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1.E.24 The Bacterophase Dp-1 Holin (Dp-1 Holin) Family

The genes coding for the lytic system of the pneumococcal phage, Dp-1, has been cloned and characterized (Sheehan et al., 1997). The lytic enzyme of this phage (Pal), an N-acetyl-muramoyl-L-alanine amidase, shows a modular organization similar to that described for the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. The construction of chimeric enzymes between pneumococcus and bacteria (or phages) that belong to different Gram-positive families has shown that the interchange of functional domains switches enzyme specificity.

The holin of phage Dp-1 is 74 aas long with two probable TMSs (residues 12-32 and 39-57). It shows sequence similarity (30% identity) with a holin encoded within the genone of Enterococcus faecalis (Paulsen et al., 2003). Several Gram-positive bacteria and their phage also possess this family of holins, representatives of which are listed in the table.

References associated with 1.E.24 family:

Escobedo, S., A.B. Campelo, U. Wegmann, P. García, A. Rodríguez, and B. Martínez. (2019). Insight into the Lytic Functions of the Lactococcal Prophage TP712. Viruses 11:. 31546996
Labrie, S., N. Vukov, M.J. Loessner, and S. Moineau. (2004). Distribution and composition of the lysis cassette of Lactococcus lactis phages and functional analysis of bacteriophage ul36 holin. FEMS Microbiol. Lett. 233: 37-43. 15043867
Paulsen, I.T., L. Banerjei, G.S.A. Myers, K.E. Nelson, R. Seshadri, T.D. Read, D.E. Fouts, J.A. Eisen, S.R. Gill, J.F. Heidelberg, H. Tettelin, R.J. Dodson, L. Umayam, L. Brinkac, M. Beanan, S. Daugherty, R.T. DeBoy, S. Durkin, J. Kolonay, R. Madupu, W. Nelson, J. Vamathevan, B. Tran, J. Upton, T. Hansen, J. Shetty, H. Khouri, T. Utterback, D. Radune, K.A. Ketchum, B.A. Dougherty, and C.M. Fraser. (2003). Role of Mobile DNA in the Evolution of Vancomycin-Resistant Enterococcus faecalis. Science. 299: 2071-2074. 12663927
Roces, C., A.B. Campelo, S. Escobedo, U. Wegmann, P. García, A. Rodríguez, and B. Martínez. (2016). Reduced Binding of the Endolysin LysTP712 to Lactococcus lactis ΔftsH Contributes to Phage Resistance. Front Microbiol 7: 138. 26904011
Sheehan, M.M., García, J.L., López R., and García P. (1997). The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of intergeneric origin. Mol Microbiol. 25: 717-725. 9379901