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People - Sal-Man Lab

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E-Mail: salmanne@bgu.ac.il. Lihi Shau . E-Mail: shaulovl@post.bgu.ac.il. Soniara@post.bgu.ac.il. Adi Madar . Adimad@post.bgu.ac.il. Tseytini@post.bgu.ac.il. Kseniay@post.bgu.ac.il. Gertlerj@post.bgu.ac.il. 2013 Neta Sal-Man Laboratory. Contact: salmanne@bgu.ac.il.

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Resources - Sal-Man Lab

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Expasy: http:/ www.expasy.org/. Reverse complement: http:/ www.bioinformatics.org/sms/rev comp.html. Pubmed: http:/ www.ncbi.nlm.nih.gov/pubmed. NEB: https:/ www.neb.com/. EPEC 0126 LEE complete sequence: http:/ www.ncbi.nlm.nih.gov/nuccore/AF022236.1. BGU website: http:/ in.bgu.ac.il/Pages/default.aspx. 2013 Neta Sal-Man Laboratory. Contact: salmanne@bgu.ac.il.

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Projects - Sal-Man Lab

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The assembly of the T3SS. The first bacterial component to physically interact with the host cell membrane is known as the translocon complex. The complex, which is made up of 2-3 proteins, facilitates the transport of effectors across the host-cell plasma membrane. Despite the critical role of the translocon in bacterial virulence, the mechanisms of translocon assembly, interactions with the host membrane, and pore formation activity remain to be elucidated. Transmembrane domains within the T3SS.

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Publications - Sal-Man Lab

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Gerber D, Shai Y. (2014). Proline localized to the interaction interface can mediate self-association of transmembrane domains. Sal-Man N., Setiaputra D., Scholz R., Deng W., Yu ACY., Strynadka NCJ., and Finlay BB. (2013) “. EscE and EscG are co-chaperones for the type III needle protein EscF of enteropathogenic. Rdquo; J. Bacteriol. 195 (11), 2481-2489. Sal-Man N., Biemans-Oldehinkel E., Sharon D., Croxen MA., Scholz R., Foster LJ., and Finlay BB. (2012) “. Rdquo; J. Bacteriol. 194 (11), 2819-2828.

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