Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain

Becker, Stephen C.; Foster‐Frey, Juli; Stodola, Angeline J.; Anacker, Daniel C.; Donovan, David M.

doi:10.1016/j.gene.2009.04.023

Cited by 107 publications

(150 citation statements)

References 48 publications

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“…The presence of a double lytic system in Lactococcus KSY1, containing two holins (ORF 53b and ORF 72) and two endolysins (ORF 53a and ORF 73), can reinforce this hypothesis (98). The third group reported here relates to endolysins formed as a product of two adjacent genes containing group I introns, as reported for the staphylococcal phage endolysins X2, G1, and 85 (99) or staphylokinase in phage phiNM3. Concerning these endolysins, there is no report of these ORFs encoding a functional protein besides their homology with a NUMOD4 motif and an HNH endonuclease or staphylokinase in phage phiNM3.…”

Section: Resultssupporting

confidence: 78%

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Oliveira

Melo

Santos

et al. 2013

J Virol

242

247

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Phages are recognized as the most abundant and diverse entities on the planet. Their diversity is determined predominantly by their dynamic adaptation capacities when confronted with different selective pressures in an endless cycle of coevolution with a widespread group of bacterial hosts. At the end of the infection cycle, progeny virions are confronted with a rigid cell wall that hinders their release into the environment and the opportunity to start a new infection cycle. Consequently, phages encode hydrolytic enzymes, called endolysins, to digest the peptidoglycan. In this work, we bring to light all phage endolysins found in completely sequenced double-stranded nucleic acid phage genomes and uncover clues that explain the phage-endolysin-host ecology that led phages to recruit unique and specialized endolysins.

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Section: Resultssupporting

confidence: 78%

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Oliveira

Melo

Santos

et al. 2013

J Virol

242

247

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“…23 The number of EADs in the modular endolysins from Gram-positive-infecting phage also varies, with several having two, each encoding a different catalytic activity. 19,24,25 For instance, the staphylococcal phage phi11 endolysin has both an endopeptidase and an amidase. 26 Likewise, the streptococcal phage endolysin B30 has both an endopeptidase and a muramidase EAD.…”

Section: Endolysins -Peptidoglycan Degrading Enzymesmentioning

confidence: 99%

“…38,42 Furthermore, introns are rare in endolysin genes, but other exceptions do exist. 25 Engineering novel endolysin constructs The modular structure of endolysins provides an opportunity to engineer enzymes with altered bacteriolytic activity. Exchanging the CBD of S. aureus phage endolysin Ply187 with the Src Homology 3b (SH3b) CBD, from the endolysin LysK, improved staphylolytic activity of the chimeric enzyme tenfold over native Ply187.…”

Section: Endolysins -Peptidoglycan Degrading Enzymesmentioning

confidence: 99%

“…Furthermore, the extracellular site of action for PGH makes it improbable that resistance will come from one the majority of known antimicrobial resistance mechanisms that tend to act intracellularly on invading small-molecules (i.e., reduced membrane permeability, active efflux pumps, inactivation of antimicrobials by cytoplasmic enzymes, modified site of action). 25 Furthermore, if endolysin resistance does occur, the large number and variety of phages and the ease of engineering endolysins provides us with a constant source of new PGHs.…”

Section: Resistance To Endolysinsmentioning

confidence: 99%

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Antimicrobial bacteriophage-derived proteins and therapeutic applications

2015

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“…Such an assumed evolutionary relationship between endolysins and autolysins would be another example of horizontal gene transfer between bacteriophages and their host bacterial cells, an event also reported for other genes (Hambly & Suttle 2005). The development and preparation of chimerical endolysins from heterologous functional domains can be a good strategy to obtain highly effective and soluble peptidoglycan hydrolases, either with narrow or broad lytic spectrum (Yoong et al 2004;Donovan et al 2006;Becker et al 2009;Manoharadas et al 2009;Daniel et al 2010;Idelevich et al 2011;Pastagia et al 2011;Fernandes et al 2012).…”

Section: Discussionmentioning

confidence: 85%

Bioinformatics analysis of bacteriophage and prophage endolysin domains

Vidová¹,

Šrámková²,

Tišáková³

et al. 2014

Biologia

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Endolysins as a class of antibacterial enzymes are expected to become a very useful tool for many purposes to control spreading of, e.g., multiresistant bacteria in different environments. Their antimicrobial properties could be broadened or altered by mutagenesis, domain swapping or gene shuffling. Therefore, the specific designing of endolysins to achieve their desired properties is challenging. This work is focused on the in silico analysis of protein domains presence in sequences of phage and prophage endolysins, followed by the study of variety of domain combinations in the individual endolysin types. The multiple sequence alignment of endolysin sequences revealed the recognition of sequence types with typical domain arrangement and conserved amino acids, divided according to the target substrate in bacterial cell walls. The five protein families of catalytic domains are specifically occurring in dependence of bacterial Gram-type. The presence, types and numbers of binding domains within endolysin sequences were also studied. The obtained results enable a more targeted design of endolysins with required antimicrobial properties.

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Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain

Cited by 107 publications

References 48 publications

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Antimicrobial bacteriophage-derived proteins and therapeutic applications

Bioinformatics analysis of bacteriophage and prophage endolysin domains

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