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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1988-3-10
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pubmed:abstractText |
The surface protein composition of members of a serogroup of Aeromonas hydrophila which exhibit high virulence for fish was examined. Treatment of whole cells of representative strain A. hydrophila TF7 with 0.2 M glycine buffer (pH 4.0) resulted in the release of sheets of a tetragonal surface protein array. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis analysis showed that this sheet material was composed primarily of a protein of apparent molecular weight 52,000 (52K protein). A 52K protein was also the predominant protein in glycine extracts of other members of the high-virulence serogroup. Immunoblotting with antiserum raised against formalinized whole cells of A. hydrophila TF7 showed the 52K S-layer protein to be the major surface protein antigen, and impermeant Sulfo-NHS-Biotin cell surface labeling showed that the 52K S-layer protein was the only protein accessible to the Sulfo-NHS-Biotin label and effectively masked underlying outer membrane (OM) proteins. In its native surface conformation the 52K S-layer protein was only weakly reactive with a lactoperoxidase 125I surface iodination procedure. A UV-induced rough lipopolysaccharide (LPS) mutant of TF7 was found to produce an intact S layer, but a deep rough LPS mutant was unable to maintain an array on the cell surface and excreted the S-layer protein into the growth medium, indicating that a minimum LPS oligosaccharide size was required for A. hydrophila S-layer anchoring. The 52K S-layer protein exhibited hear-dependent SDS-solubilization behavior when associated with OM, but was fully solubilized at all temperatures after removal from the OM, indicating a strong interaction of the S layer with the underlying OM. The native S layer was permeable to 125I in the lactoperoxidase radiolabeling procedure, and two major OM proteins of molecular weights 30,000 and 48,000 were iodinated. The 48K species was a peptidoglycan-associated, transmembrane protein which exhibited heat-modifiable SDS solubilization behaviour characteristic of a porin protein. A 50K major peptidoglycan-associated OM protein which was not radiolabeled exhibited similar SDS heat modification characteristics and possibly represents a second porin protein.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-14450081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-2413008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-2434461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-2993248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-3765354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-3810164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-3877720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-4078309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-4555955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-4580564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-4609976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-46843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6138214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6175245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6176137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6187729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6203838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6315674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6370955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6416145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-6735982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-7095843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-7237273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-7275932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-7287625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3276660-98070
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
170
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
499-506
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3276660-Aeromonas,
pubmed-meshheading:3276660-Animals,
pubmed-meshheading:3276660-Antigens, Bacterial,
pubmed-meshheading:3276660-Antigens, Surface,
pubmed-meshheading:3276660-Bacterial Outer Membrane Proteins,
pubmed-meshheading:3276660-Cell Membrane,
pubmed-meshheading:3276660-Centrifugation, Density Gradient,
pubmed-meshheading:3276660-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3276660-Fishes,
pubmed-meshheading:3276660-Immunoassay,
pubmed-meshheading:3276660-Immunoenzyme Techniques,
pubmed-meshheading:3276660-Microscopy, Electron,
pubmed-meshheading:3276660-Molecular Weight,
pubmed-meshheading:3276660-Virulence
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pubmed:year |
1988
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pubmed:articleTitle |
Surface protein composition of Aeromonas hydrophila strains virulent for fish: identification of a surface array protein.
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pubmed:affiliation |
Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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