Immunogenicity assessment of antileukemic agent glutaminase from Escherichia coli, Pseudomonas sp., and Bacillus sp.

Abstract

Background: L-glutaminase (L-glutaminase or glutamine amidohydrolase: EC 3.5.1.2) is an antileukemic agent which catalyzes the deamidation of glutamine to glutamic acid and ammonia. It is a highly potent antitumor drug solely or in combination with L-asparaginase. In the market, various microbial glutaminases are available, which are used in treatment. The high immunogenicity was reported with microbial glutaminase when they are introduced in the body during the treatment of acute lymphoblastic leukemia (ALL). Methods: This study was aimed to determine the immunogenicity of the less studied enzyme L-glutaminase from Escherichia coli, Pseudomonas sp., and Bacillus sp. to reduce the allergenicity caused by this enzyme. In the present study, we determined the immunogenicity and allergenicity of microbial glutaminase using an immunoinformatics approach to predict immunogenic and allergenic epitopes with their structural analysis also. Results: We found high immunogenicity of glutaminase from these three microbial sources but did not find a significant difference in their immunogenicity, while E. coli glutaminase showed a high relative frequency of allergenic epitopes. Conclusions: In our knowledge, this is the first research report that presented the immunogenic epitopes and structural allergenic determinants that warrant further work to minimize the immune response of glutaminase and could contribute to reducing the side effect and hypersensitivity response of glutaminase during the treatment.