Table 1.
N-terminal donor | C-terminal donor | Property | Antimicrobial spectrum | Ref. | |
---|---|---|---|---|---|
CHIMEOLYSIN | |||||
ClyS | Phage Twort lysin plyTW, endopeptidase | phiNM3 lysin | Highly soluble, superiority to mupirocin for skin decolonization | Staphylococci | Daniel et al., 2010; Pastagia et al., 2011 |
Lys168-87 | E. faecalis phage F168/08 lysin, CHAPa | Phage 87 lysin Lys87b | Highly soluble, broad antimicrobial activity | Staphylococci, E. faecalis, E. faecium, S. pyogenes | Fernandes et al., 2012 |
Lys170-87 | E. faecalis phage F170/08 lysin, amidase | Phage 87 lysin Lys87b | Highly soluble, broad antimicrobial activity | Staphylococci, E. faecalis, E. faecium, S. pyogenes | Fernandes et al., 2012 |
PRF-119 | Phage K lysin plyK, CHAP | Lysostaphin, SH3b like domain | Very good activity | Staphylococci | Idelevich et al., 2011 |
λ SA2-E-Lyso-SH3b | Phage λ SA2 lysin, endopeptidase | Lysostaphin, SH3b like domain | Increased activity and extended lytic spectrum | Staphylococci, Streptococci | Becker et al., 2009; Schmelcher et al., 2012 |
λ SA2-E-LysK-SH3b | Phage λ SA2 lysin, endopeptidase | LysK, SH3b like domain | Increased activity and extended lytic spectrum | Staphylococci, Streptococci | Becker et al., 2009; Schmelcher et al., 2012 |
B30-182-Lyso | Phage B30 lysin, endopeptidase | Lysostaphin, SH3b like domain | Extended lytic spectrum and binding capacity | S. aureus, S. uber, S. agalactiae, S. dysgalactiae | Donovan et al., 2006a |
Ply187AN-KSH3b | Phage 187 lysin Ply187, amidase | LysK, SH3b like domain | Improved lytic activity | Staphylococci | Mao et al., 2013 |
ClyH | Phage 187 lysin Ply187, amidase | phiNM3 lysin | Improved lytic activity and extended lytic spectrum | Staphylococci, S. sobrinus | Yang et al., 2014 |
Ply187N-V12C | Phage 187 lysin Ply187, amidase | Lysin PlyV12, SH3b like domain | Extend lytic spectrum | Staphylococci, Streptococci, Enterococci | Dong et al., 2014 |
ARTILYSIN | |||||
P128 | tail-associated enzyme of Phage K | Lysostaphin, SH3b like domain | High lytic activity | Staphylococci | Vipra et al., 2012 |
P16-17 | Phage p68 lysin p16, CHAP | Minor coat protein 17 of phage p68b | Highly soluble | S. aureus | Manoharadas et al., 2009 |
CLL | lysin Cpl-1, lysozyme | LytA C-terminal domain | Altered binding capacity | Streptococci | Diaz et al., 1990 |
CLA | LytA amidase domain | Lysin Cpl-1 binding domain | Altered binding capacity | Streptococci | Diaz et al., 1990 |
Art-085 | SMAP-29 peptide | Lysin KZ144 | Kills Gram-negative bacteria | P. aeruginosa, P. syringae, P. putida | Briers et al., 2014a |
Pesticin-like | T4 lysozyme | Pesticin | Kills Gram-negative bacteria | Yersinia, E. coli expressing FyuA | Lukacik et al., 2012 |
LoGT series | Various peptidesc | Various lysinsd | Kills Gram-negative bacteria | P. aeruginosa, A. baumannii, E. coli, S. Typhimurium | Briers et al., 2014b |
CHAP: cysteine and histidine-dependent aminopeptidase/hydrolase.
The characters of these CBDs cannot be confirmed for their sequences are unavailable.
These peptides include α4, MW1, MW2, polycationic peptide (PCNP), hydrophobic pentapeptide (HPP), Parasin1 (Pa1), and lycotoxin1 (Ly1).
These lysins include OBPgp279 (YP_004958186.1), PVP-SE1gp146 (YP_004893953.1), phiKZgp144 (NP_803710.1), 201ϕ 2-1gp229 (YP_001956952.1), CR8gp3.5, P2gp09 (NP_046765.1), and PsP3gp10 (NP_958065.1).