

The obtained results indicate that neither the SC3 hydrophobin nor the SC15 protein are principally necessary for S. commune to enter into the wood, to decay the wood or to affect the strength to the wood.

The fungal hydrophobin RolA recruits polyesterase and laterally moves on hydrophobic surfaces

Results suggest that RolA adsorbed to the hydrophobic surface of PBSA recruits CutL 1, resulting in condensation of CutL1 on the PBSA surface and consequent stimulation ofPBSA hydrolysis.

The pleiotropic functions of intracellular hydrophobins in aerial hyphae and fungal spores

It is revealed that at least one HFB, HFB4 in T. guizhouense, is produced and secreted by wetted spores and it is shown that this protein possibly controls spore dormancy and contributes to the water sensing mechanism required for the detection of germination conditions.

Self-assembly of hydrophobin proteins from the fungus Trichoderma reesei

The surfactant-like properties of hydrophobins from Trichoderma reesei were studied at the air-water interface, at solid surfaces, and in solution, and it was shown that the surface activity of HFBI is not directly dependent on the formation of multimers in solution.

Intracellular accumulation and secretion of hydrophobin-enriched vesicles aid the rapid sporulation of molds

A distinctive HFB secretory pathway is revealed that includes an intracellular accumulation of HFBs in lipid bodies (LBs) that can internalize in vacuoles and contributes to the maintenance of turgor pressure required for the erection of sporogenic structures and rapid HFB secretion by squeezing out periplasmic VMSs through the cell wall.



Hydrophobins: proteins that change the nature of the fungal surface.

  • J. Wessels
  • Biology
    Advances in microbial physiology
  • 1997

Interfacial Self-Assembly of a Fungal Hydrophobin into a Hydrophobic Rodlet Layer.

It is proposed that the hydrophobic rodlet layer on aerial hyphae arises by interfacial self-assembly of Sc3p hydrophobin monomers, involving noncovalent interactions only.

A surface active protein involved in aerial hyphae formation in the filamentous fungus Schizophillum commune restores the capacity of a bald mutant of the filamentous bacterium Streptomyces coelicolor to erect aerial structures

It is concluded that the production of SapB and streptofactin at the start of morphological differentiation contributes to the erection of aerial hyphae by decreasing the surface tension at the colony surface but that subsequent morphogenesis requires additional developmentally regulated events under the control of bald genes.

The fungal hydrophobin Sc3p self-assembles at the surface of aerial hyphae as a protein membrane constituting the hydrophobic rodlet layer.

The Schizophyllum commune hydrophobin Sc3p is a small, hydrophobic, cysteine-rich protein involved in the formation of aerial hyphae that self-assembles at the wall/air interface into an SDS-insoluble protein membrane, at the aerial site very hydrophilic and with the appearance of a mosaic of 10 nm spaced parallel rodlets.

Streptofactin, a novel biosurfactant with aerial mycelium inducing activity from Streptomyces tendae Tü 901/8c

The properties of streptofactin suggest that it plays a structural role in aerial mycelium development and supports the erection of aerial hyphae by lowering the surface tension of water films enclosing the colonies.

Interfacial self‐assembly of a hydrophobin into an amphipathic protein membrane mediates fungal attachment to hydrophobic surfaces.

Findings indicate that hydrophobins, in addition to forming hydrophobic wall coatings, play a role in adherence of fungal hyphae to hydrophilic surfaces.

A hydrophobin (ABH3) specifically secreted by vegetatively growing hyphae of Agaricus bisporus (common white button mushroom).

Using an S. commune mutant with a disrupted SC3 gene it was found that ABH3 can substitute for SC3 in inducing formation of aerial hyphae, suggesting a role ofABH3 in the emergence of aerial Hyphae and strands in A. bisporus.

Effect of a virus on accumulation of a tissue-specific cell-surface protein of the fungus Cryphonectria (Endothia) parasitica.

The striking similarities between the physical properties and locations of accumulation of cryparin and cerato-ulmin in fungal fruiting structures suggest either conservation of structure or convergent evolution in function of these two proteins.