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Cloning, protein expression and display of synthetic multi-epitope mycobacterial antigens on <i style="">Salmonella typhi</i> Ty21a cell surface

IR@NISCAIR: CSIR-NISCAIR, New Delhi - ONLINE PERIODICALS REPOSITORY (NOPR)


Field	Value

Title	Cloning, protein expression and display of synthetic multi-epitope mycobacterial antigens on <i style="">Salmonella typhi</i> Ty21a cell surface

Creator	Sarhan, Mohammed A A Musa, Mustaffa Zainuddin, Zainul F

Subject	Ice nucleation protein <i style="">Mycobacterium tuberculosis</i> Surface display Ty21a

Description	645-653 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 <i style="">Mycobacterium tuberculosis</i> namely, ESAT6, MTP40, 38 kDa, and MPT64 was fused with N- terminus of <i style="">Pseudomonas syringae</i> 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 <i style="">Salmonella typhi</i> 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).

Date	2011-08-29T05:57:05Z 2011-08-29T05:57:05Z 2011-09

Type	Article

Identifier	0975-1009 (Online); 0019-5189 (Print) http://hdl.handle.net/123456789/12609

Language	en_US

Rights	<img src='http://nopr.niscair.res.in/image/cc-license-sml.png'> <a href='http://creativecommons.org/licenses/by-nc-nd/2.5/in' target='_blank'>CC Attribution-Noncommercial-No Derivative Works 2.5 India</a>

Publisher	NISCAIR-CSIR, India

Source	IJEB Vol.49(09) [September 2011]