A Field Study of Naturally Occurring Specific Antibodies against Clostridium perfringens Alpha Toxin in Norwegian Broiler Flocks

ABSTRACT Clostridium perfringens mutant strain 121A/91 shows neither enzymatic (phospholipase C) nor hemolytic activity. Nevertheless, the cpa gene and the corresponding alpha-toxin variant are detectable. Vaccination with this genetically constructed alpha-toxin variant, rAT121/91, induces antibodies capable of significantly reducing activities induced by wild-type toxin. Thus, rAT121/91 could be a useful vaccine candidate.

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Immunization with a nontoxic naturally occurring Clostridium perfringens alpha toxin induces neutralizing antibodies in rabbits

Anaerobe ◽

10.1016/j.anaerobe.2017.12.004 ◽

2018 ◽

Vol 49 ◽

pp. 48-52 ◽

Cited By ~ 4

Author(s):

Flávia de Faria Siqueira ◽

Rodrigo Otávio Silveira Silva ◽

Anderson Oliveira do Carmo ◽

Bárbara Bruna Ribeiro de Oliveira-Mendes ◽

Carolina Campolina Rebello Horta ◽

...

Keyword(s):

Clostridium Perfringens ◽

Neutralizing Antibodies ◽

Alpha Toxin ◽

Naturally Occurring

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Naturally Occurring IgG Autoantibodies to Platelet Cytoskeleton Tropomyosin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650336 ◽

1996 ◽

Vol 75 (04) ◽

pp. 642-647 ◽

Cited By ~ 1

Author(s):

Ming Hou ◽

Dick Stockelberg ◽

Jack Kutti ◽

Hans Wadenvik

Keyword(s):

Molecular Weight ◽

Human Platelet ◽

Chronic Idiopathic Thrombocytopenic Purpura ◽

Thrombocytopenic Purpura ◽

Immunoblot Assay ◽

Specific Antibodies ◽

Platelet Protein ◽

Naturally Occurring ◽

Normal Individuals ◽

Cytoskeleton Protein

SummaryWe have observed that naturally occurring serum antibodies generated a 30 Kd band in a platelet immunoblot assay. The target protein had the same molecular weight (30 Kd) under nonreduced and reduced electrophoretic conditions, and could be immunoblotted from either autologous or homologous platelet lysates. Also, the 30 Kd reactive autoantibodies could be totally adsorbed by platelet cytoskeletons. From these data one likely candidate for the autoantibody target was the intracellular platelet protein tropomyosin. Indeed, a commercially available monoclonal antitropomyosin antibody reacted with proteins comigrating with this 30 Kd band; affinity purified human platelet tropomyosin was bound by the antibodies that recognized the 30 Kd protein. This body of evidence conclusively demonstrated that naturally occurring serum autoantibodies reacted with the platelet cytoskeleton protein - tropomyosin. These tropomyosin specific antibodies were found in roughly the same percentage of sera from patients with chronic idiopathic thrombocytopenic purpura (ITP) as from normal individuals.

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Perfringolysin O Expression in Clostridium perfringens Is Independent of the Upstream pfoR Gene

Journal of Bacteriology ◽

10.1128/jb.184.7.2034-2038.2002 ◽

2002 ◽

Vol 184 (7) ◽

pp. 2034-2038 ◽

Cited By ~ 5

Author(s):

Milena M. Awad ◽

Julian I. Rood

Keyword(s):

Escherichia Coli ◽

Homologous Recombination ◽

Gene Product ◽

Structural Gene ◽

Clostridium Perfringens ◽

Deletion Mutant ◽

Gas Gangrene ◽

Alpha Toxin ◽

Clostridial Myonecrosis ◽

Perfringolysin O

ABSTRACT The pathogenesis of Clostridium perfringens-mediated gas gangrene or clostridial myonecrosis involves the extracellular toxins alpha-toxin and perfringolysin O. Previous studies (T. Shimizu, A. Okabe, J. Minami, and H. Hayashi, Infect. Immun. 59:137-142, 1991) carried out with Escherichia coli suggested that the perfringolysin O structural gene, pfoA, was positively regulated by the product of the upstream pfoR gene. In an attempt to confirm this hypothesis in C. perfringens, a pfoR-pfoA deletion mutant was complemented with isogenic pfoA+ shuttle plasmids that varied only in their ability to encode an intact pfoR gene. No difference in the ability to produce perfringolysin O was observed for C. perfringens strains carrying these plasmids. In addition, chromosomal pfoR mutants were constructed by homologous recombination in C. perfringens. Again no difference in perfringolysin O activity was observed. Since it was not possible to alter perfringolysin O expression by mutation of pfoR, it was concluded that the pfoR gene product is unlikely to have a role in the regulation of pfoA expression in C. perfringens.

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The synergistic necrohemorrhagic action of Clostridium perfringens perfringolysin and alpha toxin in the bovine intestine and against bovine endothelial cells

Veterinary Research ◽

10.1186/1297-9716-44-45 ◽

2013 ◽

Vol 44 (1) ◽

pp. 45 ◽

Cited By ~ 26

Author(s):

Stefanie Verherstraeten ◽

Evy Goossens ◽

Bonnie Valgaeren ◽

Bart Pardon ◽

Leen Timbermont ◽

...

Keyword(s):

Endothelial Cells ◽

Clostridium Perfringens ◽

Alpha Toxin ◽

Bovine Endothelial Cells

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Positive assortative pairing in social and romantic partners: A cross-cultural observational field study of naturally occurring pairs

Personality and Individual Differences ◽

10.1016/j.paid.2014.12.060 ◽

2015 ◽

Vol 84 ◽

pp. 30-35 ◽

Cited By ~ 4

Author(s):

Aurelio José Figueredo ◽

Pedro Sofío Abril Wolf ◽

Sally Gayle Olderbak ◽

Jon Adam Sefcek ◽

Martha Frías-Armenta ◽

...

Keyword(s):

Field Study ◽

Romantic Partners ◽

Cross Cultural ◽

Naturally Occurring ◽

Assortative Pairing

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Abilities of the mCP Agar Method and CRENAME Alpha Toxin-Specific Real-Time PCR Assay To Detect Clostridium perfringens Spores in Drinking Water

Applied and Environmental Microbiology ◽

10.1128/aem.02791-13 ◽

2013 ◽

Vol 79 (24) ◽

pp. 7654-7661 ◽

Cited By ~ 13

Author(s):

Andrée F. Maheux ◽

Ève Bérubé ◽

Dominique K. Boudreau ◽

Romain Villéger ◽

Philippe Cantin ◽

...

Keyword(s):

Drinking Water ◽

Water Sample ◽

Real Time ◽

Clostridium Perfringens ◽

Real Time Pcr ◽

Potable Water ◽

Alpha Toxin ◽

Pcr Assay ◽

Content Type ◽

The Public

ABSTRACTWe first determined the analytical specificity and ubiquity (i.e., the ability to detect all or most strains) of aClostridium perfringens-specific real-time PCR (rtPCR) assay based on thecpagene (cpartPCR) by using a bacterial strain panel composed ofC. perfringensand non-C. perfringens Clostridiumstrains. All non-C. perfringens Clostridiumstrains tested negative, whereas allC. perfringensstrains tested positive with thecpartPCR, for an analytical specificity and ubiquity of 100%. ThecpartPCR assay was then used to confirm the identity of 116 putativeC. perfringensisolates recovered after filtration of water samples and culture on mCP agar. Colonies presenting discordant results between the phenotype on mCP agar andcpartPCR were identified by sequencing the 16S rRNA andcpagenes. Four mCP−/rtPCR+colonies were identified asC. perfringens, whereas 3 mCP+/rtPCR−colonies were identified as non-C. perfringens. ThecpartPCR was negative with all 51 non-C. perfringensstrains and positive with 64 of 65C. perfringensstrains. Finally, we compared mCP agar and a CRENAME (concentration andrecovery of microbial particles,extraction ofnucleicacids, andmolecularenrichment) procedure pluscpartPCR (CRENAME +cpartPCR) for their abilities to detectC. perfringensspores in drinking water. CRENAME +cpartPCR detected as few as oneC. perfringensCFU per 100 ml of drinking water sample in less than 5 h, whereas mCP agar took at least 25 h to deliver results. CRENAME +cpartPCR also allows the simultaneous and sensitive detection ofEscherichia coliandC. perfringensfrom the same potable water sample. In itself, it could be used to assess the public health risk posed by drinking water potentially contaminated with pathogens more resistant to disinfection.

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A simple electroelution method for rapid protein purification: isolation and antibody production of alpha toxin fromClostridium septicum

PeerJ ◽

10.7717/peerj.3407 ◽

2017 ◽

Vol 5 ◽

pp. e3407 ◽

Cited By ~ 2

Author(s):

Lorena Vázquez-Iglesias ◽

Borja Estefanell-Ucha ◽

Leticia Barcia-Castro ◽

María Páez de la Cadena ◽

Paula Álvarez-Chaver ◽

...

Keyword(s):

Protein Purification ◽

Polyclonal Antibodies ◽

Clinical Intervention ◽

Farm Animals ◽

Alpha Toxin ◽

Slot Blot ◽

Clostridium Septicum ◽

Time Saving ◽

Specific Antibodies

Clostridium septicumproduces a number of diseases in human and farm animals which, in most of the cases, are fatal without clinical intervention. Alpha toxin is an important agent and the unique lethal virulent factor produced byClostridium septicum.This toxin is haemolytic, highly lethal and necrotizing activities but is being used as an antigen to develop animal vaccines. The aim of this study was to isolate the alpha toxin ofClostridium septicumand produce highly specific antibodies against it. In this work, we have developed a simple and efficient method for alpha toxin purification, based on electroelution that can be used as a time-saving method for purifying proteins. This technique avoids contamination by other proteins that could appear during other protein purification techniques such chromatography. The highly purified toxin was used to produce polyclonal antibodies. The specificity of the antibodies was tested by western blot and these antibodies can be applied to the quantitative determination of alpha toxin by slot blot.

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