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| Author(s): |
Priscila Romero Mazzini Pereira
Total Authors: 1
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| Document type: | Master's Dissertation |
| Press: | São Paulo. |
| Institution: | Universidade de São Paulo (USP). Instituto de Ciências Biomédicas (ICB/SDI) |
| Defense date: | 2017-02-10 |
| Examining board members: |
Ana Lucia Tabet Oller do Nascimento;
Tania Aparecida Tardelli Gomes do Amaral;
Karin Kirchgatter;
Adalberto Pessoa Junior
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| Advisor: | Ana Lucia Tabet Oller do Nascimento |
| Abstract | |
Leptospirosis is the most widespread zoonosis and also a major cause of economic loss in animal production worldwide. The study of new surface antigens of Leptospira interrogans is intriguing and may shed light into the initial pathogen-host interactions. We set out to study two novel coding sequences LIC13059 and LIC10879 predicted to be located at the cell surface. The genes were cloned and the recombinant proteins were expressed in E. coli. The purified recombinant proteins presented secondary structures, and interacted with plasminogen, fibrinogen and laminin human components. rLIC13059, named Lsa25.6, when bound to fibrinogen was capable of inhibiting the formation of fibrin clot, while rLIC10879, named Lsa16, interacted with e-cadherin, a mammalian cell receptor, suggesting participation in coagulation pathway and host-cell binding, respectively. The plasminogen captured by both recombinant proteins could be converted into plasmin, a mechanism that could help bacterial penetration in the host. (AU) | |
| FAPESP's process: | 15/02590-5 - Immunological and functional characterization of two predict lipoproteins of Leptospira interrogans expressed in the host Escherichia coli |
| Grantee: | Priscila Romero Mazzini Pereira |
| Support Opportunities: | Scholarships in Brazil - Master |