Genetic characterization of staphopain genes in Staphylococcus aureus

被引:18
作者
Golonka, E
Filipek, R
Sabat, A
Sinczak, A
Potempa, J
机构
[1] Jagiellonian Univ, Dept Microbiol, Fac Biotechnol, PL-30387 Krakow, Poland
[2] Int Inst Mol & Cell Biol, Dept Biol Struct, PL-02109 Warsaw, Poland
关键词
cysteine proteinase; distribution; polymorphism; sequence;
D O I
10.1515/BC.2004.137
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Staphylococcus aureus, a leading cause of bacterial infections in humans, is endowed with a wealth of virulence factors that contribute to the disease process. Several extracellular proteolytic enzymes, including cysteine proteinases referred to as the staphopains (staphopain A, encoded by the scpA gene, and staphopain B, encoded by sspB), have proposed roles for staphylococcal virulence. Here we present data regarding the distribution, copy number and genetic variability of the genes encoding the staphopains in a large number of S. aureus strains. The polymorphism of the scpA and sspB genes in three laboratory strains and 126 clinical isolates was analyzed by polymerase chain reaction (PCR)-restriction fragment length polymorphism (RFLP). Both genes were detected in all isolates by PCR amplification and, based on the PCR-RFLP patterns, classified as four types for scpA and six types for sspB. Those with the most divergent patterns were subjected to DNA sequencing and compared with genomic sequence data for the seven available strains of S. aureus. Southern blot analysis of the scpA and sspB sequences indicates that they are strongly conserved as single-copy genes in the genome of each S. aureus strain investigated. Taken together, these data suggest that the staphopains have important housekeeping and/or virulence functions, and therefore may constitute an interesting target for the development of therapeutic inhibitors for the treatment of staphylococcal diseases.
引用
收藏
页码:1059 / 1067
页数:9
相关论文
共 27 条
[1]  
Arvidson S, 2000, GRAM-POSITIVE PATHOGENS, P379
[2]  
BJORKLIND A, 1980, FEMS MICROBIOL LETT, V33, P193
[3]  
Chan PF, 1998, J BACTERIOL, V180, P6232
[4]   Regulation of virulence determinants in vitro and in vivo in Staphylococcus aureus [J].
Cheung, AL ;
Bayer, AS ;
Zhang, GY ;
Gresham, H ;
Xiong, YQ .
FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY, 2004, 40 (01) :1-9
[5]   Staphylococcus aureus genetic loci impacting growth and survival in multiple infection environments [J].
Coulter, SN ;
Schwan, WR ;
Ng, EYW ;
Langhorne, MH ;
Ritchie, HD ;
Westbrock-Wadman, S ;
Hufnagle, WO ;
Folger, KR ;
Bayer, AS ;
Stover, CK .
MOLECULAR MICROBIOLOGY, 1998, 30 (02) :393-404
[6]   ROLE OF A METALLOPROTEASE IN ACTIVATION OF PRECURSOR OF STAPHYLOCOCCAL PROTEASE [J].
DRAPEAU, GR .
JOURNAL OF BACTERIOLOGY, 1978, 136 (02) :607-613
[7]   A novel class of cysteine protease inhibitors:: Solution structure of staphostatin A from Staphylococcus aureus [J].
Dubin, G ;
Krajewski, M ;
Popowicz, G ;
Stec-Niemczyk, J ;
Bochtler, M ;
Potempa, J ;
Dubin, A ;
Holak, TA .
BIOCHEMISTRY, 2003, 42 (46) :13449-13456
[8]  
Dubin G, 2003, ACTA BIOCHIM POL, V50, P715
[9]   Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis [J].
Dubin, G ;
Chmiel, D ;
Mak, P ;
Rakwalska, M ;
Rzychon, M ;
Dubin, A .
BIOLOGICAL CHEMISTRY, 2001, 382 (11) :1575-1582
[10]   The evolution of a resistant pathogen - the case of MRSA [J].
Enright, MC .
CURRENT OPINION IN PHARMACOLOGY, 2003, 3 (05) :474-479