S2014
Staphylococcus aureus
buffered aqueous suspension, Wood 46 strain
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About This Item
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biological source
Staphylococcus aureus
sterility
Not processed or packaged aseptically
form
buffered aqueous suspension
composition
Cell suspension, ~10% wet weight/volume
storage temp.
2-8°C
General description
Staphylococcus aureus Wood 46 is protein A deficient and spa negative. It shares 98% to 99% genome identity with S.aureus and shows a lower surface expression of cell wall-associated protein A.
Application
(Not intended for use as a starter culture.)
Staphylococcus aureus has been used:
- to mimic infection and induce fever in Pekin duck
- to test its effect on hemocyte morphology in hemolymph samples from beetle Tenebrio molitor larva
- in the antibacterial activity and minimum inhibitory concentration (MIC) assay with gedunin and 7-deacetoxy-7αhydroxygedunin potassium salt
Wood 46, a non-protein A producing S. aureus strain, prepared by the same method as P7155 (Protein A, crude cell suspension-Cowan strain), may be used as a control in protein A-immunoglobulin binding studies.
Biochem/physiol Actions
Staphylococcus aureus Wood 46 displays reduced virulence compared to the S. aureus. This isolate is useful in understanding protein A role in pathogenesis and virulence.
Physical form
Formalin-fixed crude cell suspension of essentially non-viable S. aureus (Wood 46 strain) in 0.05 M potassium phosphate buffer, pH 7.5, containing 0.2% sodium azide
Preparation Note
Produced in pure culture.
Analysis Note
This strain binds less than 10% of the rabbit IgG bound by P 7155 as assayed by a modification of the method of Kessler.
Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Poultry science, 90(6), 1234-1238 (2011-05-21)
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Journal of immunology (Baltimore, Md. : 1950), 117(5 Pt 1), 1482-1490 (1976-11-01)
Procedures are detailed for the rapid isolation of representative cell membrane antigens with protein A-bearing staphylococci as an adsorbent for IgG antibodies complexed with the antigens. Cell surface membrane proteins were radioiodinated and solubilized in nonionic detergent. Specific antisera were
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