Biological characterization of major polypeptides on the surface of spotted fever group rickettsiae

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Abstract

There are two major polypeptides on the surface of spotted fever group rickettsiae that play important roles as immunogens and possibly relate to the pathogenicity of rickettsial diseases. Digestion with trypsin and staphylococcal V-8 protease shows that the 115-kDa protein of Rickettsia conorii is a trypsin-sensitive, surface-exposed protein. The 135-kDa protein is relatively trypsin resistant. Both proteins resist heat treatment up to 52°C and maintain their antigenic reactivity with monoclonal antibodies when the intact rickettsiae are heated. When rickettsiae are dissolved in SDS-containing sample buffer, these polypeptides lose their antigenic reactivity with monoclonal antibodies after incubation at 45°C for 10 min. Staphylococcal V-8 protease does not appear to affect these polypeptides under the current experimental conditions. Monoclonal antibody to the 115-kDa protein reduces rickettsial attachment. The 115-kDa polypeptide may play a role in rickettsial adhesion to the host cell surface.

Original languageEnglish (US)
Pages (from-to)389-394
Number of pages6
JournalAnnals of the New York Academy of Sciences
Volume590
DOIs
StatePublished - 1990

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Rickettsia
Fever
Trypsin
Peptides
Monoclonal Antibodies
Proteins
Rickettsia conorii
Virulence
Digestion
Buffers
Membrane Proteins
Hot Temperature
Adhesion
Heat treatment
Protein
glutamyl endopeptidase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

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title = "Biological characterization of major polypeptides on the surface of spotted fever group rickettsiae",
abstract = "There are two major polypeptides on the surface of spotted fever group rickettsiae that play important roles as immunogens and possibly relate to the pathogenicity of rickettsial diseases. Digestion with trypsin and staphylococcal V-8 protease shows that the 115-kDa protein of Rickettsia conorii is a trypsin-sensitive, surface-exposed protein. The 135-kDa protein is relatively trypsin resistant. Both proteins resist heat treatment up to 52°C and maintain their antigenic reactivity with monoclonal antibodies when the intact rickettsiae are heated. When rickettsiae are dissolved in SDS-containing sample buffer, these polypeptides lose their antigenic reactivity with monoclonal antibodies after incubation at 45°C for 10 min. Staphylococcal V-8 protease does not appear to affect these polypeptides under the current experimental conditions. Monoclonal antibody to the 115-kDa protein reduces rickettsial attachment. The 115-kDa polypeptide may play a role in rickettsial adhesion to the host cell surface.",
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T1 - Biological characterization of major polypeptides on the surface of spotted fever group rickettsiae

AU - Li, H.

AU - Walker, David

PY - 1990

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N2 - There are two major polypeptides on the surface of spotted fever group rickettsiae that play important roles as immunogens and possibly relate to the pathogenicity of rickettsial diseases. Digestion with trypsin and staphylococcal V-8 protease shows that the 115-kDa protein of Rickettsia conorii is a trypsin-sensitive, surface-exposed protein. The 135-kDa protein is relatively trypsin resistant. Both proteins resist heat treatment up to 52°C and maintain their antigenic reactivity with monoclonal antibodies when the intact rickettsiae are heated. When rickettsiae are dissolved in SDS-containing sample buffer, these polypeptides lose their antigenic reactivity with monoclonal antibodies after incubation at 45°C for 10 min. Staphylococcal V-8 protease does not appear to affect these polypeptides under the current experimental conditions. Monoclonal antibody to the 115-kDa protein reduces rickettsial attachment. The 115-kDa polypeptide may play a role in rickettsial adhesion to the host cell surface.

AB - There are two major polypeptides on the surface of spotted fever group rickettsiae that play important roles as immunogens and possibly relate to the pathogenicity of rickettsial diseases. Digestion with trypsin and staphylococcal V-8 protease shows that the 115-kDa protein of Rickettsia conorii is a trypsin-sensitive, surface-exposed protein. The 135-kDa protein is relatively trypsin resistant. Both proteins resist heat treatment up to 52°C and maintain their antigenic reactivity with monoclonal antibodies when the intact rickettsiae are heated. When rickettsiae are dissolved in SDS-containing sample buffer, these polypeptides lose their antigenic reactivity with monoclonal antibodies after incubation at 45°C for 10 min. Staphylococcal V-8 protease does not appear to affect these polypeptides under the current experimental conditions. Monoclonal antibody to the 115-kDa protein reduces rickettsial attachment. The 115-kDa polypeptide may play a role in rickettsial adhesion to the host cell surface.

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