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The streptococci are classified as beta-hemolytic if complete hemolysis of the blood cells in the agar surrounding the colonies is observed, alpha-hemolytic if a characteristic greenish color is seen, or nonhemolytic if the blood cells are not affected. This chapter mainly focuses on the group A streptococci () that cause a large number of different disease syndromes. The group A streptococci are the causative agents of several serious diseases, such as necrotizing fasciitis, scarlet fever, sepsis, and a recently recognized toxic shock-like syndrome, as well as suppurative infections of the skin and throat , such as impetigo, erysipelas, and pharyngitis ("strepthroat") . A number of surface structures have been implicated as virulence factors of the group A streptococci. M protein is considered t h e major virulence factor of group A streptococci () because it protects the bacteria from phagocytosis by polymorphonuclear leukocytes. Infection by causes production of antibodies that include those that react with M protein. The M protein or a derivative of it is being considered as a possible antistreptococcus vaccine. A greater understanding of the relation of the structure of the M protein to its function should help in the rational design of an antistreptococcal vaccine and should also increase our understanding of the way in which coiled-coil fibrous proteins can act.

Citation: Scott J, Caparon M. 1993. , p 53-63. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch4
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Figure 1

The M protein of the group A streptococcus. The left half of the figure is a schematic representation of the dimeric coiled-coil M-protein molecules and the streptococcal cell wall. M-protein dimers, cell membrane, cytoplasm, peptidoglycan (cell wall), and group A-specific carbohydrate(s) are shown. The right half of the figure shows the domains of the M6.1 protein, which has served as a prototype for the structures of all M proteins. The brackets between the two halves of the figure indicate the locations of the main structural features of the M molecule. Shown is the cell wall-associated region, which remains after trypsin digestion of streptococcal cells; the helical rod region, which forms the coiled-coil structure; and the nonhelical amino terminus (N), which is the region most distal to the streptococcal cell wall. Specific domains of the M6 molecule are shown, including the five A repeats of 14 amino acids each, the five B repeats of 25 amino acids each, and the two C repeats of 27 amino acids each. Also shown is the anchor domain, which consists of the carboxy-terminal (C) cytoplasmic charged tail, a membrane-spanning hydrophobic region, and a flexible region rich in proline and glycine residues that traverses the cell wall. LPSTGE indicates the location of an amino acid motif conserved among many gram-positive surface proteins that is also found in eukaryotic proteins attached to membranes by a GPI linkage. The arrow at Pepsin indicates the site at which the M molecule is cleaved preferentially by pepsin. Brackets on the far right of the figure show locations of the three major domains of all M-protein molecules: the polymorphic N terminus, the hypervariable coiled-coil domain, and the conserved domain, which is highly similar among the different M proteins that have been studied.

Citation: Scott J, Caparon M. 1993. , p 53-63. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch4
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Image of Figure 2
Figure 2

Model for the roles of different proteins in the attachment of to epithelial cells. (A) Chains composed of individual streptococcal cells are shown in the process of attaching to an epithelial cell. Both M protein (↓) and protein F (↑), a fibronectin-binding protein, are shown on the surface of the streptococcal cells. Molecules of fibronectin (symbol here) are shown on the surface of the epithelial cell. The streptococcal chain in the center of the figure has adhered to the epithelial cell by a mechanism that involves the binding of protein F to a molecule of fibronectin. (B) Once a chain of streptococci has attached by its protein F to a tonsillar epithelial cell, the M protein of the attached organisms interacts with other streptococci to cause bacterial aggregation. This type of M-protein-mediated interstreptococcal interaction may contribute to colonization of the host.

Citation: Scott J, Caparon M. 1993. , p 53-63. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch4
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