Fungi have evolved these small, adaptable proteins that polymerize
and facilitate life at interfaces. The remarkable hydrophobins
serve an amazingly broad range of functions in fungal
development and life cycle. Recent discoveries in their specific
biological roles, such as in host evasion, together with an
advancing understanding of their molecular structure and
mechanisms of assembly have opened up new and exciting avenues
of biotechnological and medical research based on modified
hydrophobins. These include the use of hydrophobins to
facilitate cell attachment, protein purification, and drug delivery.
However, some key questions remain. For instance, what
are the three-dimensional structure and molecular organization
of assembled hydrophobins? Will the structure tolerate
mixed hydrophobin assembly with multiple functionalities?
Are there other undiscovered biological roles given that only
relatively few hydrophobin proteins with different sequences
have been examined experimentally? What are the signals that
trigger spore germination? Can the same signals be used as
switches for hydrophobin-coated nanoparticles to release their
contents? It is likely that answering these questions, together
with improvements in large-scale hydrophobin production,
will allow the biotechnological potential of hydrophobins to be
fully exploited in the years to come.