Evidence for three different fibrinogen-binding proteins with unique properties from Staphylococcus aureus strain Newman.
Binding of extracellular components of Staphylococcus aureus strain Newman to fibrinogen and prothrombin was investigated. Affinity-purified material from fibrinogen- and prothrombin-Sepharose was analysed on immunoblots, and two proteins with coagulase activity were identified. The two coagulases were produced in a sequential manner during staphylococcal growth. An 87 kDa fibrinogen-binding coagulase was produced mainly during the exponential growth phase and was replaced by a 60 kDa fibrinogen- and prothrombin-binding coagulase which was produced mainly during the post-exponential growth phase. In addition, a 19 kDa fibrinogen-binding protein was constitutively produced. Analyses of immunogenic properties and NH2-terminal sequences suggested that the 19, 60 and 87 kDa fibrinogen-binding proteins are not closely related. The NH2-terminal sequence of the 87 kDa protein is identical to a previously described coagulase from Staphylococcus aureus strain 8325-4. The 19 kDa fibrinogen-binding protein, which spontaneously aggregates into dimers and larger molecular weight complexes, had a unique NH2-terminal sequence.
Bodén
M K
MK
Center for Biotechnology, Karolinska Institute, NOVUM, Huddinge, Sweden.
Flock
J I
JI
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification; D002352:Carrier Proteins / Q000032:analysis* / Q000302:isolation & purification; D003030:Coagulase / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000378:metabolism*; D015151:Immunoblotting; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D011516:Prothrombin / Q000378:metabolism; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000254:growth & development
D001426:Bacterial Proteins; D002352:Carrier Proteins; D003030:Coagulase; D011516:Prothrombin; D005340:Fibrinogen