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PMID: 7275932 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification and disposition of a surface protein associated with virulence of Aeromonas salmonicida.

Journal of bacteriology ·Vol. 147 ·No. 3 ·1981-09-00 ·Pages 1077-84

Kay WW, Buckley JT, Ishiguro EE, Phipps BM, Monette JP, Trust TJ

Abstract

Virulent strains of Aeromonas salmonicida observed by electron microscopy were characterized by an outer layer exhibiting a tetragonal repeat pattern. Attenuated strains had a 2.5 X 10(3)- to 5 X 10(3)-fold reduction in virulence and lost the outer layer, autoaggregating properties, and a 49-kilodalton protein (A protein) simultaneously. The A protein is the major protein component of outer membrane fractions of virulent strains. A variety of radiolabeling studies showed that this protein was surface localized and that it provided an effective barrier against iodination of other outer membrane proteins with either lactoperoxidase or diazoiodosulfanilic acid; A protein was not labeled with lactoperoxidase but was specifically labeled with diazoidosulfanilic acid. The A protein was purified by selective extraction with detergent and guanidine hydrochloride, and its amino acid composition was determined. The properties of A protein are compared with those of other bacterial surface layer proteins.

MeSH Terms
Aeromonas/analysis,pathogenicity Amino Acids/analysis Bacterial Proteins/analysis,isolation & purification Membrane Proteins/analysis,isolation & purification
Chemicals
Amino Acids Bacterial Proteins Membrane Proteins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Kay W W
Buckley J T
Ishiguro E E
Phipps B M
Monette J P
Trust T J
References (23)
23 references, click to expand
  1. Sulfanilic acid diazonium salt: a label for the outside of the human erythrocyte membrane.
    Biochim Biophys Acta. 1969 Jun 3;183(1):65-78 PMID: 4183114
  2. Studies on the cell wall of Spirillum serpens. 1. Isolation and partial purification of the outermost cell wall layer.
    Can J Microbiol. 1970 Oct;16(10):1011-22 PMID: 4991779
  3. The fine structure of Cardiobacterium hominis.
    Acta Pathol Microbiol Scand B Microbiol Immunol. 1971;79(1):51-60 PMID: 4102476
  4. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
    Biochemistry. 1971 Jun 22;10(13):2606-17 PMID: 4326772
  5. Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system.
    J Biol Chem. 1971 Oct 25;246(20):6328-34 PMID: 5127429
  6. Enzymic iodination. A probe for accessible surface proteins of normal and neoplastic lymphocytes.
    Biochem J. 1971 Oct;124(5):921-7 PMID: 5131013
  7. Studies on the cell wall of Spirillum serpens. II. Chemical characterization of the outer structured layer.
    Can J Microbiol. 1973 Jan;19(1):59-66 PMID: 4119519
  8. Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate.
    J Bacteriol. 1973 Sep;115(3):717-22 PMID: 4580564
  9. Detachment and chemical characterization of the regularly arranged subunits from the surface of an Acinetobacter.
    J Bacteriol. 1974 May;118(2):654-62 PMID: 4208137
  10. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding.
    J Biol Chem. 1974 Dec 25;249(24):8019-29 PMID: 4609976
  11. Studies on gonococcus infection. VIII. 125Iodine labeling of gonococci and studies on their in vitro interactions with eukaryotic cells.
    Infect Immun. 1975 Mar;11(3):453-9 PMID: 803927
  12. Superficial antigens of Campylobacter (Vibrio) fetus: characterization of antiphagocytic component.
    Infect Immun. 1975 Mar;11(3):517-25 PMID: 46843
  13. Chemical characterization of the regularly arranged surface layers of Clostridium thermosaccharolyticum and Clostridium thermohydrosulfuricum.
    J Bacteriol. 1976 Apr;126(1):377-83 PMID: 816775
  14. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples.
    Anal Biochem. 1978 Jun 15;87(1):206-10 PMID: 98070
  15. Surface-specific iodination of membrane proteins of viruses and eucaryotic cells using 1,3,4,6-tetrachloro-3alpha,6alpha-diphenylglycoluril.
    Biochemistry. 1978 Oct 31;17(22):4807-17 PMID: 215191
  16. Microcapsule of Campylobacter fetus: chemical and physical characterization.
    Infect Immun. 1978 Dec;22(3):963-71 PMID: 730387
  17. Specific interaction of the tetragonally arrayed protein layer of Bacillus sphaericus with its peptidoglycan sacculus.
    J Bacteriol. 1979 Jun;138(3):1010-21 PMID: 457591
  18. Isolation, characterization, and in vitro assembly of the tetragonally arrayed layer of Bacillus sphaericus.
    J Bacteriol. 1979 Jun;138(3):999-1009 PMID: 457597
  19. Outer membrane of Pseudomonas aeruginosa: heat- 2-mercaptoethanol-modifiable proteins.
    J Bacteriol. 1979 Dec;140(3):902-10 PMID: 118160
  20. Ultrastructure of the Bacteroides nodosus cell envelope layers and surface.
    J Bacteriol. 1980 Feb;141(2):845-57 PMID: 6154040
  21. Structure of the regular surface layer of Spirillum putridiconchylium.
    J Mol Biol. 1980 Feb 15;137(1):1-8 PMID: 7365794
  22. Structure of the regular surface layer of Sporosarcina ureae.
    J Bacteriol. 1980 Apr;142(1):302-9 PMID: 7372574
  23. The reactions of diazonium compounds with amino acids and proteins.
    Biochem J. 1957 Apr;65(4):651-9 PMID: 13426079
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1981-09-00
Pages
1077-84
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC216148
Subset
IM
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