Preparation of antigens and immunoadsorbents corresponding to the Streptococcus group a cell-wall polysaccharide

1996 ◽  
Vol 4 (11) ◽  
pp. 2003-2010 ◽  
Author(s):  
France-Isabelle Auzanneau ◽  
B.Mario Pinto
1972 ◽  
Vol 18 (1) ◽  
pp. 93-96 ◽  
Author(s):  
S. E. Read ◽  
R. W. Reed

The replicative events of a virulent phage (A25) infection of a group A Streptococcus (T253) were studied using the electron microscope. The first intracellular evidence of phage replication in a cell occurred 30 min after infection with arrest of cell division and increase in the nucleic acid pool. Phage heads were evident in the nucleic acid pool of the cells 45 min after infection. Release of phages occurred by splitting of the cell wall along discrete lines. This appeared to be at sites of active wall synthesis, i.e., near the region of septum formation. Many phage components were released but relatively few complete phages indicating a relatively inefficient replicative system.


2005 ◽  
Vol 73 (10) ◽  
pp. 6383-6389 ◽  
Author(s):  
Francis Michon ◽  
Samuel L. Moore ◽  
John Kim ◽  
Milan S. Blake ◽  
France-Isabelle Auzanneau ◽  
...  

ABSTRACT A number of epitope specificities associated with the cell wall polysaccharide antigen of group A streptococci were identified in a polyclonal rabbit antiserum induced in rabbits by whole group A streptococci and in polyclonal convalescent human antisera from children that had recovered from streptococcal A infections. The identification was achieved by using a series of synthetic oligosaccharides, glycoconjugates, and bacterial polysaccharide inhibitors to inhibit the binding of the group A helical polysaccharide to the polyclonal antisera. The exclusively dominant epitope expressed in the convalescent human antisera was the doubly branched extended helical hexasaccharide with the structure α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap(1→3)α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap. The hexasaccharide epitope also bound with the highest immunoreactivity to the rabbit antiserum. In contrast, the human antisera did not show significant binding to the singly branched pentasaccharide with the structure α-l-Rhap(1→2)α-l-Rhap(1→3)α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap or the branched trisaccharide α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap, although both these haptens bound significantly to the same rabbit antiserum, albeit with less immunoreactivity than the hexasaccharide. Inhibition studies using streptococcal group A and B rabbit antisera and the inhibitors indicated above also suggested that the group A carbohydrate, unlike the group B streptococcal polysaccharide, does not contain the disaccharide α-l-Rhap(1→2)α-l-Rhap motif at its nonreducing chain terminus, stressing the importance of mapping the determinant specificities of these two important streptococcal subcapsular group polysaccharides to fully understand the serological relationships between group A and group B streptococci.


1963 ◽  
Vol 117 (3) ◽  
pp. 377-399 ◽  
Author(s):  
Earl H. Freimer

Intact bacterial membranes have been isolated from protoplasts prepared from Group A streptococci by a cell wall-dissolving enzyme. A membrane fraction with identical chemical and serological properties has been obtained by differential centrifugation of mechanically disrupted streptococci. The membrane is chemically distinct from the cell wall and is composed of 72 per cent protein, 26 per cent lipid, and 2 per cent carbohydrate. Capillary precipitin tests and analysis by microdiffusion have demonstrated that the membrane contains antigens distinct from those of the cell wall and from those of the cytoplasm which it envelops. Evidence is presented which demonstrates that this antigenic material is common to the membranes of Group A streptococci, and that it can be distinguished by immunodiffusion from related antigenic substances present in membranes of several other serological groups of hemolytic streptococci. This antigenic material does not cross-react with the membrane antigens of other Gram-positive cocci.


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