Review of the Article: Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase.
Authors: Kimberly Payne1, Qingan Sun2, James Sacchettini2, and Graham F. Hatfull1.
By: Joannieliz Rodríguez Cora Course: Biol 3033 Secc.: 127 Prof. Michael Rubin

This article shows a study carried out by using phages. In this case, they used the phage lysin b9 to identify new structures, the behavior of this, features and analysis of its replication even lead to total lysis. Comparative analysis of mycobacteriophage genomes Reveals Them to Be Highly diverse with mosaic architectures (Hatfull et al., 2006, Pedulla et al., 2003). Because phage lysin has a much Broader Than range lytic phage, Infection of paired and multi-strain cultures with a lysin-producing phage has the Potential to cause fermentation failure, dead-vats, and Consequent Economic loss. That They Have Shown here LysB the mycobacteriophage D29 is a novel protein mycolylarabinogalactan esterase required for completion of mycobacterial lysis of host cells, and a model for the role of the Lysine Lysine A and B proteins as well as the reaction catalyzed by LysB.

They use mycolic acid rich mycobacterial outer membrane that presents an unusual problem for phages of Gram-positive bacteria, which typically complete lysis through simple endolysin-mediated degradation of the peptidoglycan layer. The mycolylarabinogalactan linkage is not common among bacteria, since mycolic acids are found primarily in the Corynebacterineae suborder of the Actinomycetales, which includes
Corynebacteria, Gordonia, Nocardia, Rhodoccocci and Mycobacteria. Few phages infecting non-mycobacterial members of the Corynebacterineae have been characterized, and these would be good candidates for also encoding mycolylarabinogalactan esterases. We note that neither phage P2101 of Corynebacterium glutamicum (Chen et al., 2008) nor BFK20 of Brevibacterium flavum (Bukovska et al., 2006) encode a LysB relative, although unlike the Mycobacteria, mycolic acids are dispensable for growth of C. glutamicum (Portevin et al., 2004) and therefore may not pose a barrier to efficient lysis.

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