Reaction Components Influencing CAMP Factor Induced Lysis

Sterzik, B; Fehrenbach, F. J.

doi:10.1099/00221287-131-4-817

Cited by 12 publications

(16 citation statements)

References 14 publications

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“…The CAMP effect involves at least two individual membrane-active components interacting sequentially with the erythrocyte membrane, which contains at least 45 mol% sphingomyelin (26). The first step involves a nonlytic hydrolysis of membrane sphingomyelin and phospholipids by sphingomyelinase or phospholipase (7).…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of CAMP Cohemolysin as a Potential Virulence Factor of Riemerella anatipestifer

et al. 2002

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Riemerella anatipestifer is responsible for exudative septicemia in ducks. The genetic determinant of the CAMP cohemolysin, cam, from a strain of R. anatipestifer was cloned and expressed in Escherichia coli. Chromosomal DNA from serotype 19 strain 30/90 was used to construct a gene library in pBluescript II SK(؊) vector in E. coli XL-1-Blue strain. The clones containing recombinant plasmids were screened for the CAMP reaction with Staphylococcus aureus. Those that showed cohemolysis were chosen for further analysis by sequencing. One of these clones, JFRA8, was subcloned to identify the smallest possible DNA fragment containing the CAMP cohemolysin determinant, which was located on a 3,566-bp BamHI-BstXI fragment which specified a 1,026-bp open reading frame. Clones containing recombinant plasmids carrying cam obtained by PCR cloning into E. coli M15 strain secreted an active CAMP cohemolysin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analyses confirmed that the recombinant strain expressed a protein with a molecular mass of 37 kDa and that strains from serotypes 1, 2, 3, 5, 6, and 19 expressed the cohemolysin. The deduced amino acid sequence showed high homology to those of O-sialoglycoprotein endopeptidases. Hydrolysis of radioiodinated glycophorin A confirmed that Cam is a sialoglycoprotease.

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Section: Discussionmentioning

confidence: 99%

Identification and Characterization of CAMP Cohemolysin as a Potential Virulence Factor of Riemerella anatipestifer

et al. 2002

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“…Protein B may cause lysis of ␤-toxin-modified RBCs, as mentioned above; however, only cells containing more than 45 mol% of sphingomyelin in the plasma membrane are sensitive to the combined actions of the staphylococcal toxin and pro-tein B (31). Thus, the CAMP reaction is seen on agar plates prepared from bovine RBCs and SRBCs, whereas RBCs from humans, rabbits, and guinea pigs and horse RBCs (HRBCs) are not lysed (8,31).…”

mentioning

confidence: 99%

“…Thus, the CAMP reaction is seen on agar plates prepared from bovine RBCs and SRBCs, whereas RBCs from humans, rabbits, and guinea pigs and horse RBCs (HRBCs) are not lysed (8,31).…”

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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“…When erythrocytes from different mammalian species were compared, CAMP factor was found to be considerably more active on sheep red cells than on bovine ones, although the membranes of both of these have virtually the same sphingomyelin content [26]. Human red cells, which contain little sphingomyelin but a high amount of phosphatidylcholine (PC), can be rendered sensitive by treatment with phospholipase C [9], suggesting that the diacylglycerol produced by such treatment may replace ceramide, and therefore that the effect of either is of low specificity.…”

mentioning

confidence: 94%

Streptococcus agalactiae CAMP factor binds to GPI-anchored proteins

Lang

Xue

Guo

et al. 2006

Med Microbiol Immunol

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CAMP factor (protein B) is a pore-forming protein secreted by Streptococcus agalactiae. It causes lysis of sheep red blood cells when these have been sensitized with staphylococcal sphingomyelinase. We here show that CAMP factor binds to GPI-anchored proteins, and that this interaction involves the carbohydrate core of the GPI-anchor. Enzymatic cleavage of GPI-anchors with phosphatidylinositol-specific phospholipase C strongly reduces the sensitivity of erythrocytes to CAMP factor. Incorporation of alkaline phosphatase, a model GPI-anchored protein, into liposome membranes renders the latter susceptible to permeabilization by CAMP factor. GPI-anchored proteins therefore function as cellular receptors for CAMP factor.

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Reaction Components Influencing CAMP Factor Induced Lysis

Cited by 12 publications

References 14 publications

Identification and Characterization of CAMP Cohemolysin as a Potential Virulence Factor of Riemerella anatipestifer

Identification and Characterization of CAMP Cohemolysin as a Potential Virulence Factor of Riemerella anatipestifer

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

Streptococcus agalactiae CAMP factor binds to GPI-anchored proteins

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