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Chapter 13 : Interactions of with the Proteins of the Complement Pathways

Author: Margaret K. Hostetter1
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Affiliations: 1: Department of Pediatrics, Yale University School of Medicine, 333 Cedar Street, LMP 4085, P.O. Box 208064, New Haven, CT 06520-8064
Content Type: Monograph
Publication Year: 2004

Category: Bacterial Pathogenesis; Clinical Microbiology

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Interactions of with the Proteins of the Complement Pathways, Page 1 of 2

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Abstract:

Thirty-three years later, the heat-stable, specific components of the opsonic interaction (antibodies) were distinguished from nonspecific, heat-labile serum proteins, now named complement. In the presence of antibody alone, the rate of neutrophil phagocytosis of serotype 3 was accelerated more than sevenfold by the addition of active complement proteins in fresh human serum. Mannose binding lectin (MBL), a member of the collectin family, exhibits the collagen-like domain and the carbohydrate recognition domain of the collectin family. The most compelling evidence for the role of innate immunity in defense against pneumococcal infection focuses on C3. Recent genetic investigations have identified a number of pneumococcal proteins that affect the activation, deposition, or cleavage of C3 so as to interfere with C3-mediated opsonization and phagocytosis. Deleting the choline-binding region of the family 2 PspA generated a mutant that failed to bind human lactoferrin but retained most of its complement deposition. Virulence was moderately attenuated. The gene is present in 75% or more of pneumococcal strains, but the encoded proteins are highly polymorphic and are divided into 11 groups. Studies of type 3 pneumococci, highly resistant to phagocytosis, also pointed to absorption of factor H from plasma and led to the isolation of Hic. Pneumococcal proteins that interact with components of the classical or alternative complement pathways are predominantly surface expressed (except for Pla), related if not completely conserved (e.g., CbpA, PspA, PspC, and Hic), and potently immunogenic.

Citation: Hostetter M. 2004. Interactions of with the Proteins of the Complement Pathways, p 201-210. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch13
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Interactions of Streptococcus pneumoniae with the Proteins of the Complement Pathways
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Citation: Hostetter M. 2004. Interactions of with the Proteins of the Complement Pathways, p 201-210. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch13
/content/10.1128/9781555816537.chap13.fig13-1
FIGURE 1

Diagram of complement-mediated opsonization and phagocytosis. AB, antibody.

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10.1128/9781555816537/fig13-1.gif
Image of FIGURE 1
FIGURE 1

Diagram of complement-mediated opsonization and phagocytosis. AB, antibody.

Citation: Hostetter M. 2004. Interactions of with the Proteins of the Complement Pathways, p 201-210. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch13
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References

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Tables

Interactions of Streptococcus pneumoniae with the Proteins of the Complement Pathways
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Citation: Hostetter M. 2004. Interactions of with the Proteins of the Complement Pathways, p 201-210. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch13
/content/10.1128/9781555816537.chap13.tab13-1
TABLE 1

Interactions of pneumococcal components with complement proteins

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10.1128/9781555816537/tab13-1.gif
Generic image for table
TABLE 1

Interactions of pneumococcal components with complement proteins

Citation: Hostetter M. 2004. Interactions of with the Proteins of the Complement Pathways, p 201-210. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch13

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