Neocallimastigomycota
Neocallimastigomycota | |
---|---|
Scientific classification | |
Domain: | Eukaryota |
Kingdom: | Fungi |
Division: | Neocallimastigomycota M.J. Powell 2007[2] |
Class: | Neocallimastigomycetes M.J. Powell 2007[2] |
Order: | Neocallimastigales J.L. Li, I.B. Heath & L. Packer[1] |
Family: | Neocallimastigaceae |
Type genus | |
Neocallimastix (I.B. Heath 1983) Vavra & Joyon
| |
Genera | |
Aestipascuomyces |
Neocallimastigomycota is a phylum containing anaerobic fungi, which are symbionts found in the digestive tracts of larger herbivores. Anaerobic fungi were originally placed within phylum Chytridiomycota, within Order Neocallimastigales but later raised to phylum level,[3] a decision upheld by later phylogenetic reconstructions.[4] It encompasses only one family.[3]
Discovery
The fungi in Neocallimastigomycota were first recognised as fungi by Orpin in 1975,
Neocallimastigomycota have also been found in humans.[9]
Circumscription
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Reproduction and growth
These fungi reproduce in the rumen of ruminants through the formation of zoospores which are released from sporangia. These zoospores bear a kinetosome but lack the nonflagellated centriole known in most chytrids,[2] and have been known to utilize horizontal gene transfer in their development of xylanase (from bacteria) and other glucanases.[10]
The
Metabolism
Neocallimastigomycota lack
Polysaccharide-degrading activity
Neocallimastigomycota play an essential role in fibre-digestion in their host species. They are present in large numbers in the digestive tracts of animals which are fed on high fibre diets.[13] The polysaccharide degrading enzymes produced by anaerobic fungi can hydrolyse the most recalcitrant plant polymers and can degrade unlignified plant cell walls entirely.[14][15] Orpinomyces sp. exhibited the capacity of xylanase, CMCase, lichenase, amylase, β-xylosidase, β-glucosidase, α-Larabinofuranosidase and minor amounts of β-cellobiosidase production by utilizing avicel as the sole energy source.[16] The polysaccharide degrading enzymes are organised into a multiprotein complex, similar to the bacterial cellulosome.[17]
Spelling of name
The Greek termination, "-mastix", referring to "whips", i.e. the many
References
- S2CID 83723423.
- ^ S2CID 4686378.
- ^ S2CID 4686378.
- ISSN 1560-2745.
- PMID 1462.
- PMID 864435.
- S2CID 20006974.
- S2CID 25961316.
- PMID 26455903.
- ^ ISBN 0-471-52229-5
- ISSN 0168-6496.
- PMID 10719208.
- JSTOR 3760810.
- PMID 2178175.
- PMID 16887555.
- S2CID 21167921.
- .
- ^ combform3.qxd Archived 2007-03-15 at the Wayback Machine
- ^ "Suprafamilial Names". Archived from the original on 2007-02-22. Retrieved 2007-03-26.
External links
- Neocallimastigomycota at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- The Anaerobic Fungi Network