Purification and biochemical characterization of a novel glutamyl endopeptidase secreted by a clinical isolate of Staphylococcus aureus

International Journal of Molecular Medicine

Volumn 27, Issue 5, 2011, Pages 637-645

  Park, Jong Woo ^a   Park, Jung Eun ^a   Park, Jong Kun ^b   Lee, Jung Sup ^a  

^a Chosun University   (South Korea)

^b Wonkwang University   (South Korea)

Author keywords

Glutamyl endopeptidase; PCR cloning; Serine protease; Site directed mutagenesis; Staphylococcus aureus

Indexed keywords

ENZYME PRECURSOR; GLUTAMYL AMINOPEPTIDASE; PROTEINASE; PROTHROMBIN; SERINE PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL BOND; ESCHERICHIA COLI; MUTAGENESIS; NONHUMAN; PH; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PURIFICATION; STAPHYLOCOCCUS AUREUS; SUPERNATANT;

AMINO ACID SEQUENCE; BASE SEQUENCE; CATIONS, DIVALENT; CLONING, MOLECULAR; CULTURE MEDIA, CONDITIONED; ENZYME ASSAYS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEASE INHIBITORS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE ANALYSIS, PROTEIN; SERINE ENDOPEPTIDASES; STAPHYLOCOCCUS AUREUS; SUBSTRATE SPECIFICITY;

EID: 79952920070     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm.2011.625     Document Type: Article

References (36)

