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Alejandra Habarta Patricia A. E. Abreu Noelia Olivera Pricila Hauk Maia T. Cédola María F. Ferrer Paulo L. Ho Ricardo M. Gomez 《Current microbiology》2011,62(2):526-531
Leptospirosis is one of the most widespread zoonosis in the world. The development of a recombinant leptospira vaccine remains
a challenge. In this study, we cloned the Leptospira interrogans open reading frame (ORF) coding the external membrane protein LipL32, an immunodominant antigen found in all pathogenic leptospira,
downstream of the highly immunogenic cholera toxin B subunit (CTB) ORF. Expression and assembly of the CTB-LipL32 fusion protein
into oligomeric structures of pentameric size were observed in soluble fractions by Western blot analysis. The CTB-LipL32
protein demonstrated strong affinity for monosialotetrahexosylgaglioside (GM1-ganglioside) in an enzyme-linked immunosorbent
assay (ELISA), suggesting that the antigenic sites for binding and proper folding of the pentameric CTB structure were conserved.
Furthermore, antisera against LipL32 also recognized the CTB-LipL32 fusion protein, suggesting that LipL32 also conserved
its antigenic sites, a fact confirmed by an ELISA assay showing soluble CTB-LipL32 recognition by sera from convalescent patients.
In addition, soluble CTB-LipL32 generated higher specific titers in mice immunized without external adjuvant than co-administration
of CTB with LipL32. The data presented here provide support for CTB-LipL32 as a promising antigen for use in the control and
study of leptospirosis. 相似文献
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Andrea Hauk 《当今生物学》2014,44(5):296-296