Search anything and hit enter
  • Teams
  • Members
  • Projects
  • Events
  • Calls
  • Jobs
  • publications
  • Software
  • Tools
  • Network
  • Equipment

A little guide for advanced search:

  • Tip 1. You can use quotes "" to search for an exact expression.
    Example: "cell division"
  • Tip 2. You can use + symbol to restrict results containing all words.
    Example: +cell +stem
  • Tip 3. You can use + and - symbols to force inclusion or exclusion of specific words.
    Example: +cell -stem
e.g. searching for members in projects tagged cancer
Search for
Count
IN
OUT
Content 1
  • member
  • team
  • department
  • center
  • program_project
  • nrc
  • whocc
  • project
  • software
  • tool
  • patent
  • Administrative Staff
  • Assistant Professor
  • Associate Professor
  • Clinical Research Assistant
  • Full Professor
  • Graduate Student
  • Lab assistant
  • Non-permanent Researcher
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Operations
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
Content 2
  • member
  • team
  • department
  • center
  • program_project
  • nrc
  • whocc
  • project
  • software
  • tool
  • patent
  • Administrative Staff
  • Assistant Professor
  • Associate Professor
  • Clinical Research Assistant
  • Full Professor
  • Graduate Student
  • Lab assistant
  • Non-permanent Researcher
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Operations
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
Search
Go back
Scroll to top
Share
© Pierre Gounon
Entrée de Listeria dans une cellule épithéliale (Grossissement X 10000). Image colorisée.
Publication : Molecular microbiology

Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of gram-positive bacteria

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular microbiology - 01 Dec 1999

Jonquières R, Bierne H, Fiedler F, Gounon P, Cossart P

Link to Pubmed [PMID] – 10594817

Mol. Microbiol. 1999 Dec;34(5):902-14

InlB is a Listeria monocytogenes protein that is sufficient to promote entry in a variety of mammalian cells. The last 232-amino-acid domain (Csa) of InlB has been shown to mediate attachment on the listerial surface, although its sequence does not suggest any known mechanism of association to the bacterial surface. InlB is present both on the bacterial surface and in culture supernatants. As has been recently demonstrated, both forms of InlB, soluble and surface-bound, can trigger signalling in host cells. To elucidate the specific role of each of the two forms, it was important to understand how InlB associates with the bacterial surface. Using microscopy, we find evidence that InlB is partially buried in the cell wall layer, and using fractionation experiments we demonstrate that InlB associates with the bacterial cytoplasmic membrane. Moreover, using purified lipoteichoic acid (LTA) and the three polypeptides InlB, Csa, or InlBDeltaCsa (InlB lacking the last 232 amino acids), we demonstrate that LTA is a ligand for the Csa domain of InlB. These results provide the first evidence of an interaction between lipoteichoic acids and a bacterial protein involved in adhesion and signalling, and highlight a new mechanism of protein association on the surface of Gram-positive bacteria.

http://www.ncbi.nlm.nih.gov/pubmed/10594817