Charles Darwin University

CDU eSpace
Institutional Repository

 
CDU Staff and Student only
 

Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus

Turner, Mark S., Hafner, Louise M., Walsh, Terry and Giffard, Philip M. (2004). Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus. Applied and Environmental Microbiology,70(6):3673-3680.

Document type: Journal Article
Citation counts:
Google Scholar Search Google Scholar
Attached Files (Some files may be inaccessible until you login with your CDU eSpace credentials)
Name Description MIMEType Size Downloads
Download this reading Giffard_8902.pdf Published version application/pdf 783.39KB 40
Reading the attached file works best in Firefox, Chrome and IE 9 or later.

Title Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus
Author Turner, Mark S.
Hafner, Louise M.
Walsh, Terry
Giffard, Philip M.
Journal Name Applied and Environmental Microbiology
Publication Date 2004
Volume Number 70
Issue Number 6
ISSN 0099-2240   (check CDU catalogue open catalogue search in new window)
Start Page 3673
End Page 3680
Total Pages 8
Place of Publication Washington, United States
Publisher The American Society for Microbiology
Field of Research 0605 - Microbiology
0799 - Other Agricultural and Veterinary Sciences
1199 - Other Medical and Health Sciences
HERDC Category C1 - Journal Article (DEST)
Abstract Examination of supernatant fractions from broth cultures of Lactobacillus fermentum BR11 revealed the presence of a number of proteins, including a 27-kDa protein termed Sep. The amino-terminal sequence of Sep was determined, and the gene encoding it was cloned and sequenced. Sep is a 205-amino-acid protein and contains a 30-amino-acid secretion signal and has overall homology (between 39 and 92% identity) with similarly sized proteins of Lactobacillus reuteri, Enterococcus faecium, Streptococcus pneumoniae, Streptococcus agalactiae, and Lactobacillus plantarum. The carboxy-terminal 81 amino acids of Sep also have strong homology (86% identity) to the carboxy termini of the aggregation-promoting factor (APF) surface proteins of Lactobacillus gasseri and Lactobacillus johnsonii. The mature amino terminus of Sep contains a putative peptidoglycan-binding LysM domain, thereby making it distinct from APF proteins. We have identified a common motif within LysM domains that is shared with carbohydrate binding YG motifs which are found in streptococcal glucan-binding proteins and glucosyltransferases. Sep was investigated as a heterologous peptide expression vector in L. fermentum, Lactobacillus rhamnosus GG and Lactococcus lactis MG1363. Modified Sep containing an amino-terminal six-histidine epitope was found associated with the cells but was largely present in the supernatant in the L. fermentum, L. rhamnosus, and L. lactis hosts. Sep as well as the previously described surface protein BspA were used to express and secrete in L. fermentum or L. rhamnosus a fragment of human E-cadherin, which contains the receptor region for Listeria monocytogenes. This study demonstrates that Sep has potential for heterologous protein expression and export in lactic acid bacteria.
Keywords Lactobacillus
Lactococcus
DOI http://dx.doi.org/10.1128/AEM.70.6.3673-3680.2004   (check subscription with CDU E-Gateway service for CDU Staff and Students  check subscription with CDU E-Gateway in new window)


© copyright

Every reasonable effort has been made to ensure that permission has been obtained for items included in CDU eSpace. If you believe that your rights have been infringed by this repository, please contact digitisation@cdu.edu.au.

 
Versions
Version Filter Type
Access Statistics: 58 Abstract Views, 41 File Downloads  -  Detailed Statistics
Created: Mon, 12 Apr 2010, 01:49:26 CST