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Neutralizing activity of monoclonal antibodies to heat-sensitive and heat-resistant epitopes of Rickettsia rickettsii surface proteins.

Infection and Immunity, 01 Mar 1987, 55(3):825-827
https://doi.org/10.1128/iai.55.3.825-827.1987 PMID: 2434430 PMCID: PMC260417

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Abstract 

Antiprotein monoclonal antibodies derived from mice inoculated with Rickettsia rickettsii heated at 56 degrees C for 15 min are of two types: one is type specific for epitopes denatured by moderate temperatures, and the other is specific for epitopes resistant to 100 degrees C for 5 min. The heat-resistant epitopes are found by immunoblotting on multiple polypeptides after solubilization of the rickettsiae at temperatures of 56 degrees C or higher. Most, but not all, antibodies to the heat-sensitive epitopes passively protected mice against two 50% lethal doses of R. rickettsii, whereas none of the antibodies to heat-resistant epitopes did.

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Infect Immun. 1987 Mar; 55(3): 825–827.
PMCID: PMC260417
PMID: 2434430

Neutralizing activity of monoclonal antibodies to heat-sensitive and heat-resistant epitopes of Rickettsia rickettsii surface proteins.

R L Anacker, G A McDonald, R H List, and R E Mann
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Abstract

Antiprotein monoclonal antibodies derived from mice inoculated with Rickettsia rickettsii heated at 56 degrees C for 15 min are of two types: one is type specific for epitopes denatured by moderate temperatures, and the other is specific for epitopes resistant to 100 degrees C for 5 min. The heat-resistant epitopes are found by immunoblotting on multiple polypeptides after solubilization of the rickettsiae at temperatures of 56 degrees C or higher. Most, but not all, antibodies to the heat-sensitive epitopes passively protected mice against two 50% lethal doses of R. rickettsii, whereas none of the antibodies to heat-resistant epitopes did.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
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