Antibacterial activity of Bacillus amyloliquefaciens phage endolysin without holin conjugation

Morita, Masatomo; Tanji, Yasunori; Mizoguchi, Katsunori; Soejima, Aya; Orito, Yuji; Unno, Hajime

doi:10.1016/s1389-1723(01)80275-9

Cited by 31 publications

(9 citation statements)

References 14 publications

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“…In general, pH optima above 8.0 seem uncommon for cell wall hydrolases. In fact, most other phage and bacterial lysins studied require neutral or slightly acidic conditions, with activity rapidly decreasing above pH 7.5 or 8 (Vasala et al 1995;Morita et al 2001;Loeffler et al 2003;Pritchard et al 2004;Yoong et al 2004;Cheng and Fischetti 2006;Donovan et al 2006;Fukushima et al 2007;Sugahara et al 2007). However, another L-alanoyl-D-glutamate peptidase from E. coli phage T5 revealed a pH profile similar to the enzymes reported here, with highest activity at pH 8.5 (Mikoulinskaia et al 2009).…”

Section: Discussionmentioning

confidence: 99%

Listeria bacteriophage peptidoglycan hydrolases feature high thermoresistance and reveal increased activity after divalent metal cation substitution

Schmelcher

Waldherr

Loessner

2011

Appl Microbiol Biotechnol

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The ability of the bacteriophage-encoded peptidoglycan hydrolases (endolysins) to destroy Gram-positive bacteria from without makes these enzymes promising antimicrobials. Recombinant endolysins from Listeria monocytogenes phages have been shown to rapidly lyse and kill the pathogen in all environments. To determine optimum conditions regarding application of recombinant Listeria phage endolysins in food or production equipments, properties of different Listeria endolysins were studied. Optimum NaCl concentration for the amidase HPL511 was 200 nM and 300 mM for the peptidases HPL118, HPL500, and HPLP35. Unlike most other peptidoglycan hydrolases, all four enzymes exhibited highest activity at elevated pH values at around pH 8-9. Lytic activity was abolished by EDTA and could be restored by supplementation with various divalent metal cations, indicating their role in catalytic function. While substitution of the native Zn 2+ by Ca 2+ or Mn 2+ was most effective in case of HPL118, HPL500, and HPLP35, supplementation with Co 2+ and Mn 2+ resulted in an approximately 5-fold increase in HPL511 activity. Interestingly, the glutamate peptidases feature a conserved SxHxxGxAxD zinc-binding motif, which is not present in the amidases, although they also require centrally located divalent metals for activity.The endolysins HPL118, HPL511, and HPLP35 revealed a surprisingly high thermostability, with up to 35% activity remaining after 30 min incubation at 90°C. The available data suggest that denaturation at elevated temperatures is reversible and may be followed by rapid refolding into a functional state.

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Section: Discussionmentioning

confidence: 99%

Listeria bacteriophage peptidoglycan hydrolases feature high thermoresistance and reveal increased activity after divalent metal cation substitution

Schmelcher

Waldherr

Loessner

2011

Appl Microbiol Biotechnol

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“…A partial list includes the Twort endolysin (Loessner et al, 1998), B30 endolysin (Donovan et al, 2006b), λSa2 endolysin , Ф11 endolysin (Donovan et al, 2006c;Sass and Bierbaum, 2007), and the Bacillus amyloliquifaciens endolysin (Morita et al, 2001). Some of these efforts have yielded truncations with a greater lytic specific activity than the full length PG hydrolase e.g.…”

Section: A Swapping And/or Combining Endolysin Domainsmentioning

confidence: 99%

Endolysins as Antimicrobials

Nelson

Schmelcher²,

Rodríguez-Rubio

et al. 2012

Advances in Virus Research

310

330

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“…93 Likewise, the Gram-positive Bacillus amyloliquefaciens phage endolysin Lys1521 can naturally lyse several P. aeruginosa and E. coli strains. 90,94,95 These types of endolysins tend to contain an amphipathic (both hydrophobic and hydrophilic regions) or highly cationic region, which interacts with the negatively charged surface lipopolysaccharides (LPS) to transverse the outer membrane. 20,22,90,94,95 The Gram-negative Acinetobacter baumannii phage endolysin LysAB2, with a predicted Cterminus amphipathic region, has broad lytic activity for both Gram-positive and Gram-negative hosts.…”

Section: Gram-negative Bacteria Infectionsmentioning

confidence: 99%