Home LiteratureArticle Details
PMID: 6094999 Published · ppublish English Comparative Study Journal Article

Quantitative differences in specific binding of fibrinogen fragment D by M-positive and M-negative group-A streptococci.

Medical microbiology and immunology ·Vol. 173 ·No. 3 ·1984-00-00 ·Pages 145-53

Schmidt KH, Gerlach D, Kühnemund O, Köhler W

Abstract

Selected M-positive and M-negative group-A streptococcal strains were investigated with respect to their selective absorption of plasmin fibrinogen degradation products (FDP) in a simple batch technique. After incubation of killed streptococci with the FDP mixture, the centrifuged supernatants were investigated by SDS-electrophoresis and the binding capacity of the strains was calculated by evaluation of the scanning curves of stained gels. It was found that there is a specific uptake of the C-terminal fragment D by both M-positive and M-negative strains. Although the M-positive strains bound more fragment D (30%-80%) than did the M-negative strains (10%-15%), it could be clearly shown that the loss of M-protein was not necessarily linked with a total disappearance of fibrinogen binding activity. Fragment D blocked the agglutination of streptococci by fibrinogen. Washing the streptococci preincubated with FDP with a 0.1 M citric acid, 6 M urea buffer, pH 3.0, restored agglutination. Treatment of FDP-incubated bacteria with this buffer was found to be a means of recovering pure fragment D from streptococcal cells. It is suggested that M-positive and M-negative streptococci have qualitatively similar binding sites. These receptors might be reduced in the M-negative streptococci. Human serum albumin and Tween 20 did not influence the interaction between streptococcus and fibrinogen.

MeSH Terms
Agglutination Antigens, Bacterial Bacterial Outer Membrane Proteins Bacterial Proteins/metabolism Carrier Proteins Fibrin Fibrinogen Degradation Products/metabolism Platelet Membrane Glycoproteins Protein Binding Receptors, Cell Surface/metabolism Streptococcus pyogenes/metabolism
Chemicals
Antigens, Bacterial Bacterial Outer Membrane Proteins Bacterial Proteins Carrier Proteins Fibrin Fibrinogen Degradation Products Platelet Membrane Glycoproteins Receptors, Cell Surface fibrinogen D fragment streptococcal M protein
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schmidt K H
Gerlach D
Kühnemund O
Köhler W
References (18)
18 references, click to expand
  1. Binding of fibrinogen degradation products to S. aureus and to beta-hemolytic streptococci group A, C and G.
    Acta Pathol Microbiol Scand B. 1981 Apr;89(2):49-55 PMID: 7020340
  2. Fibrinogen binding structures in beta-hemolytic streptococci group A, C, and G. Comparisons with receptors for IgG and aggregated beta 2-microglobulin.
    Acta Pathol Microbiol Scand B. 1979 Oct;87(5):303-10 PMID: 93400
  3. Plasminogen: purification from human plasma by affinity chromatography.
    Science. 1970 Dec 4;170(3962):1095-6 PMID: 5475635
  4. Interaction of streptococcal cell wall components with fibrinogen. I. adsorption of fibrinogen by immobilized T-proteins of streptococcus pyogenes.
    Immunobiology. 1981;158(4):330-7 PMID: 7016738
  5. Paracoagulation of fibrinogen in vitro and in vivo by protein T of Steptococcus pyogenes.
    Zentralbl Bakteriol Orig A. 1978 Sep;241(3):301-7 PMID: 364884
  6. Primary structure of the B-chain of human plasmin.
    Eur J Biochem. 1977 Jun 1;76(1):129-37 PMID: 142009
  7. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
    J Biol Chem. 1969 Aug 25;244(16):4406-12 PMID: 5806584
  8. Fibrinogen-mediated adherence of group A Streptococcus to influenza A virus-infected cell cultures.
    Infect Immun. 1982 Nov;38(2):513-20 PMID: 6754619
  9. FIBRINOGEN PRECIPITATION BY STREPTOCOCCAL M PROTEIN. I. IDENTITY OF THE REACTANTS, AND STOICHIOMETRY OF THE REACTION.
    J Exp Med. 1965 May 1;121:849-59 PMID: 14278234
  10. Human fibrinogen possesses binding site for staphyococci on Aalpha and Bbeta polypeptide chains.
    Nature. 1975 Dec 18;258(5536):643-5 PMID: 1207746
  11. Identification of a region of human fibrinogen interacting with staphylococcal clumping factor.
    Biochemistry. 1982 Mar 16;21(6):1407-13 PMID: 7074095
  12. Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci.
    J Clin Invest. 1982 Apr;69(4):1042-5 PMID: 7042754
  13. Binding of human fibrinogen and its polypeptide chains to group B streptococci.
    Med Microbiol Immunol. 1983;172(3):149-53 PMID: 6358819
  14. Comparative studies on surface hydrophobicity of streptococcal strains of groups A, B, C, D and G.
    J Gen Microbiol. 1984 Mar;130(3):657-64 PMID: 6726181
  15. Isolation, characterization, and synthesis of peptides from human fibrinogen that block the staphylococcal clumping reaction and construction of a synthetic clumping particle.
    Biochemistry. 1982 Mar 16;21(6):1414-20 PMID: 7074096
  16. The action of fibrinogen on certain pathogenic cocci.
    J Gen Microbiol. 1955 Oct;13(2):383-93 PMID: 13278487
  17. Domains in the fibrinogen molecule.
    J Mol Biol. 1982 Aug 25;159(4):665-83 PMID: 7143446
  18. Nature of the interaction between M protein of Streptococcus pyogenes and fibrinogen.
    J Infect Dis. 1972 Jun;125(6):626-30 PMID: 4556570
Article Info
Journal
Medical microbiology and immunology
Abbr.
Med Microbiol Immunol
ISSN
0300-8584
Published
1984-00-00
Pages
145-53
Language
English
Region
Germany
NLM ID
0314524
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]