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Master's Dissertation
DOI
https://doi.org/10.11606/D.87.2017.tde-23052017-141254
Document
Author
Full name
Priscila Romero Mazzini Pereira
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 2017
Supervisor
Committee
Nascimento, Ana Lucia Tabet Oller do (President)
Amaral, Tania Aparecida Tardelli Gomes do
Kirchgatter, Karin
Pessoa Junior, Adalberto
Title in Portuguese
Caracterização imunogênica e funcional de duas lipoproteínas preditas de Leptospira interrogans expressas em Escherichia coli.
Keywords in Portuguese
Leptospira
Leptospirose
Lipoproteínas
Proteína recombinante
Abstract in Portuguese
A leptospirose é a zoonose mais disseminada no mundo e uma das principais causas de perda econômica no agronegócio. O estudo de novos antígenos de superfície de Leptospira interrogans, é intrigante e pode fornecer conhecimento na interação inicial patógeno-hospedeiro. Os genes LIC13059 e LIC10879, escolhidos por bioinformática, com predição de localização na superfície celular, foram clonados e as proteínas recombinantes expressas em E. coli, para avaliar a interação com componentes do hospedeiro. Após purificação, as proteínas encontravam-se estruturadas e foram reconhecidas por soro de indivíduos infectados. As proteínas recombinantes interagem com plasminogênio, fibrinogênio e laminina. rLIC13059, nomeada Lsa25.6, quando ligada ao fibrinogênio é capaz de inibir a formação de coágulo de fibrina e rLIC10879, nomeada Lsa16, interage com e-caderina, sugerido envolvimento na cascata de coagulação e ligação com o hospedeiro, respectivamente. O plasminogênio ligado às proteínas é convertido em plasmina, o que poderia ajudar a penetração bacteriana no hospedeiro.
Title in English
Immunogenic and functional characterization of two probable lipoproteins of Leptospira interrogans expressed in Escherichia coli.
Keywords in English
Leptospira
Leptospirosis
Lipoproteins
Recombinant proteins
Abstract in English
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.
 
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Publishing Date
2017-05-23
 
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