On the physiological functions of teichoic acids

Tomasz, Alexander; Westphal, Monika; Briles, Eve Barak; Fletcher, Paul W.

doi:10.1002/jss.400030102

Cited by 56 publications

(41 citation statements)

References 11 publications

(8 reference statements)

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“…Pneumococci display an unusual surface molecule, phosphocholine, on the cell wall teichoic acid and the membranebound lipoteichoic acid (154). Studies have shown that PspA attaches itself to S. pneumoniae by noncovalent binding to the choline of both lipoteichoic and teichoic acids via its C-terminal end, consisting of the repeat region, also called the choline binding region (CBR) (Fig.…”

Section: Attachment To the Surface Of S Pneumoniaementioning

confidence: 99%

Pneumococcal Virulence Factors: Structure and Function

Jedrzejas

2001

Microbiol Mol Biol Rev

407

354

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The overall goal for this review is to summarize the current body of knowledge about the structure and function of major known antigens of Streptococcus pneumoniae, a major gram-positive bacterial pathogen of humans. This information is then related to the role of these proteins in pneumococcal pathogenesis and in the development of new vaccines and/or other antimicrobial agents. S. pneumoniae is the most common cause of fatal community-acquired pneumonia in the elderly and is also one of the most common causes of middle ear infections and meningitis in children. The present vaccine for the pneumococcus consists of a mixture of 23 different capsular polysaccharides. While this vaccine is very effective in young adults, who are normally at low risk of serious disease, it is only about 60% effective in the elderly. In children younger than 2 years the vaccine is ineffective and is not recommended due to the inability of this age group to mount an antibody response to the pneumococcal polysaccharides. Antimicrobial drugs such as penicillin have diminished the risk from pneumococcal disease. Several pneumococcal proteins including pneumococcal surface proteins A and C, hyaluronate lyase, pneumolysin, autolysin, pneumococcal surface antigen A, choline binding protein A, and two neuraminidase enzymes are being investigated as potential vaccine or drug targets. Essentially all of these antigens have been or are being investigated on a structural level in addition to being characterized biochemically. Recently, three-dimensional structures for hyaluronate lyase and pneumococcal surface antigen A became available from X-ray crystallography determinations. Also, modeling studies based on biophysical measurements provided more information about the structures of pneumolysin and pneumococcal surface protein A. Structural and biochemical studies of these pneumococcal virulence factors have facilitated the development of novel antibiotics or protein antigen-based vaccines as an alternative to polysaccharide-based vaccines for the treatment of pneumococcal disease

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Section: Attachment To the Surface Of S Pneumoniaementioning

confidence: 99%

Pneumococcal Virulence Factors: Structure and Function

Jedrzejas

2001

Microbiol Mol Biol Rev

407

354

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“…The ethanolamine-containing cell wall (R6EA) was prepared by an identical procedure, except that choline was replaced by 20 μg/ml ethanolamine (Sigma-Aldrich) in the growth medium (49).…”

Section: Figurementioning

confidence: 99%

Bacterial programmed cell death of cerebral endothelial cells involves dual death pathways

Bermpohl¹,

Halle²,

Freyer³

et al. 2005

J. Clin. Invest.

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Major barriers separating the blood from tissue compartments in the body are composed of endothelial cells. Interaction of bacteria with such barriers defines the course of invasive infections, and meningitis has served as a model system to study endothelial cell injury. Here we report the impressive ability of Streptococcus pneumoniae, clinically one of the most important pathogens, to induce 2 morphologically distinct forms of programmed cell death (PCD) in brain-derived endothelial cells. Pneumococci and the major cytotoxins H 2 0 2 and pneumolysin induce apoptosis-like PCD independent of TLR2 and TLR4. On the other hand, pneumococcal cell wall, a major proinflammatory component, causes caspase-driven classical apoptosis that is mediated through TLR2. These findings broaden the scope of bacterial-induced PCD, link these effects to innate immune TLRs, and provide insight into the acute and persistent phases of damage during meningitis.

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“…Since previous examinations of wall turnover in pneumococci had utilized either [3H]choline-labelled teichoic acid or peptidoglycan labelled with either ['4C]glutamic acid or [14C]lysine during growth in ethanolamine-containing medium [IS,16a], it was necessary to establish that lysine-labelled peptidoglycan synthesized in the usual choline-containing medium was also conserved and that release of cell wall label did not complicate the interpretation of peptidoglycan synthesis experiments. Exponential phase cultures of wild type, autolysis prone R 6 and the autolysis deficient strain lyt 4-4 were pulse labeled (3 min) with [3H]lysine (1 pCi/ml, 0.19 ng/ ml) and subsequently grown with an excess of unlabelled lysine (225 pg/ml) added immediately after the pulse.…”

Section: Analysis Of Pep T Idogly Can T Urno Ver During Growthmentioning

confidence: 99%

Inhibition of cell wall synthesis and acylation of the penicillin binding proteins during prolonged exposure of growing Streptococcus pneumoniae to benzylpenicillin

Williamson

Tomasz

1985

Eur J Biochem

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Growing cultures of an autolysis‐defective pneumococcal mutant were exposed to [3H]benzylpenicillin at various multiples of the minimal inhibitory concentration and incubated until the growth of the cultures was halted. During the process of growth inhibition, we determined the rates and degree of acylation of the five penicillin‐binding proteins (PBPs) and the rates of peptidoglycan incorporation, protein synthesis, and turbidity increase. The time required for the onset of the inhibitory effects of benzylpenicillin was inversely related to the concentration of the antibiotic, and inhibition of peptidoglycan incorporation always preceded inhibition of protein synthesis and growth. When cultures first started to show the onset of growth inhibition the same characteristic fraction of each PBP was in the acylated form in all cases, irrespective of the antibiotic concentration. Apparently, saturation of one or more PBPs with the antibiotic beyond these threshold levels is needed to bring about interference with normal peptidoglycan production and celluar growth. Although it was not possible to correlate the inhibition of cell wall synthesis or cell growth with the degree of acylation (percentage saturation) of any single PBP, there was a correlation between the amount of peptidoglycan synthesized and the actual amount of PBP 2b that was not acylated. In cultures exposed to benzylpenicillin concentrations greater than eight times the minimal inhibitory concentration, the rates of peptidoglycan incorporation underwent a rapid decline when bacterial growth stopped. However, in cultures exposed to lower concentrations of benzylpenicillin (one to six times the minimal inhibitory concentration) peptidoglycan synthesis continued at constant rate for prolonged periods, after the turbidity had ceased to increase. We conclude that inhibition of bacterial growth does not require a complete inhibition or even a major decline in the rate of peptidoglycan incorporation. Rather, inhibition of growth must be caused by an as yet undefined process that stops cell division when the rate of incorporation of peptidoglycan (or synthesis of protein) falls below a critical value.

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On the physiological functions of teichoic acids

Cited by 56 publications

References 11 publications

Pneumococcal Virulence Factors: Structure and Function

Pneumococcal Virulence Factors: Structure and Function

Bacterial programmed cell death of cerebral endothelial cells involves dual death pathways

Inhibition of cell wall synthesis and acylation of the penicillin binding proteins during prolonged exposure of growing Streptococcus pneumoniae to benzylpenicillin

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