Loss of Antibiotic Resistance in Staphylococcus Aureus Resulting from Growth at High Temperature

Asheshov, Elizabeth H.

doi:10.1099/00221287-42-3-403

Cited by 84 publications

(57 citation statements)

References 10 publications

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“…Plasmid profiling was carried out as described in Dowsett et al (1984). Curing ofresistance was attempted by growing staphylococci at 42 'C with repeated subculture (Asheshov, 1966). Resistance transfers on mouse skin and on filters were made as described in Naidoo & Noble (1987), mixed broth culture studies were made as described by Cookson & Phillips (1988) and attempts to induce phage made using mitomycin C. Centrifugation in caesium chloride/ethidium bromide was carried out using an MSE Europa centrifuge at 50000 rev./min.…”

Section: Methodsmentioning

confidence: 99%

Transmissible mupirocin resistance inStaphylococcus aureus

1989

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SUMMARYThe spread of two strains of Staphylococcus aureus with high level resistance to mupirocin is described. The resistance proved to be easily transferred to other S. aureus strains by filter mating experiments and on the skin of mice. No plasmid band corresponding to the resistance could be demonstrated by agarose gel electrophoresis or by caesium chloride gradient centrifugation but cleavage of 'chromosomal' DNA from resistant recipients showed bright bands of DNA absent from sensitive controls.

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Section: Methodsmentioning

confidence: 99%

Transmissible mupirocin resistance inStaphylococcus aureus

1989

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“…Phage 85 was used to transduce plasmids and chromosomal markers in S. aureus (Asheshov, 1966). Recombinant plasmids were introduced into S. aureus by electroporation.…”

Section: Transduction and Electrotransformationmentioning

confidence: 99%

The dipeptide repeat region of the fibrinogen‐binding protein (clumping factor) is required for functional expression of the fibrinogen‐binding domain on the Staphylococcus aureus cell surface

Hartford

François

Vaudaux

et al. 1997

Molecular Microbiology

127

152

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SummaryClumping factor of Staphylococcus aureus is a fibrinogen-binding protein that is located on the bacterial cell surface. The protein has an unusual repeat domain (region R) comprising mainly the dipeptide aspartate and serine. To determine if region R has a role in the surface display of the fibrinogen-binding region A domain, deletions lacking the region R encoding region of the clfA gene were generated. To determine the minimum length of region R required for wild-type levels of ClfA expression, variants with truncated region R domains were constructed. S. aureus cells expressing mutated clfA genes were tested for (i) proteins released by lysostaphin treatment that reacted with antisera specific for region A, (ii) clumping in soluble fibrinogen, (iii) adherence to immobilized fibrinogen and (iv) expression of the ClfA antigen on the cell surface by fluorescent activated cell sorting analysis. Each construct expressed three major immunoreactive proteins, two of which were putative Nterminal degradation products. Region R residues greater than 40 were required between region A and W (72 residues between region A and the LPDTG sorting signal) for wild-type levels of clumping in fibrinogen. A stepwise decrease in clumping titre was observed as the distance between region A and LPDTG was decreased from 72 to 4 residues. Similarly, a decrease in binding of anti-ClfA serum and in binding to fibrinogen-coated plastic surfaces was observed with cells expressing ClfA with 40 region R residues or less. Nevertheless, low levels of adherence to fibrinogen and binding to anti-ClfA serum occurred with ClfA derivatives that lacked region R altogether. This indicates that a small proportion of the ClfA molecules are linked to peptidoglycan very close to the cell surface but that residues greater than 72 are needed to allow sufficient ClfA molecules to span the entire cell wall and to display the biologically active A domain in a form that can participate fully in fibrinogen binding.

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“…Fragment F is known to carry att4ll and may carry att413. Transduction was performed with phage 480a as described by Asheshov (1966).…”

Section: E T H O D Smentioning

confidence: 99%

Physical and Genetic Mapping of the Protein A Gene in the Chromosome of Staphylococcus aureus 8325-4

Patel

Foster²,

Pattee³

1989

Microbiology

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The gene coding for protein A (spa) has been mapped close to nov on the genetic map of the chromosome of Staphylococcus aureus 8 325-4. A rapid mapping procedure has been developed which first allowed the region of the chromosome carrying the spa gene to be identified by blot hybridization of large DNA fragments which had been separated by pulsed-field gel electrophoresis. Restriction endonuclease SmaI fragment G was shown to carry the spa gene. An insertion mutation in spa was constructed by in vitro insertion of a fragment of DNA expressing resistance to kanamycin and neomycin. A spa : :KanrNeof mutation was isolated in S. aureus 8325-4 by allele replacement. This provided a selectable marker which allowed the spa gene to be mapped by transformation analysis.

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Loss of Antibiotic Resistance in Staphylococcus Aureus Resulting from Growth at High Temperature

Cited by 84 publications

References 10 publications

Transmissible mupirocin resistance inStaphylococcus aureus

Transmissible mupirocin resistance inStaphylococcus aureus

The dipeptide repeat region of the fibrinogen‐binding protein (clumping factor) is required for functional expression of the fibrinogen‐binding domain on the Staphylococcus aureus cell surface

Physical and Genetic Mapping of the Protein A Gene in the Chromosome of Staphylococcus aureus 8325-4

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