Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 78, Issue 7, Pages 2241-2248Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.07621-11
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Funding
- Agricultural Research Service and Cooperator Instituto de Productos Lacteos de Asturias, CSIC, Spain [58-1265-0-092FN, PIE200970I090]
- Ministry of Science and Innovation, Spain [AGL2009-13144-C02-01]
- Science, Technology and Innovation Programme, Principado de Asturias, Spain [IB08-052]
- NIH [1RO1AI075077-01A1]
- NRI [2007-35204-18395]
- U.S. State Department
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Virion-associated peptidoglycan hydrolases have potential as antimicrobial agents due to their ability to lyse Gram-positive bacteria on contact. In this work, our aim was to improve the lytic activity of HydH5, a virion-associated peptidoglycan hydrolase from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88. Full-length HydH5 and two truncated derivatives containing only the CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) domain exhibited high lytic activity against live S. aureus cells. In addition, three different fusion proteins were created between lysostaphin and HydH5, each of which showed higher staphylolytic activity than the parental enzyme or its deletion construct. Both parental and fusion proteins lysed S. aureus cells in zymograms and plate lysis and turbidity reduction assays. In plate lysis assays, HydH5 and its derivative fusions lysed bovine and human S. aureus strains, the methicillin-resistant S. aureus (MRSA) strain N315, and human Staphylococcus epidermidis strains. Several nonstaphylococcal bacteria were not affected. HydH5 and its derivative fusion proteins displayed antimicrobial synergy with the endolysin LysH5 in vitro, suggesting that the two enzymes have distinct cut sites and, thus, may be more efficient in combination for the elimination of staphylococcal infections.
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