Serine proteases and ovine footrot
Xiaoyan Han , Ruth M Kennan and Julian I Rood
+ Author Affiliations
- Author Affiliations
Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Department of Microbiology, Monash University, Clayton, Vic. 3800, Australia
Email: julian.rood@monash.edu
Microbiology Australia 34(1) 37-40 https://doi.org/10.1071/MA13012
Published: 20 March 2013
Abstract
Footrot is a disease that is of importance to the wool and sheep meat industries. The principle causative agent of ovine footrot is the anaerobic bacterium, Dichelobacter nodosus, virulent isolates of which secrete three closely related subtilisin-like proteases, AprV2, AprV5 and BprV. By constructing isogenic mutants and carrying out virulence tests in sheep it was shown that AprV2 is a major virulence factor of D. nodosus. Structural analysis of AprV2 has revealed that it contains several novel loops, one of which appears to act as an exosite that may modulate substrate accessibility. Both elastase activity and protease thermostability have been used for the differential diagnosis of D. nodosus isolates. Analysis of the protease mutants has shown that AprV2 is the thermostable protease and also is responsible for the elastase activity of D. nodosus, while AprV5 is the major extracellular protease. In addition, AprV5 is required for its own maturation and for the optimal cleavage of AprV2 and BprV to their mature active forms.
References
[1] Kennan, R.M. et al. (2011) The pathogenesis of ovine footrot. Vet. Microbiol. 153, 59–66.| The pathogenesis of ovine footrot.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXhtFKiurzE&md5=cc43f7d331a42d337618e745b78ab8beCAS |
[2] Kennan, R.M. et al. (2010) The subtilisin-like protease AprV2 is required for virulence and uses a novel disulphide-tethered exosite to bind substrates. PLoS Pathog. 6, e1001210.
| The subtilisin-like protease AprV2 is required for virulence and uses a novel disulphide-tethered exosite to bind substrates.Crossref | GoogleScholarGoogle Scholar |
[3] Han, X. et al. (2012) The AprV5 subtilase is required for the optimal processing of all three extracellular serine proteases from Dichelobacter nodosus. PLoS ONE 7, e47932.
| The AprV5 subtilase is required for the optimal processing of all three extracellular serine proteases from Dichelobacter nodosus.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC38Xhs1KisLrE&md5=2455f525aeb6d140a31273814358ab63CAS |
[4] Egerton, J.R. et al. (1969) The aetiology and pathogenesis of ovine footrot. I.A histological study of the bacterial invasion. J. Comp. Pathol. 79, 207–216.
| The aetiology and pathogenesis of ovine footrot. I.A histological study of the bacterial invasion.Crossref | GoogleScholarGoogle Scholar | 1:STN:280:DyaF1M7mtF2kug%3D%3D&md5=3ffcbfdf72ed5c39f550f33faebce145CAS |
[5] Stewart, D.J. et al. (1984) Differences between strains of Bacteroides nodosus in their effects on the severity of footrot, bodyweight and wool growth on Merino sheep. Aust. Vet. J. 61, 348–352.
| Differences between strains of Bacteroides nodosus in their effects on the severity of footrot, bodyweight and wool growth on Merino sheep.Crossref | GoogleScholarGoogle Scholar | 1:STN:280:DyaL2M7kvFSgtg%3D%3D&md5=0aae009db086336de864a7beecd8411cCAS |
[6] Siezen, R.J. and Leunissen, J.A. (1997) Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 6, 501–523.
| Subtilases: the superfamily of subtilisin-like serine proteases.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2sXhvVOlsrY%3D&md5=49f8a5cf7b34bf7f4599a9bcc40f4ad3CAS |
[7] Egerton, J.R. (1986) Control and eradication of ovine footrot. In Footrot in Ruminants. Proceedings of a Workshop, Melbourne 1985 (Stewart, D.J. et al., eds), pp. 35–42, CSIRO Division of Animal Health and Australian Wool Corporation.
[8] Green, L.E. and George, T.R. (2008) Assessment of current knowledge of footrot in sheep with particular reference to Dichelobacter nodosus and implications for elimination or control strategies for sheep in Great Britain. Vet. J. 175, 173–180.
| Assessment of current knowledge of footrot in sheep with particular reference to Dichelobacter nodosus and implications for elimination or control strategies for sheep in Great Britain.Crossref | GoogleScholarGoogle Scholar | 1:STN:280:DC%2BD1c7jtlersg%3D%3D&md5=1005a27013f5ede4f78a62b843b29f1aCAS |
[9] Kennan, R.M. et al. (2001) The type IV fimbrial subunit gene (fimA) of Dichelobacter nodosus is essential for virulence, protease secretion, and natural competence. J. Bacteriol. 183, 4451–4458.
| The type IV fimbrial subunit gene (fimA) of Dichelobacter nodosus is essential for virulence, protease secretion, and natural competence.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXlsVensrw%3D&md5=f36d3b3677639f3cedb0446294f5de2cCAS |
[10] Han, X. et al. (2008) Twitching motility is essential for virulence in Dichelobacter nodosus. J. Bacteriol. 190, 3323–3335.
