scholarly journals Epitopes of streptococcal M proteins shared with cardiac myosin.

1985 ◽  
Vol 162 (2) ◽  
pp. 583-591 ◽  
Author(s):  
J B Dale ◽  
E H Beachey
Keyword(s):  
Acute Rheumatic Fever ◽  
M Protein ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Poststreptococcal Glomerulonephritis ◽  
Heavy Chains ◽  
M Proteins ◽  
Group A

We present evidence that M proteins from three different serotypes of group A streptococci share epitopes with cardiac myosin. Rabbit antisera evoked by a purified fragment of type 5 M protein crossreacted with myosin, but not alpha-tropomyosin, actin, or myosin light chains. In enzyme-linked immunosorbent assays, the myosin-crossreactive antibodies were totally inhibited by type 5 M protein and partially inhibited by types 6 and 19 M proteins. The affinity-purified myosin antibodies opsonized type 5 streptococci, indicating that they were directed against protective M protein epitopes on the surface of the organisms. Immunoblot analyses demonstrated the binding of the crossreactive antibodies to myosin heavy chains. Sera from patients with acute rheumatic fever showed significantly stronger reactions with myosin than did sera from their siblings, hospitalized controls, or patients with poststreptococcal glomerulonephritis.

scholarly journals Sequence of myosin-crossreactive epitopes of streptococcal M protein.

1986 ◽  
Vol 164 (5) ◽  
pp. 1785-1790 ◽  
Author(s):  
J B Dale ◽  
E H Beachey
Keyword(s):  
Synthetic Peptide ◽  
Synthetic Peptides ◽  
Human Myocardium ◽  
M Protein ◽  
Cardiac Myosin ◽  
Streptococcal M Protein ◽  
M Proteins ◽  
Group A ◽  
Inhibition Studies ◽  
Rheumatic Heart

Group A streptococcal M proteins contain epitopes that crossreact with sarcolemmal membrane proteins of human myocardium and myosin. In the present study, synthetic peptide copies spanning the entire 197-residue pepsin extracted fragment of type 5 M protein were used to localize the myosin-crossreactive epitopes of the molecule. Peptide 84-116 inhibited by 75% the binding of myosin-crossreactive antibodies evoked by pep M5, as determined by ELISA. Immunoblot inhibition studies confirmed that peptide 84-116 almost totally inhibited the binding of pep M5 antibodies to the heavy chain of human cardiac myosin. None of the remaining synthetic peptides, including peptide 1-35, which contains protective epitopes, inhibited antibodies binding to myosin. Two of three rabbits immunized with peptide 84-116 developed low but significant levels of antibodies crossreactive with myosin. Identification of the primary structures containing tissue-crossreactive as opposed to protective epitopes should not only allow the development of safe and effective M protein vaccines, but may also provide insights into the pathogenesis of rheumatic heart disease.

scholarly journals Reactivity of Rheumatic Fever and Scarlet Fever Patients' Sera with Group A Streptococcal M Protein, Cardiac Myosin, and Cardiac Tropomyosin: a Retrospective Study

2000 ◽  
Vol 68 (12) ◽  
pp. 7132-7136 ◽  
Author(s):  
Kevin F. Jones ◽  
Stephen S. Whitehead ◽  
Madeleine W. Cunningham ◽  
Vincent A. Fischetti
Keyword(s):  
Retrospective Study ◽  
Rheumatic Fever ◽  
Scarlet Fever ◽  
Acute Rheumatic Fever ◽  
M Protein ◽  
Group A Streptococci ◽  
Cardiac Myosin ◽  
Streptococcal M Protein ◽  
Group A ◽  
Low Levels

ABSTRACT Archived sera (collected in 1946) from acute rheumatic fever (ARF) and untreated scarlet fever and/or pharyngitis patients were reacted with streptococcal M protein, cardiac myosin, and cardiac tropomyosin. Except for very low levels to tropomyosin, antibodies to other antigens were not elevated in the sera of ARF patients relative to those of non-ARF patients, even though there was roughly equivalent exposure to group A streptococci. This suggests that antibodies to these molecules may not play a central role in the induction of ARF.

scholarly journals Antigenic domains of the streptococcal Pep M5 protein. Localization of epitopes crossreactive with type 6 M protein and identification of a hypervariable region of the M molecule.

