Identification, characterisation and specificity of a cell wall lytic enzyme from Lactobacillus fermentum BR11

Turner, Mark S., Hafner Louise M., Walsh, Terry and Giffard, Philip M. (2004) Identification, characterisation and specificity of a cell wall lytic enzyme from Lactobacillus fermentum BR11. FEMS Microbiology Letters, 238 1: 9-15. doi:10.1016/j.femsle.2004.07.008


Author Turner, Mark S.
Hafner Louise M.
Walsh, Terry
Giffard, Philip M.
Title Identification, characterisation and specificity of a cell wall lytic enzyme from Lactobacillus fermentum BR11
Journal name FEMS Microbiology Letters   Check publisher's open access policy
ISSN 0378-1097
1574-6968
Publication date 2004-09-01
Sub-type Article (original research)
DOI 10.1016/j.femsle.2004.07.008
Volume 238
Issue 1
Start page 9
End page 15
Total pages 7
Place of publication Oxford England
Publisher Blackwell Publishing
Language eng
Subject 0605 Microbiology
Abstract Screening of a genomic library with an antiserum raised against whole Lactobacillus fermentum BR11 cells identified a clone expressing an immunoreactive 37-kDa protein. Analysis of the 3010-bp DNA insert contained within the clone revealed four open reading frames (ORFs). One ORF encodes LysA, a 303 amino acid protein which has up to 35% identity with putative endolysins from prophages Lj928 and Lj965 from Lactobacillus johnsonii and Lp1 and Lp2 from Lactobacillus plantarum as well as with the endolysin of Lactobacillus gasseri bacteriophage Φadh. The immunoreactive protein was shown to be encoded by a truncated ORF downstream of lysA which has similarity to glutamyl-tRNA synthetases. The N-terminus of LysA has sequence similarity with N-acetylmuramidase catalytic domains while the C-terminus has sequence similarity with putative cell envelope binding bacterial SH3b domains. C-terminal bacterial SH3b domains were identified in the majority of Lactobacillus bacteriophage endolysins. LysA was expressed in Escherichia coli and unusually was found to have a broad bacteriolytic activity range with activity against a number of different Lactobacillus species and against Lactococcus lactis, streptococci and Staphylococcus aureus. It was found that LysA is 2 and 8000 times more active against L. fermentum than L. lactis and Streptococcus pyogenes, respectively.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Agriculture and Food Sciences
 
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