One 2015 study by US scientists found that repeated drying and wetting may render soil bound prions less infectious, although this was dependent on the soil type they were bound to. Fungi
Proteins showing prion-type behavior are also found in some fungi, which has been useful in helping to understand mammalian prions. Fungal prions do not appear to cause disease in their hosts. In yeast, protein refolding to the prion configuration is assisted by chaperone proteins such as Hsp104. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. Amyloid aggregates are fibrils, growing at their ends, and replicate when breakage causes two growing ends to become four growing ends. The incubation period of prion diseases is determined by the exponential growth rate associated with prion replication, which is a balance between the linear growth and the breakage of aggregates.Fungal proteins exhibiting templated conformational change were discovered in the yeast Saccharomyces cerevisiae by Reed Wickner in the early 1990s. For their mechanistic similarity to mammalian prions, they were termed yeast prions. Subsequent to this, a prion has also been found in the fungus Podospora anserina. These prions behave similarly to PrP, but, in general, are nontoxic to their hosts.
Lichen spinulosus  is a rare skin disorder characterized by follicular keratotic papules that are grouped into large patches. It is a variant of keratosis pilaris named for its resemblance to a patch of lichen. See also
Hook nail
List of cutaneous conditions

Notes
References
Friedman S (1990). "Lichen spinulosus. Clinicopathologic review of thirty-five cases". J Am Acad Dermatol. 22 (2 Pt 1): 261–4. doi:10.1016/0190-9622(90)70035-G. PMID 2179296. External links
Derm Net NZ
Emedicine
Thehinhso