1986 ◽  
Vol 163 (1) ◽  
pp. 129-138 ◽  
Author(s):  
B N Manjula ◽  
A S Acharya ◽  
T Fairwell ◽  
V A Fischetti
Keyword(s):  
Protein Localization ◽  
Hypervariable Region ◽  
Coiled Coil ◽  
M Protein ◽  
Terminal Domain ◽  
Coil Structure ◽  
M Proteins ◽  
Group A ◽  
Antigenic Domains ◽  
Antigenic Epitopes

Pep M5, the pepsin-derived N-terminal half of the group A streptococcal type 5 M protein exhibits immunologic crossreaction with type 6 M protein, localizing some of the M6-crossreactive epitope(s) within this segment of the M5 protein. Based on the amino acid sequence of the Pep M5 protein, two structurally distinct domains have been recognized within its coiled-coil structure. We have now found that peptides derived from both the structurally distinct domains of the Pep M5 protein contain antigenic epitopes. Furthermore, only the peptides from the C-terminal domain of the Pep M5 protein crossreacted with rabbit anti-M6 sera, whereas those from the N-terminal domain did not. Consistent with this, sequence analyses of the arginyl peptides of the Pep M6 protein, the pepsin-derived N-terminal half of the M6 protein, revealed extensive homology of some of these peptides with regions within the C-terminal domain of the Pep M5 molecule. While an arginyl peptide of the Pep M6 protein exhibits 84% homology with region 150-186 of the Pep M5 protein, the C-terminal hexadecapeptide of the Pep M6 protein is virtually identical with the corresponding region of the Pep M5 protein. These results are suggestive of conformational similarities in the region around the pepsin-susceptible site within the M5 and M6 proteins. In addition, one or more epitopes of the M5 protein that are crossreactive with the M6 protein may be placed close to the pepsin-susceptible site of the M5 protein. Previous studies have suggested the N-terminal half of the M proteins to be the variable part of the molecule among the different M protein serotypes. The present results suggest that the N-terminal quarter of the M protein may represent the hypervariable domain of the M molecule.

scholarly journals Relative synthesis of cardiac contractile proteins. Evidence for synthesis from the same precursor pool

1981 ◽  
Vol 194 (3) ◽  
pp. 673-678 ◽  
Author(s):  
C D Evans ◽  
S S Schreiber ◽  
M Oratz ◽  
M A Rothschild
Keyword(s):  
Light Chain ◽  
Contractile Proteins ◽  
Light Chains ◽  
Myosin Heavy Chains ◽  
Perfused Heart ◽  
Precursor Pool ◽  
Heavy Chains ◽  
Cardiac Contractile ◽  
Specific Activities ◽  
Cardiac Contractile Proteins

The relative molar synthesis of cardiac contractile proteins has been measured in the perfused heart under control haemodynamic conditions. This synthesis, of myosin heavy chains, individual light chains (1 and 2), actin and tropomyosin, was determined from isolated guinea-pig hearts perfused for 3h simultaneously with constant specific radioactivities and concentrations of [3H]lysine and [3H]phenylalanine.The data strongly suggest that all of the proteins studied were synthesized from the same precursor pools of lysine and phenylalanine, since the ratio of the specific activities of the two labels was the same in all of the proteins. Measurement of molar synthesis of each contractile protein was the same with either labelled amino acid. Under control haemodynamic-perfusion conditions, the relative molar synthesis of the contractile proteins was actin greater than heavy chains greater than light chain 2 greater than light chain 1 greater than tropomyosin.

scholarly journals AN IDIOTYPIC CROSS-REACTION BETWEEN ALLOTYPE a3 AND ALLOTYPE a NEGATIVE RABBIT ANTIBODIES TO STREPTOCOCCAL CARBOHYDRATE

1973 ◽  
Vol 137 (3) ◽  
pp. 636-648 ◽  
Author(s):  
Thomas J. Kindt ◽  
David G. Klapper ◽  
Michael D. Waterfield
Keyword(s):  
Chemical Analysis ◽  
Cross Reaction ◽  
The Other ◽  
Light Chains ◽  
Binding Affinities ◽  
Variable Regions ◽  
Heavy Chains ◽  
Relative Binding ◽  
Group A

Two antibodies to Group C streptococcal carbohydrate isolated from an individual rabbit had similar relative binding affinities for a Group C immuno-adsorbent column. Their light chains were similar, if not identical, as were the constant regions of their heavy chains. Differences in the variable regions of the H chains of the two antibodies were detected by chemical analysis. The two antibodies had serologically identical idiotypic determinants although one antibody possessed the a3 allotype and the other had no detectable group a marker. The occurrence of such antibodies indicates the absence of obligatory associations between group a allotypes and idiotypic specificities, despite the fact that both determinants have antigenic components in the VH region of the H chain.

Cardiac myosin heavy chains in mice treated with NG-nitro-l-arginine methyl ester and thyroxine

2013 ◽  
Vol 23 (5) ◽  
pp. 1639-1644 ◽  
Author(s):  
Mukhallad A. M. Mohammad ◽  
Muhanad S. Abdelwahab ◽  
Mohamad M. J. Mohamad ◽  
Othman El shboul ◽  
Waleed R. Ezzat
Keyword(s):  
Methyl Ester ◽  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Heavy Chains
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