GENETIC ANALYSIS OF EXTRACELLULAR TOXINS OF <i>STAPHYLOCOCCUS AUREUS</i>

Iandolo, John J.

doi:10.1146/annurev.mi.43.100189.002111

Cited by 128 publications

(66 citation statements)

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“…The molecular characterization of S. aureus Rif' Expmutants may give insights into the structure and function of RNA polymerase and the interaction of RNA polymerase with regulatory signals involved in postexponential phase expression of exoprotein virulence factors (Abbas-Ali & Coleman, 1977;Janzon et al, 1986;Iandolo, 1989;Kornblum et al, 1990;Vandenesch et al, 1991). As an essential step in this analysis, the rpoBC region of S. aureus has been cloned and mapped.…”

Section: -7482 0 1992 Sgmmentioning

confidence: 99%

Cloning and physical mapping of the Staphylococcus aureus rplL, rpoB and rpoC genes, encoding ribosomal protein L7/L12 and RNA polymerase subunits and '

Aboshkiwa

Al‐Ani

Coleman

et al. 1992

Journal of General Microbiology

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Using segments of the Escherichia coli rpoB and rpoC genes as heterologous probes, we have identified and cloned an 8.3 kb PstI fragment from the Staphylococcus aureus genome containing the rpoB and rpoC genes, which respectively encode the p and p' subunits of DNA-directed RNA polymerase. This region is almost certainly equivalent to the riflocus, located near tofus at interval 12/13 on the S. aureus linkage map. Limited DNA sequencing revealed the gene order rpoB-rpoC (transcribed from left to right) and identified the rplL gene, encoding ribosomal protein L7/L12, upstream of rpoB. This and other evidence suggests that the rpoBC genes of S. aureus form part of a large gene cluster encoding components of the transcription and translation apparatus which is well-conserved in other eubacteria.

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Section: -7482 0 1992 Sgmmentioning

confidence: 99%

Cloning and physical mapping of the Staphylococcus aureus rplL, rpoB and rpoC genes, encoding ribosomal protein L7/L12 and RNA polymerase subunits and '

Aboshkiwa

Al‐Ani

Coleman

et al. 1992

Journal of General Microbiology

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“…kinds of exoproteins (17). It was found that no single virulence factor alone would be either necessary or sufficient for the establishment of infection, albeit the infective dose does vary (48).…”

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confidence: 99%

Two‐Dimensional Analysis of Exoproteins of Methicillin‐Resistant Staphylococcus aureus (MRSA) for Possible Epidemiological Applications

Nakano

Kawano

Kawagishi

et al. 2002

Microbiology and Immunology

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Staphylococcus aureus releases a large number of exoproteins such as toxins and enzymes, as extracellular and surface-associated forms, many of which have been shown to contribute to pathogenic activity or to enhance virulence (17,35,48,57). These exoproteins include (i) factors involved in invasion/tissue penetration, (ii) factors involved in evasion of host defenses and (iii) factors involved in attachment. The first group of exoproteins are alpha-toxin (14), beta-hemolysin (47), gammahemolysin (46), delta-hemolysin (20), and phospholipase C (9). The second group are toxic shock syndrome toxin-1 (TSST-1) (29), enterotoxins (3,4,8,15,22,52), protein A (34), and others (6,31,32,50,53), and the third group contains clumping factor (37) and others (7,12,23,45). More than 30 of these exoproteins that are significantly linked to pathogenesis have been purified to homogeneity, and the genes encoding these exoproteins have been cloned and sequenced (5,48 Abstract: We applied two-dimensional gel electrophoresis (2-DE) to the total exoproteins secreted from pathogenic MRSA strains and identified major protein spots by N-terminal amino acid sequence analysis. In approximately 300 to 500 spots visualized on each gel, various exoproteins and cell-associated proteins were identified and their sites on the gels confirmed for construction of a reference map. Major exotoxins such as enterotoxins SEA, SEB, and SEC3, toxic shock syndrome toxin-1 (TSST-1), and hemolysins were distributed in the region of pI 6.8 to 8.1 and MW 21 to 35 kDa. Although the differences between calculated and observed values of pI and MW were relatively small in each exoprotein, those of several proteins including alpha-hemolysin and SEB were considerably deviated from the positions of the expected values. Some exoproteins were detected as multiple spots. These included beta-hemolysin, enterotoxins SEA, SEB, and SEC3, glutamic acid-specific endopeptidase, glycerophosphoryl diester phosphodiesterase and triacylglycerol lipase. The multiple spots of these exoproteins may be generated by the action of own proteases. Certain similarities of 2-DE patterns among strains belonging to the same coagulase types were observed. On the basis of 2-DE image analysis, coagulase type II strains secreted somewhat larger amounts of SEB and SEC3 as well as TSST-1 than the strains belonging to other coagulase types. Taken together, 2-DE analysis of exoproteins is applicable to epidemiological studies for MRSA, as compared with pulsed field gel electrophoresis of restricted chromosomal DNA.

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“…LM929 cells are fibroblasts that do not express MHCII and express H-2 k at MHCI loci [19]. We used superantigens from two distinct families of Staphylococcus aureus enterotoxins [23,24], SEA and SEC1, to address the second hypothesis that superantigens would bind MHCI in a molecule-dependent fashion. We found that both SEA and SEC1 bound to LM929 cells in a concentration-dependent and saturable manner (Fig.…”

Section: Binding Of Sea and Sec1 To Lm929 Cellsmentioning

confidence: 99%

Complex high affinity interactions occur between MHCI and superantigens

Chapes

Herpich

1998

Journal of Leukocyte Biology

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Staphylococcal enterotoxins A and C1 (SEA or SEC1) bound to major histocompatibility-I (MHCI) molecules with high affinity (binding constants ranging from 1.1 M to 79 nM). SEA and SEC1 directly bound MHCI molecules that had been captured by monoclonal antibodies specific for H-2K k , H-2D k , or both. In addition, MHCIspecific antibodies inhibited the binding of SEC1 to LM929 cells and SEA competitively inhibited SEC1 binding; indicating that the superantigens bound to MHCI on the cell surface. The affinity and number of superantigen binding sites differed depending on whether MHCI was expressed in the membrane of LM929 cells or whether it was captured. These data support the hypothesis that MHCI molecules can serve as superantigen receptors. J. Leukoc. Biol. 64: 587-594; 1998.

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GENETIC ANALYSIS OF EXTRACELLULAR TOXINS OF STAPHYLOCOCCUS AUREUS

Cited by 128 publications

References 0 publications

Cloning and physical mapping of the Staphylococcus aureus rplL, rpoB and rpoC genes, encoding ribosomal protein L7/L12 and RNA polymerase subunits and '

Cloning and physical mapping of the Staphylococcus aureus rplL, rpoB and rpoC genes, encoding ribosomal protein L7/L12 and RNA polymerase subunits and '

Two‐Dimensional Analysis of Exoproteins of Methicillin‐Resistant Staphylococcus aureus (MRSA) for Possible Epidemiological Applications

Complex high affinity interactions occur between MHCI and superantigens

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