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Role of outer envelope contamination in protection elicited by ribosomal preparations against Neisseria gonorrhoeae infection
Author(s) -
M D Cooper,
Michael J. Wannemuehler,
Richard D. Miller,
Mark Floyd Fedyk
Publication year - 1981
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.32.1.173-179.1981
Subject(s) - microbiology and biotechnology , biology , precipitin , neisseria gonorrhoeae , ribosomal rna , pronase , bacterial outer membrane , ribosomal protein , antigen , ribosome , escherichia coli , immunology , biochemistry , rna , trypsin , gene , enzyme
A recent report (Cooper et al., Infect. Immun. 28:92-100, 1980) demonstrated that immunization of guinea pigs with ribosomal preparations was protective (approximately 90%) against chamber infections with Neisseria gonorrhoeae. Similar protection has been demonstrated with other cellular immunogens such as outer membranes (OM) (92%) or purified lipopolysaccharide (LPS) (83%). Protection of LPS (5 to 100 micrograms) was dose dependent (83% with 100 micrograms). Treatment of LPS with pronase reduced the protection by 50%. Ribosomal preparations contained LPS contamination (3.9%) based on dry weight determinations by 2-keto-3-deoxyoctonate analysis. Analysis of ribosomal preparations isolated from cells after lactoperoxidase-mediated 125I labeling indicated a major OM contamination (Protein I). The ribosomal preparation also contained low levels of succinic and lactic dehydrogenase. Passive hemagglutination tests revealed that sera from guinea pigs immunized with ribosomal preparations also demonstrated antibody to OM proteins and LPS. LPS was able to absorb one line of precipitation seen in immunodiffusion reactions as well as the bactericidal activity of such sera. OM preparations were unable to absorb the remaining precipitin line or remove the bactericidal activity. It appears that LPS is the major antigen responsible for the bactericidal activity seen in ribosome-immune sera.

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