Characterisation of an extracellular serine protease gene (nasp gene) from Dermatophilus congolensis

FEMS Microbiology Letters

Volumn 231, Issue 1, 2004, Pages 53-57

  Garcia Sanchez, Alfredo ^a,b   Cerrato, Rosario ^b   Larrasa, Jose ^c   Ambrose, Nicholas C ^d   Parra, Alberto ^b   Alonso, Juan M ^b   Hermoso De Mendoza, Miguel ^b   Rey, Joaquin M ^b   Mine, Madisa O ^e   Carnegie, Patrick R ^f   Ellis, Trevor M ^g   Masters, Anne M ^h   Pemberton, Alan D ^d   Hermoso De Mendoza, Javier ^b  

^a MOREDUN RESEARCH INSTITUTE   (United Kingdom)

^b UNIVERSITY OF EXTREMADURA   (Spain)

^c Laboratorios Larrasa   (Spain)

^d UNIVERSITY OF EDINBURGH   (United Kingdom)

^e BOTSWANA COLLEGE OF AGRICULTURE   (Botswana)

^f MURDOCH UNIVERSITY   (Australia)

^g Agric   (Hong Kong)

^h DEPARTMENT OF AGRICULTURE AND FOOD WESTERN AUSTRALIA   (Australia)

Author keywords

Dermatophilosis; nasp gene; Pathogenesis; Serine protease

Indexed keywords

GENOMIC DNA; OLIGONUCLEOTIDE; SERINE PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; DERMATOPHILUS; EXTRACELLULAR SPACE; GENE AMPLIFICATION; GENETIC CODE; NASP GENE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

DERMATOPHILUS CONGOLENSIS;

EID: 10744230483     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00958-3     Document Type: Article

References (24)

1. Ambrose N.C. The pathogenesis of dermatophilosis. Trop. Anim. Health Prod. 28:1996;29S-37S.
2. Skalka B., Pospisil L. Hemolytic interactions of Dermatophilus congolensis. Zent.bl. Vet.med. [B]. 39:1992;139-143.
3. Masters A.M., Ellis T.M., Grein S.B. Dermatophilus congolensis: strain differences in expression of phospholipase activities. Vet. Microbiol. 57:1997;199-213.
4. Gordon M.A. The genus Dermatophilus. J. Bacteriol. 88:1964;509-522.
5. Hermoso de Mendoza J., Arenas A., Alonso J.M., Rey J.M., Gil M.C., Anton J.M., Hermoso de Mendoza M. Enzymatic activities of Dermatophilus congolensis measured by API ZYM. Vet. Microbiol. 37:1993;175-179.
6. Ambrose N.C., el Jack M.A., McOrist S., Boid R. Electrophoretic and antigenic characterisation of Dermatophilus congolensis extracellular products. Vet. Microbiol. 59:1997;37-51.
7. Scott, D.W. (1988) Actionomycetic infections: Dermatophilosis. In: Large Animal Dermatology, pp. 136-167. W.B. Saunders, Philadelphia, PA.
8. Travis J., Potempa J., Maeda H. Are bacterial proteases pathogenic factors? Trends Microbiol. 3:1995;407-407.
9. Henderson B., Wilson M., Wren B. Are bacterial exotoxins cytokine network regulators? Trends Microbiol. 5:1997;454-458.
10. Ambrose N., Lloyd D., Maillard J.C. Immune responses to Dermatophilus congolensis infections. Parasitol. Today. 15:1999;295-300.
11. Mine O.M., Carnegie P.R. Use of degenerate primers and heat-soaked polymerase chain reaction (PCR) to clone a serine protease antigen from Dermatophilus congolensis. Immunol. Cell Biol. 75:1997;484-491.
12. Ambrose N.C., Mijinyawa M.S., Hermoso de Mendoza J. Preliminary characterisation of extracellular serine proteases of Dermatophilus congolensis isolates from cattle, sheep and horses. Vet. Microbiol. 62:1998;321-335.
13. Shibata Y., Fujimura S., Nakamura T. Purification and partial characterization of an elastolytic serine protease of Prevotella intermedia. Appl. Environ. Microbiol. 59:1993;2107-2111.
14. Azghani A.O., Gray L.D., Johnson A.R. A bacterial protease perturbs the paracellular barrier function of transporting epithelial monolayers in culture. Infect. Immun. 61:1993;2681-2686.
15. Bowles V.G., Carnegie P.R., Sandeman R.M. Characterization of proteolytic and collagenolytic enzymes from the larvae of Lucilia cuprina, the sheep blowfly. Aust. J. Biol. Sci. 41:1988;269-278.
16. Cole G.T., Zhu S.W., Hsu L.L., Kruse D., Seshan K.R., Wang F. Isolation and expression of a gene which encode a wall-associated proteinase of Coccidiodes immitis. Infect. Immun. 60:1992;416-427.
17. Kolattukudy P.E., Lee J.D., Rogers L.M., Zimmerman P., Ceselski S., Fox B., Stein B., Copelan E.A. Evidence for possible involvement of an elastolytic serine protease in aspergillosis. Infect. Immun. 61:1993;2357-2368.
18. Wilson, K. (1987) Preparation of genomic DNA from bacteria. In: Current Protocols in Molecular Biology (Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Siedman, J.G., Smith, J.A. and Struhl, K., Eds.), pp. 2.4.1-2.4.4. Green Publishing Associates and Wiley Interscience, New York.
19. Larrasa J., García A., Ambrose N.C., Alonso J.M., Parra A., Hermoso de Mendoza M., Salazar J., Rey J., Hermoso de Mendoza J. A simple random amplified polymorphic DNA genotyping method for field isolates of Dermatophilus congolensis. J. Vet. Med. B. 49:2002;135-141.
20. Marck C. DNA Strider: a 'C' program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers. Nucleic Acids Res. 16:1988;1829-1836.
21. Altschul S.F., Gish W., Miller W., Myers W., Lipman D.J. Basic local alignment search tool. J. Mol. Biol. 215:1990;403-410.
22. Henrik N., Engelbrech T.J., Brunak S., Von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
23. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:1984;387-395.
24. Siezen R.J., de Vos W.M., Leunissen J.A., Dijkstra B.W. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Protein Eng. 4:1991;719-737.