Biomaterial Database

Evidence for three different fibrinogen-binding proteins with unique properties from Staphylococcus aureus strain Newman. 1992

M K Bodén, and J I Flock

Center for Biotechnology, Karolinska Institute, NOVUM, Huddinge, Sweden.

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.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010449	Peptide Mapping	Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.	Fingerprints, Peptide,Peptide Fingerprinting,Protein Fingerprinting,Fingerprints, Protein,Fingerprint, Peptide,Fingerprint, Protein,Fingerprinting, Peptide,Fingerprinting, Protein,Mapping, Peptide,Peptide Fingerprint,Peptide Fingerprints,Protein Fingerprint,Protein Fingerprints
D011516	Prothrombin	A plasma protein that is the inactive precursor of thrombin. It is converted to thrombin by a prothrombin activator complex consisting of factor Xa, factor V, phospholipid, and calcium ions. Deficiency of prothrombin leads to hypoprothrombinemia.	Coagulation Factor II,Factor II,Blood Coagulation Factor II,Differentiation Reversal Factor,Factor II, Coagulation,Factor, Differentiation Reversal,II, Coagulation Factor
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003030	Coagulase	Enzymes that cause coagulation in plasma by forming a complex with human PROTHROMBIN. Coagulases are produced by certain STAPHYLOCOCCUS and YERSINIA PESTIS. Staphylococci produce two types of coagulase: Staphylocoagulase, a free coagulase that produces true clotting of plasma, and Staphylococcal clumping factor, a bound coagulase in the cell wall that induces clumping of cells in the presence of fibrinogen.	Staphylocoagulase,Staphylococcal Clumping Factor,Clumping Factor (Staphylococcal),Staphylococcus aureus clone pSCa2 of Coagulase,Staphylococcus aureus strain 213 of Coagulase,Staphylococcus aureus strain 8325-4 of Coagulase,Clumping Factor, Staphylococcal,Factor, Staphylococcal Clumping,Staphylococcus aureus strain 8325 4 of Coagulase
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D005340	Fibrinogen	Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.	Coagulation Factor I,Factor I,Blood Coagulation Factor I,gamma-Fibrinogen,Factor I, Coagulation,gamma Fibrinogen
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D013211	Staphylococcus aureus	Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications.