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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1989-10-23
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pubmed:abstractText |
A homologous polyclonal antibody was produced in a rabbit to the 104-kilodalton (kDa) protein hemolysin of Actinobacillus pleuropneumoniae serotype 1 strain CM-5. In immunoblots, this antibody recognized a similar 104-kDa protein produced in culture supernatants by A. pleuropneumoniae serotypes 1 to 12 and taxon "Minor group" in addition to Pasteurella haemolytica, Actinobacillus suis, and alpha-hemolysin-producing Escherichia coli (but only weakly in the latter two organisms). These results were reproduced by using a mouse monoclonal antibody to the CM-5 104-kDa protein hemolysin, except that the monoclonal antibody bound more strongly to the alpha-hemolysin produced by E. coli, only weakly to the 104-kDa protein produced by "Minor group," and not at all to any extracellular antigens produced by A. suis. Pigs experimentally infected with A. pleuropneumoniae serotypes 1 to 10 and A. suis produced an antibody that recognized the 104-kDa hemolysin produced by CM-5. A pig challenged with a "Minor group" strain did not have such antibodies. Rabbit antiserum produced against the leukotoxin of P. haemolytica and alpha-hemolysin-producing E. coli also recognized the CM-5 hemolysin, but the latter only weakly. The hemolytic activity produced by CM-5 in culture supernatant was neutralized strongly by the pig serum to serotypes 1, 2, 5, 6, 9, and 10 and A. suis, only partially by serotype 8 antiserum and the rabbit antiserum to P. haemolytica leukotoxin, and not all by the antiserum to serotypes 3, 4, and 7 and "Minor group" and the E. coli alpha-hemolysin. These results indicate that a similar but not identical 104-kDa protein is produced in vitro and in vivo by all serotypes of A. pleuropneumoniae and may be related to cytolysins produced by other gram-negative bacteria.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-2465272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-2465275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-2713790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3417350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3421527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3514465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3539296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3592376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3905610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3943895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3943899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-3986682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-6348003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674017-6493974
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0019-9567
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3210-3
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2674017-Actinobacillus,
pubmed-meshheading:2674017-Actinobacillus Infections,
pubmed-meshheading:2674017-Animals,
pubmed-meshheading:2674017-Bacterial Proteins,
pubmed-meshheading:2674017-Escherichia coli,
pubmed-meshheading:2674017-Hemolysin Proteins,
pubmed-meshheading:2674017-Mice,
pubmed-meshheading:2674017-Mice, Inbred BALB C,
pubmed-meshheading:2674017-Molecular Weight,
pubmed-meshheading:2674017-Neutralization Tests,
pubmed-meshheading:2674017-Pasteurella,
pubmed-meshheading:2674017-Rabbits,
pubmed-meshheading:2674017-Swine,
pubmed-meshheading:2674017-Virulence
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pubmed:year |
1989
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pubmed:articleTitle |
Immunoserological comparison of 104-kilodalton proteins associated with hemolysis and cytolysis in Actinobacillus pleuropneumoniae, Actinobacillus suis, Pasteurella haemolytica, and Escherichia coli.
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pubmed:affiliation |
Department of Veterinary Microbiology and Immunology, University of Guelph, Ontario, Canada.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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