The functional characterization of these three genomes shows that each of them independently acquired dozens of virulent genes horizontally from the other microbial genomes. Our hypothesis is that new genes may have been acquired horizontally to exert the digestion tract infection and toxicity. mirabilis C02011/C04010/C04013 were isolated from a local outbreak of a food poisoning event in Shenzhen, China. Its notorious ability to resist multiple antibiotics and to form urinary tract stones makes its treatment a long and painful process, which is further challenged by the frequent horizontal gene transferring events in P. Proteus mirabilis is a common urinary tract pathogen, and may induce various inflammation symptoms. Shi, Xiaolu Lin, Yiman Qiu, Yaqun Li, Yinghui Jiang, Min Chen, Qiongcheng Jiang, Yixiang Yuan, Jianhui Cao, Hong Hu, Qinghua Huang, Shenghe PMID:22174977Ĭomparative Screening of Digestion Tract Toxic Genes in Proteus mirabilis. Used in conjunction with anti-abrin monoclonal and polyclonal antibodies, these reagents can fill a role to discriminate between the highly toxic abrin and the related, but much less toxic, Abrus agglutinin and distinguish between different crude preparations. Through gel analysis and the behavior of anti-abrin monoclonal antibodies, we determined that the commercial toxoid preparation used for the original immunizations contained a high percentage of Abrus agglutinin, explaining the selection of Abrus agglutinin binders. These binders had sub nM affinities and regained most of their secondary structure after heating to 95 Â☌. The best binders were specific for the Abrus agglutinin, showing minimal binding to purified abrin fractions or unrelated proteins. Isolated sdAb were also evaluated for their ability to refold after heat denaturation and ability to be used in sandwich assays as both capture and reporter elements. The selected sdAb were evaluated for their ability to bind to commercial abrin as well as abrax (a recombinant abrin A-chain), purified abrin fractions, Abrus agglutinin (a protein related to abrin but with lower toxicity), ricin, and unrelated proteins. Abrin is a potent toxin similar to ricin in structure, sequence and mechanism of action. Llama derived single domain antibodies (sdAb), the recombinantly expressed variable heavy domains from the unique heavy-chain only antibodies of camelids, were isolated from a library derived from llamas immunized with a commercial abrin toxoid preparation. Bernstein, Rachael Calm, Alena Carney, James P. Zabetakis, Dan Walper, Scott Liu, Jinny L. Llama-Derived Single Domain Antibodies Specific for Abrus Agglutinin