1. Archer GL: Staphylococcus aureus: a well-armed pathogen. Clin Infect Dis 26: 1179-1181, 1998.
2. Becker K, Friedrich AW, Lubritz G, Weilert M, Peters G and von Eiff C: Prevalence of genes encoding pyrogenic toxin superantigens and exfoliative toxins among strains of Staphylococcus aureus isolated from blood and nasal specimens. J Clin Microbiol 41: 1434-1439, 2003. (Pubitemid 36428085)
3. Cai Y, Kong F, Wang Q, et al: Comparison of single- and multilocus sequence typing and toxin gene profiling for characterization of methicillin-resistant Staphylococcus aureus. J Clin Microbiol 45: 3302-3308, 2007. (Pubitemid 47585655)
4. Ferry T, Thomas D, Genestier AL, et al: Comparative prevalence of superantigen genes in Staphylococcus aureus isolates causing sepsis with and without septic shock. Clin Infect Dis 41: 771-777, 2005. (Pubitemid 41266740)
5. Bjerketorp J, Jacobsson K and Frykberg L: The von Willebrand factor-binding protein (vWbp) of Staphylococcus aureus is a coagulase. FEMS Microbiol Lett 234: 309-314, 2004. (Pubitemid 38595648)
6. Prokesova L, Potuznikova B, Potempa J, et al: Cleavage of human immunoglobulins by serine proteinase from Staphylococcus aureus. Immunol Lett 31: 259-265, 1992.
7. Cheung AL, Nishina KA, Trotonda MP and Tamber S: The SarA protein family of Staphylococcus aureus. Int J Biochem Cell Biol 40: 355-361, 2008.
8. Li D and Cheung A: Repression of hla by Rot is dependent on Sae in Staphylococcus aureus. Infect Immun 76: 1068-1075, 2008. (Pubitemid 351428066)
9. Sun F, Li C, Jeong D, Sohn C, He C and Bae T: In the Staphylococcus aureus two-component system Sae, the response regulator SaeR binds to a direct repeat sequence and DNA binding requires phosphorylation by the sensor kinase SaeS. J Bacteriol 192: 2111-2127, 2010.
10. Maruo K, Akaike T, Inada Y, Ohkubo I, Ono T and Maeda H: Effect of microbial and mite proteases on low and high molecular weight kininogens. Generation of kinin and inactivation of thiol protease inhibitory activity. J Biol Chem 268: 17711-17715, 1993. (Pubitemid 23260276)
11. Olsen RJ and Musser JM: Molecular pathogenesis of necrotizing fasciitis. Ann Rev Path 5: 1-31, 2010.
12. Drapeau GR, Boily Y and Houmard J: Purification and properties of an extracellular protease of Staphylococcus aureus. J Biol Chem 247: 6720-6726, 1972.
13. Nickerson NN, Prasad L, Jacob L, Delbaere LT and McGavin MJ: Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing. J Biol Chem 282: 34129-34138, 2007. (Pubitemid 350159450)
14. Arvidson S: Hydrolysis of casein by three extracellular proteolytic enzymes from Staphylococcus aureus, strain V8. Acta Pathol Microbiol 81: 538-544, 1973.
15. Drapeau GR: Role of metalloprotease in activation of the precursor of staphylococcal protease. J Bacteriol 136: 607-613, 1978.
16. Massimi I, Park E, Rice K, Müller-Esterl W, Sauder D and McGavin MJ: Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of Staphylococcus aureus. J Biol Chem 277: 41770-41777, 2002. (Pubitemid 35257486)
17. Yoshikawa K, Tsuzuki H, Fujiwara T, et al: Purification, characterization and gene cloning of a novel glutamic acid-specific endopeptidase from Staphylococcus aureus ATCC 12600. Biochim Biophys Acta 1121: 221-228, 1992.
18. Rice K, Peralta R, Bast D, De Azavedo J and McGavin MJ: Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and non-polar inactivation of sspA-encoded serine protease. Infect Immun 69: 159-169, 2001. (Pubitemid 32038312)
19. Shaw L, Golonka E, Potempa J and Foster SJ: The role and regulation of the extracellular proteases of Staphylococcus aureus. Microbiology 150: 217-228, 2004. (Pubitemid 38111488)
20. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
21. Hulo N, Bairoch A, Bulliard V, et al: The 20 years of PROSITE. Nucleic Acids Res 36: D245-D249, 2008. (Pubitemid 351149730)
22. Fisher CL and Pei GK: Modification of a PCR-based site-directed mutagenesis method. Biotechniques 23: 570-571, 574, 1997.
23. Chang AK, Kim HY, Park JE, et al: Vibrio vulnificus secretes a broad-specificity metalloprotease capable of interfering with blood homeostasis through prothrombin activation and fibrino-lysis. J Bacteriol 187: 6909-6916, 2005. (Pubitemid 41428866)
24. Kwon JY, Chang AK, Park JE, Shin SY, Yoon SM and Lee JS: Vibrio extracellular protease with prothrombin activation and fibrinolytic activities. Int J Mol Med 19: 157-163, 2007.
25. Ohara-Nemoto Y, Ikeda Y, Kobayashi M, Sasaki M, Tajika S and Kimura S: Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis. Microb Patho 33: 33-41, 2002. (Pubitemid 35034597)
26. Iwahana H, Yoshimoto K, Shigekiyo T, Shirakami A, Saito S and Itakura M: Molecular and genetic analysis of a compound heterozygote for dysprothrombinemia of prothrombin Tokushima and hypoprothrombinemia. Am J Hum Genet 51: 1386-1395, 1992. (Pubitemid 23001098)
27. Houmard J and Drapeau GR: Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds. Proc Natl Acad Sci USA 69: 3506-3509, 1972.
28. Potempa J, Dubin A, Korzus G and Travis J: Degradation of elastin by a cysteine proteinase from Staphylococcus aureus. J Biol Chem 263: 2664-2667, 1988. (Pubitemid 18062907)
29. Kakudo S, Kikuchi N, Kitadokoro K, et al: Purification, characterization, cloning, and expression of a glutamic acid-specific protease from Bacillus licheniformis ATCCCC 14580. J Biol Chem 267: 23782-23788, 1992. (Pubitemid 23088186)
30. Nemoto TK, Ohara-Nemoto Y, Ono T, et al: Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli. FEBS J 275: 573-587, 2008.
31. Yabuta M, Ochi N and Ohsuye K: Hyperproduction of a recombinant fusion protein of Staphylococcus aureus V8 protease in Escherichia coli and its processing by OmpT protease to release an active V8 protease derivative. Appl Microbiol Biotechnol 44: 118-125, 1995.
32. Ono T, Nemoto TK, Shimoyama Y, Kimura S and Ohara-Nemoto Y: An Escherichia coli expression system for glutamyl endopeptidases optimized by complete suppression of autodegradation. Anal Biochem 381: 74-80, 2008.
33. Reed SB, Wesson CA, Liou LE, et al: Molecular characterization of a novel Staphylococcus aureus serine protease operon. Infect Immun 69: 1521-1527, 2001. (Pubitemid 32187604)
34. Barbosa JA, Saldanha JW and Garratt RC: Novel features of serine protease active sites and specificity pockets: sequence analysis and modelling studies of glutamate-specific endopeptidases and epidermolytic toxins. Protein Eng 9: 591-601, 1996. (Pubitemid 26241636)
35. D Demidyuk IV, Romanova DV, Nosovskaya EA, Chestukhina GG, Kuranova IP and Kostrov SV: Modification of substrate-binding site of glutamyl endopeptidase from Bacillus intermedius. Protein Eng Des Sel 17: 411-416, 2004. (Pubitemid 39280042)
36. Redpath MB, Foster TJ and Bailey CJ: The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus. FEMS Microbiol Lett 65: 151-155, 1991.