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Chapter 4 : Choline-Binding Proteins

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Abstract:

Pneumococci covalently link phosphorylcholine to teichoic and lipoteichoic acids found in the peptidoglycan and cytoplasmic membrane, respectively. The functions of most of the choline-binding proteins (CBPs) are unknown, but a few have been studied in some depth and it is apparent that they have a role in pathogenesis and can be protective immunogens. The presence of choline-binding domains implies that any protein expressing these domains is secreted, since choline is a constituent of teichoic and lipoteichoic acids, which are cell surface polymers. The major pneumococcal autolysin LytA contains four to six choline-binding domains but is not found in eluates of pneumococcal strain Rx1 incubated with choline-containing buffers. Pneumococcal CBPs have been shown to play a role in pathogenesis in various murine models of disease. It is likely that there is some redundancy in the function of CBPs, and this, along with the large effect of the pneumococcal capsule, may explain why more is not known about the function of CBPs in pneumococcal disease. PspA and PspC are the two most well-characterized CBPs in terms of their biological functions and roles in disease. While these two proteins can be considered paralogs based on sequence homology, they make distinct contributions to pneumococcal virulence. The major autolysin of pneumococci, designated LytA, is known to be important in remodeling the cell wall of dividing pneumococci and is the common final point for many processes which lead to cell lysis.

Citation: Swiatlo E, McDaniel L, Briles D. 2004. Choline-Binding Proteins, p 49-60. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch4
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Figures

Image of FIGURE 1
FIGURE 1

General organization of PspA and PspC from the nonencapsulated strain Rx1. PspA contains 619 amino acid residues, and PspC contains 923. The strains contain an identical 31-amino-acid leader peptide at the amino terminus, followed by an α-helical domain that varies in length. In PspA a sequence of about 100 amino acids directly adjacent to the proline-rich domain defines specific clades. Arrows below PspC mark the locations of direct repeats in the α-helical domain. In both molecules a region rich in prolines follows the α-helix and is thought to interact with the cell wall. At the carboxyl terminus is a choline-binding domain containing 10 repeats of 20 amino acids each and a short “tail” of uncharged amino acids. The proline-rich and choline-binding domains of PspA and PspC have identical amino acid sequences as determined by all alleles sequenced to this point.

Citation: Swiatlo E, McDaniel L, Briles D. 2004. Choline-Binding Proteins, p 49-60. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch4
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Image of FIGURE 2
FIGURE 2

Schematic representation of CBPs in TIGR4, with the amino terminus at the far left. Diamonds represent choline-binding domains with homology to the consensus sequence, GWVKDNGTWYYLNSSGAMAT. Boxes within the structures represent domains with a high degree of homology to protein families in the Pfam database. RICH, rich in charged residues; CHAP, cysteine, histidine-dependent, amidohydrolase/peptidase. Boxes at the amino termini of some proteins designate potential cleavage sites of putative leader sequences.

Citation: Swiatlo E, McDaniel L, Briles D. 2004. Choline-Binding Proteins, p 49-60. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch4
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Image of FIGURE 3
FIGURE 3

Diagram of binding of sIgA via the secretory component and factor H (FH) to PspC. The host proteins bind to separate sites on the α-helical portion of PspC. Both are relatively large host proteins but do not compete for binding in in vitro assays, indicating that they bind separate sites. Simultaneous binding in vivo has not been demonstrated.

Citation: Swiatlo E, McDaniel L, Briles D. 2004. Choline-Binding Proteins, p 49-60. In Tuomanen E, Mitchell T, Morrison D, Spratt B (ed), The Pneumococcus. ASM Press, Washington, DC. doi: 10.1128/9781555816537.ch4
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