Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity.

Jürgens, Dagmar; Sterzik, B; Fehrenbach, F. J.

doi:10.1084/jem.165.3.720

Cited by 72 publications

(60 citation statements)

References 39 publications

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“…Osmotic protection experiments using polyethelyne glycol and recombinant CAMP suggest that porins formed on the surface of sheep RBC are larger than 1.6 nm, whereas pores observed on electron microscopy are 12-16 nm in diameter (73). CAMP protein also binds weakly to the Fc portion of human IgG and IgM (74).…”

Section: Camp Factormentioning

confidence: 99%

“…Skalka and colleagues produced mortality in rabbits and mice by direct injection of partially purified CAMP preparation (75). Jurgens et al, also working in the murine model, induced septicemia and death when CAMP was coadministered with a sublethal dose of GBS (74). It is unknown whether the cytolytic or immunoglobulin-binding properties of CAMP factor, or both, may contribute to disease pathogenesis.…”

Section: Camp Factormentioning

confidence: 99%

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Extracellular virulence factors of group B Streptococci

Liu

Nizet²

2004

Front Biosci

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Section: Camp Factormentioning

confidence: 99%

Section: Camp Factormentioning

confidence: 99%

Extracellular virulence factors of group B Streptococci

Liu

Nizet²

2004

Front Biosci

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“…CAMP factor was found to bind to the F c fragments of immunoglobulins, and it was therefore designated as protein B in analogy to protein A of S. aureus (9).…”

mentioning

confidence: 99%

Characterization of Streptococcus agalactiae CAMP Factor as a Pore-forming Toxin

Lang

Palmer

2003

Journal of Biological Chemistry

106

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A recombinant form of CAMP factor of Streptococcus agalactiae has been expressed as glutathione S-transferase-CAMP fusion protein in Escherichia coli. After thrombin cleavage of the fusion protein, the recombinant CAMP factor exhibited hemolytic activity comparable with that of the native form. Osmotic protection experiments with polyethylene glycols show that CAMP factor forms discrete transmembrane pores with a diameter upward of 1.6 nm on susceptible membranes; electron microscopy reveals circular membrane lesions of heterogeneous size, up to 12-15 nm in diameter. Liposome permeabilization studies show that pore formation is a highly cooperative process, which suggests that it involves the oligomerization of CAMP factor. Chemical cross-linking experiments also support an oligomeric mode of action.The CAMP reaction consists of a distinct zone of hemolysis on blood agar plates produced by Streptococcus agalactiae when grown near the colonies of Staphylococcus aureus (1). It has been used in diagnostic microbiology to identify the S. agalactiae strains ever since its discovery in 1944 by Christie et al. (1). The proteins responsible for the CAMP reaction are sphingomyelinase from S. aureus and CAMP factor, a protein secreted by S. agalactiae that has a molecular weight of 25 kDa and a pI of 8.9 (2). Sphingomyelinase initially hydrolyzes sphingomyelin to ceramide, which renders the erythrocytes susceptible to the lytic activity of CAMP factor. Erythrocytes from different mammalian species support the CAMP reaction to different extents depending on the sphingomyelin content in their cell membranes (3). Sheep red blood cells are the most susceptible, in keeping with their sphingomyelin content as high as 51% (by moles) (4). Human red blood cells and rabbit red blood cells, with 26 and 19% mol of sphingomyelin, respectively (4, 5), were reportedly not sensitive to CAMP factor after sphingomyelinase treatment (3). The latter, however, were rendered susceptible to the CAMP factor after phospholipase C treatment, which converted the glycerophospholipids to diacylglycerol (6), indicating that ceramide is not specifically required for CAMP activity. Previous work with liposomes also suggested that the fraction of cholesterol in the membrane influences the activity of CAMP factor (6, 7). CAMP factor has long been known as a pathogenic determinant that exerted lethal effects when administered to rabbits and mice (8). Apart from its membrane damaging activity, CAMP factor was found to bind to the F c fragments of immunoglobulins, and it was therefore designated as protein B in analogy to protein A of S. aureus (9).The CAMP factor genes of S. agalactiae (10), Streptococcus uberis (11), and Streptococcus pyogenes (12) have been cloned in Escherichia coli, and their sequences were found to be highly homologous with each other (12). Co-hemolytic phenomena have also been reported with various other bacterial genera, but the proteins responsible for those, although sometimes referred to by the name "CAMP factor" as well, are not...

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“…Binding of protein B causes disorganization of the lipid bilayer of the cell membrane to an extent that results in cell lysis (4). The in vivo function of protein B has not been disclosed yet; however, the hemolytic activity seems to be an epiphenomenon (19,27). Binding of this protein to the Fc region of immunoglobulins has been demonstrated (12,19), and the protein seems to be lethal to rabbits and mice (30).…”

mentioning

confidence: 99%

“…The in vivo function of protein B has not been disclosed yet; however, the hemolytic activity seems to be an epiphenomenon (19,27). Binding of this protein to the Fc region of immunoglobulins has been demonstrated (12,19), and the protein seems to be lethal to rabbits and mice (30). Protein B seems to be essential for S. agalactiae, as the cfb gene encoding this protein (24) was found to be universally present in the genomes of 162 GBS strains from different geographic areas (20).…”

mentioning

confidence: 99%

Method for Quantitative Detection and Presumptive Identification of Group B Streptococci on Primary Plating

Hansen

Sørensen

2003

J Clin Microbiol

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Maternal prenatal screening for group B streptococci (GBS) followed by offering of intrapartum chemoprophylaxis to carriers is one of the strategies used to reduce the incidence of neonatal early-onset GBS infections. Culturing of vaginal and anorectal swab specimens in selective broth is the screening procedure recommended by the Centers for Disease Control and Prevention. This technique is sensitive; it does not, however, allow either evaluation of the degree of colonization or detection of cocolonization with several GBS clones. We have examined the carriage rate and population dynamics of GBS in a group of Danish women during pregnancy and 1 year after delivery using a new detection method. In the present paper we describe a mixed blood agar medium (MB agar) that identifies GBS in the primary cultures by detection of a double hemolysis pattern consisting of characteristic, large zones of partial hemolysis ("CAMP zones") and of narrow zones of complete hemolysis. The MB agar was at least as sensitive as culturing in selective broth for detection of GBS in vaginal and anorectal swab specimens, and GBS strains could be identified directly on the primary plate due to the CAMP zones without the need for subculturing. The carriage rate of GBS in a group of Danish women was found to be more than 30%, a figure considerably higher than the rate that was reported previously.

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Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity.

Cited by 72 publications

References 39 publications

Extracellular virulence factors of group B Streptococci

Extracellular virulence factors of group B Streptococci

Characterization of Streptococcus agalactiae CAMP Factor as a Pore-forming Toxin

Method for Quantitative Detection and Presumptive Identification of Group B Streptococci on Primary Plating

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