Butyrivibrio
Butyrivibrio | |
---|---|
Scientific classification | |
Domain: | Bacteria |
Phylum: | Firmicutes |
Class: | Clostridia |
Order: | Clostridiales |
Family: | Lachnospiraceae |
Genus: | Butyrivibrio Bryant and Small (1956) |
Species | |
B. crossotus[1] |
Butyrivibrio is a genus of bacteria in Class Clostridia. Bacteria of this genus are common in the gastrointestinal systems of many animals. Genus Butyrivibrio was first described by Bryant and Small (1956) as anaerobic, butyric acid-producing, curved rods (or vibroids). Butyrivibrio cells are small, typically 0.4 – 0.6 µm by 2 – 5 µm. They are motile, using a single polar or subpolar monotrichous flagellum. They are commonly found singly or in short chains but it is not unusual for them to form long chains. Despite historically being described as Gram-negative,[2] their cell walls contain derivatives of teichoic acid,[3] and electron microscopy indicates that bacteria of this genus have a Gram-positive cell wall type.[3][4] It is thought that they appear Gram-negative when Gram stained because their cell walls thin to 12 to 18 nm as they reach stationary phase.[4]
Butyrivibrio species are common in the rumens of ruminant animals such as cows, deer and sheep, where they are involved in a number of ruminal functions of agricultural importance in addition to butyrate production.[5] These include fibre degradation, protein breakdown, biohydrogenation of lipids and the production of microbial inhibitors.[6][7][8][9][10] Of particular importance to ruminant digestion, and therefore productivity, is their contribution to the degradation of plant structural carbohydrates, principally hemicellulose.[9][11]
Butyrivibrio species are metabolically versatile and are able to ferment a wide range of sugars[12] and cellodextrins.[13] Some strains have been reported to break down cellulose,[14] although their ability to sustain growth on cellulose appears to be lost during in vitro culturing. Most isolates are amylolytic[15] and are able to degrade xylan by producing xylanolytic[16][17] and esterase enzymes.[18][19] The induction of xylanase enzymes varies between strains; in group D1 strains (49, H17c, 12) xylanase expression appears to be constitutively expressed, while groups B1 (113) and C (CF3) are induced only by growth on xylan, and those of group B2 are induced by growth on xylan or arabinose.[20]
A number of genes encoding glycoside hydrolases (GH) have been identified in Butyrivibrio species including endocellulase (GH family 5 and 9); β-Glucosidase (GH family 3); endoxylanase (GH family 10 and 11); β-Xylosidase (GH family 43); and α-Amylase (GH family 13) enzymes. Several carbohydrate binding modules (CBM) have also been identified that are predicted to bind glycogen (CBM family 48); xylan or chitin (CBM family 2); and starch (CBM family 26).[21][22]
The Butyrivibrio genus encompasses over 60 strains that were originally confined to the species Butyrivibrio fibrisolvens based on their phenotypic and metabolic characteristics. However, phylogenetic analyses based on 16S ribosomal RNA (rRNA) gene sequences has divided the genus Butyrivibrio into six families.[23] These families include the rumen isolates Butyrivibrio fibrisolvens, B. hungateii, B. proteoclasticus, Pseudobutyrivibrio xylanivorans, and P. ruminis and the human isolate B. crossotus. The families B. fibrisolvens, B. crossotus, B. hungateii as well as B. proteoclasticus all belong to the Clostridium sub-cluster XIVa.[24]
Butyrivibrio proteoclasticus B316T
Butyrivibrio proteoclasticus B316T was the first Butyrivibrio species to have its genome sequenced.[25] It was first isolated and described by Attwood et al. (1996),[26] and was originally assigned to the genus Clostridium based on its similarity to Clostridium aminophilum, a member of the Clostridium sub-cluster XIVa. Further analysis has shown that it is more appropriately placed within the genus Butyrivibrio and the organism was given its current name.[27] Within this genus its 16S rDNA sequence is most similar to, but distinct from, that of B. hungateii.
B. proteoclasticus is found in rumen contents at significant concentrations of from 2.01 x 106/ml to 3.12 x 107/mL as estimated by competitive PCR[28] or 2.2% to 9.4% of the total eubacterial DNA within the rumen, as estimated by real time PCR.[29] B. proteoclasticus cells are anaerobic, slightly curved rods, commonly found singly or in short chains, but it is not unusual for them to form long chains. They possess a single sub-terminal flagellum, but unlike other Butyrivibrio species, they are not motile. They are ultrastructurally Gram-positive, although as with all Butyrivibrio species, they stain Gram-negative[26]
B. proteoclasticus has been shown to have an important role in biohydrogenation, converting linoleic acid to stearic acid.[30]
References
- 1 2 3 4 LPSN bacterio.net
- ↑ Bryant & Small, 1956
- 1 2 Cheng & Costerton, 1977
- 1 2 Beveridge, 1990
- ↑ Miller & Jenesel, 1979
- ↑ Blackburn & Hobson, 1962
- ↑ Kalmokoff & Teather, 1997
- ↑ Kepler et al., 1966
- 1 2 Dehority & Scott, 1967
- ↑ Polan et al., 1964
- ↑ Morris & Van Gylswyk, 1980
- ↑ Stewart et al., 1997
- ↑ Russell, 1985
- ↑ Shane et al., 1969
- ↑ Cotta, 1988
- ↑ Hespell et al., 1987
- ↑ Sewell et al., 1988
- ↑ Hespell & O'Bryan-Shah, 1988
- ↑ Lin & Thomson, 1991
- ↑ Hespell & Whitehead, 1990
- ↑ Krause et al., 2003
- ↑ Cantarel et al., 2008
- ↑ Kopecny et al., 2003 (fig. 1.1)
- ↑ Willems et al., 1996
- ↑ Kelly W. J., et al. (2010). (2010). "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316T highlights adaptation to a polysaccharide-rich environment.". PLoS ONE. 5 (8): e11942. 2010. doi:10.1371/journal.pone.0011942. PMC 2914790. PMID 20689770.. PLoS One 5(8): e11942
- 1 2 Attwood et al., 1996
- ↑ Moon et al., 2008
- ↑ Reilly & Attwood 1998
- ↑ Paillard et al., 2007)
- ↑ Wallace et al., 2006
- ↑ Palevich, N. (2016). Comparative genomics of Butyrivibrio and Pseudobutyrivibrio from the rumen : a thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Microbiology and Genetics at Massey University, Palmerston North, New Zealand (Thesis). Massey University. Retrieved from http://mro.massey.ac.nz/handle/10179/9992 or http://hdl.handle.net/10179/9992