Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/12609
Title: Cloning, protein expression and display of synthetic multi-epitope mycobacterial antigens on Salmonella typhi Ty21a cell surface
Authors: Sarhan, Mohammed A A
Musa, Mustaffa
Zainuddin, Zainul F
Keywords: Ice nucleation protein
Mycobacterium tuberculosis
Surface display
Ty21a
Issue Date: Sep-2011
Publisher: NISCAIR-CSIR, India
Abstract: Expressing proteins of interest as fusion to proteins of bacterial envelope is a powerful technique for biotechnological and medical applications. The synthetic gene (VacII) encoding for T-cell epitopes of selected genes of Mycobacterium tuberculosis namely, ESAT6, MTP40, 38 kDa, and MPT64 was fused with N- terminus of Pseudomonas syringae ice nucleation protein (INP) outer membrane protein. The fused genes were cloned into a bacterial expression vector pKK223-3. The recombinant protein was purified by Ni-NAT column. VacII gene was displayed on the cell surface of Salmonella typhi Ty21a using N-terminal region of ice nucleation proteins (INP) as an anchoring motif. Glycine method confirmed that VacII was anchored on the cell surface. Western blot analysis further identified the synthesis of INP derivatives containing the N-terminal domain INP- VacII fusion protein of the expected size (52 kDa).
Description: 645-653
URI: http://hdl.handle.net/123456789/12609
ISSN: 0975-1009 (Online); 0019-5189 (Print)
Appears in Collections:IJEB Vol.49(09) [September 2011]

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