| Twitching motility is essential for virulence in Dichelobacter nodosus.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXlt1Kqu7k%3D&md5=6089142890fd1ff4fdb87362380e7ff2CAS |
[11] Han, X. et al. (2007) Type IV fimbrial biogenesis is required for protease secretion and natural transformation in Dichelobacter nodosus. J. Bacteriol. 189, 5022–5033.
| Type IV fimbrial biogenesis is required for protease secretion and natural transformation in Dichelobacter nodosus.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXotFaksbY%3D&md5=7741937e70b741ba397e4cb5fa1564e3CAS |
[12] Thomas, J.H. (1964) The pathogenesis of footrot in sheep with reference to proteases of Fusiformis nodosus. Aust. J. Agric. Res. 15, 1001–1016.
| The pathogenesis of footrot in sheep with reference to proteases of Fusiformis nodosus.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaF2MXosFWksw%3D%3D&md5=c8be4ef868474f578be33414b60d23c6CAS |
[13] Kortt, A.A. et al. (1993) Amino acid sequence of extracellular acidic protease V5 of Dichelobacter nodosus, the causative organism of ovine footrot. Biochem. Mol. Biol. Int. 29, 989–998.
| 1:CAS:528:DyaK3sXkvFSjsrs%3D&md5=6689f78b40e0d0d5c2d11b05f037ef59CAS |
[14] Kortt, A.A. et al. (1994) Characterization of a basic serine protease (pI ~ 9.5) secreted by virulent strains of Dichelobacter nodosus and identification of a distinct, but closely related, proteinase secreted by benign strains. Biochem. J. 299, 521–525.
| 1:CAS:528:DyaK2cXktVeluro%3D&md5=f065d8f405fd83969f0dc1812bbaa1aeCAS |
[15] Stewart, D.J. (1979) The role of elastase in the differentiation of Bacteroides nodosus infections in sheep and cattle. Res. Vet. Sci. 27, 99–105.
| 1:CAS:528:DyaL3cXitFejtbk%3D&md5=67f705ffcbc1bc86e4f865b20f8bf825CAS |
[16] Palmer, M.A. (1993) A gelatin test to detect activity and stability of proteases produced by Dichelobacter nodosus. Vet. Microbiol. 36, 113–122.
| A gelatin test to detect activity and stability of proteases produced by Dichelobacter nodosus.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2cXivFamt7o%3D&md5=928cd38c94288b014469d89e2b4d8caeCAS |
[17] Riffkin, M.C. et al. (1993) Cloning, sequence and expression of the gene (aprV5) encoding extracellular serine acidic protease V5 from Dichelobacter nodosus. Gene 137, 259–264.
| Cloning, sequence and expression of the gene (aprV5) encoding extracellular serine acidic protease V5 from Dichelobacter nodosus.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2cXhvVCgu78%3D&md5=76bd81aa8113ead1768d9acdb03bec6fCAS |
[18] Riffkin, M.C. et al. (1995) A single amino-acid change between the antigenically different extracellular serine proteases V2 and B2 from Dichelobacter nodosus. Gene 167, 279–283.
| A single amino-acid change between the antigenically different extracellular serine proteases V2 and B2 from Dichelobacter nodosus.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK28XlvVOgtw%3D%3D&md5=2b28ac11f16bf810391f47f62f41ab51CAS |
[19] Lilley, G.G. et al. (1995) Nucleotide and deduced protein sequence of the extracellular, serine basic protease gene bprB from Dichelobacter nodosus strain 305: comparison with the basic protease gene bprV from virulent strain 198. Biochem. Mol. Biol. Int. 36, 101–111.
| 1:CAS:528:DyaK2MXpt1Ciu7s%3D&md5=16870b29dde5ef44544c1b9471e8c8e7CAS |
[20] Lilley, G.G. et al. (1992) Amino acid and DNA sequences of an extracellular basic protease of Dichelobacter nodosus show that it is a member of the subtilisin family of proteases. Eur. J. Biochem. 210, 13–21.
| Amino acid and DNA sequences of an extracellular basic protease of Dichelobacter nodosus show that it is a member of the subtilisin family of proteases.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK3sXltlChtrg%3D&md5=b5d724976db772d312aed75fa4d085a4CAS |
[21] Shinde, U. and Thomas, G. (2011) Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furin. Methods Mol. Biol. 768, 59–106.
| Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furin.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC38XkvV2gt78%3D&md5=031975c480da932994cc82fb8243b8feCAS |
[22] Wong, W. et al. (2011) S1 pocket of a bacterially derived subtilisin-like protease underpins effective tissue destruction. J. Biol. Chem. 286, 42 180–42 187.
| S1 pocket of a bacterially derived subtilisin-like protease underpins effective tissue destruction.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXhsFKjsr%2FP&md5=cbd6f7befceac810cf9c1e10cb6b9557CAS |
