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LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions

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ABSTRACT

Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered new chimeric enzymes comprising the enzymatically active domain (EAD) of autolysin LytM from S. aureus and the cell wall binding domain (CBD) from bacteriocin lysostaphin. They display potent activity in extended environmental conditions. Our results exemplify the possibility of exploring autolytic enzymes in engineering lysins with desired features. Moreover, they suggest a possible mechanism of autolysin physiological activity regulation by local ionic environments in the cell wall.

No MeSH data available.


Lysin constructs. Numbers in boxes represent amino acid positions in full-length proteins according to UniProt.
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f1: Lysin constructs. Numbers in boxes represent amino acid positions in full-length proteins according to UniProt.

Mentions: One of the best characterized S. aureus autolysin is LytM, Zn2+-dependent glycylglycine endopeptidase,31–34 with a characteristic HxH motif that belongs to the MEROPS M23 family of metallopeptidases.35 Full-length LytM protein remains inactive against purified PGNs or live S. aureus and only truncated enzyme (residues 185–316, Fig. 1), which lacks the N-terminal fragment and the occluding region, shows a high lytic activity.34 The C-terminal region of LytM (LytM enzymatically active domain, LytM_EAD) has high similarity to the lysostaphin enzymatically active domain, Lss_EAD (52% amino acid identity over 106 residues). Both enzymes are well characterized not only biochemically but also structurally.24,34,36,37


LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions
Lysin constructs. Numbers in boxes represent amino acid positions in full-length proteins according to UniProt.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC5036312&req=5

f1: Lysin constructs. Numbers in boxes represent amino acid positions in full-length proteins according to UniProt.
Mentions: One of the best characterized S. aureus autolysin is LytM, Zn2+-dependent glycylglycine endopeptidase,31–34 with a characteristic HxH motif that belongs to the MEROPS M23 family of metallopeptidases.35 Full-length LytM protein remains inactive against purified PGNs or live S. aureus and only truncated enzyme (residues 185–316, Fig. 1), which lacks the N-terminal fragment and the occluding region, shows a high lytic activity.34 The C-terminal region of LytM (LytM enzymatically active domain, LytM_EAD) has high similarity to the lysostaphin enzymatically active domain, Lss_EAD (52% amino acid identity over 106 residues). Both enzymes are well characterized not only biochemically but also structurally.24,34,36,37

View Article: PubMed Central - PubMed

ABSTRACT

Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered new chimeric enzymes comprising the enzymatically active domain (EAD) of autolysin LytM from S. aureus and the cell wall binding domain (CBD) from bacteriocin lysostaphin. They display potent activity in extended environmental conditions. Our results exemplify the possibility of exploring autolytic enzymes in engineering lysins with desired features. Moreover, they suggest a possible mechanism of autolysin physiological activity regulation by local ionic environments in the cell wall.

No MeSH data available.