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Chapter 14 : Surface Structures of Group B Streptococci Important in Human Immunity

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Abstract:

The seminal findings by Rebecca Lancefield and coworkers on the role of carbohydrate and protein antigens in group B streptococcus (GBS) immunity have led a generation of researchers not only to a better understanding of these antigens in immunity but also toward the development of effective vaccine. This chapter highlights critical advances in our understanding of the role(s) of GBS surface antigens (namely, the group B carbohydrate, the type-specific capsular polysaccharides [CPSs], and proteins) in immunity and their application as components of experimental vaccines. With few exceptions, all strains of GBS isolated from humans are encapsulated and can be classified on the basis of serology and CPS structure. Nine distinct GBS serotypes have thus far been identified: Ia, Ib, II, III, IV, V, VI, VII, and VIII. In the past, serotypes Ia, Ib, II, and III were equally prevalent in normal vaginal carriage and early-onset sepsis. The protein antigens of GBS discussed are alphalike proteins, beta C protein, and other surface proteins.

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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Image of FIGURE 1
FIGURE 1

Proposed structure of the group B carbohydrate antigen, as modified from reference 98. The dashed line indicates that the linkage between the group B carbohydrate and the cell wall has not been discerned.

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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Image of FIGURE 2
FIGURE 2

Immunogold-labeled electron micrographs showing surface localization of type Ia CPS (A) and the alpha C protein (B) of GBS strain A909. For CPS type Ia staining, rabbit antiserum to the CPS, followed by 20-nm-diameter-gold-labeled protein A, was used. For alpha C protein, rabbit antiserum to the purified one-repeat alpha C protein, followed by 15-nm-diameter-gold-labeled protein A, was used. Bar, 500 nm. (Reproduced from Infection and Immunity [ ] with permission.)

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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Image of FIGURE 3a
FIGURE 3a

Chair models of the repeating units of GBS capsular polysaccharides.

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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Image of FIGURE 3b
FIGURE 3b

Chair models of the repeating units of GBS capsular polysaccharides.

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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Image of FIGURE 3c
FIGURE 3c

Chair models of the repeating units of GBS capsular polysaccharides.

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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Image of FIGURE 4
FIGURE 4

Schematic of gene clusters in all nine GBS serotypes. Conserved genes are depicted by white arrows. Variable genes are depicted by black arrows. The variable gap in the center of the clusters was introduced to permit alignment of homologous genes ( ).

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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Image of FIGURE 5
FIGURE 5

Comparison of the Rib and alpha C proteins. Overall structure of Rib from strain BM110 and alpha C protein from strain A909 and degree of amino acid residue identity between different regions of the proteins. S, signal peptide; N, NH-terminal region; R, one repeat; P, partial repeat; C, COOH-terminal region. The number of amino acids in each region is indicated. The Rib protein has 12 repeats of 79 amino acids, and the alpha C protein has 9 repeats of 82 amino acids. (Reproduced from the Journal of Biological Chemistry [ ] with permission.)

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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Image of FIGURE 6
FIGURE 6

Mouse models of group B streptococcal disease. The immunogenicity and efficacy of GBS vaccines have been evaluated with the maternal vaccination-neonatal mouse model by actively vaccinating female mice, mating these mice, and subsequently challenging their offspring with GBS (top timeline). In a passive vaccination-protection model (bottom timeline), newborn pups born to dams that received immune sera during pregnancy are challenged with GBS as a means of measuring the functional capacity of IgG. The therapeutic potential of GBS vaccine-induced serum (middle timeline) has been ascertained by inoculating naive pups with GBS 4 h before administration of immune sera. In all three models, pups are infected or challenged with GBS within 24 to 48 h of birth, and survival is assessed 48 h after challenge.

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
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107. Paoletti, L. C.,, J. Pinel,, A. K. Rodewald,, and D. L. Kasper. 1997. Therapeutic potential of human antisera to group B streptococcal glycoconjugate vaccines in neonatal mice. J. Infect. Dis. 175: 1237 1239.
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Tables

Generic image for table
TABLE 1

Characteristics of selected group B streptococcal protein antigens

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
Generic image for table
TABLE 2

Characteristics of group B streptococcal conjugate vaccines

Adipic acid dihydrazide.

Carbodiimide reduction.

14 pentasaccharide repeating units.

Monomeric tetanus toxoid.

6-Aminohexyl-1-β-D-galactopyranoside.

Reductive amination using sodium cyanoborohydride.

Via aldehydes formed on a selected number of sialic acid residues.

6 and 25 pentasaccharide repeating units.

GBS beta C protein.

GBS alpha C protein.

Cross-reactive material, a diphtheria mutant toxoid isolated from

Recombinant cholera B toxin.

Recombinant duck hepatitis B core antigen.

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14
Generic image for table
TABLE 3

Effect of covalent attachment of polysaccharide to protein on the efficacy in mice of group B streptococcal polysaccharide conjugate vaccines

Female outbred mice received a priming dose of vaccine emulsified with complete Freund's adjuvant and were mated 2 weeks later. A booster dose of vaccine was administered with imcomplete Freund's adjuvant 3 weeks after the priming dose. Newborn pups (<36 h old) were challenged with an ordinarily lethal dose of GBS type III strain M781, and survival was assessed 48 h later. All groups received 1 μg per dose of type III capsular polysaccharide, either uncoupled (III CPS) or covalently coupled (III-TT) to or admixed with (III+TT) tetanus toxoid.

Citation: Madoff L, Paoletti L, Kasper D. 2006. Surface Structures of Group B Streptococci Important in Human Immunity, p 169-185. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch14

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