| Literature DB >> 19549817 |
Timothy J LaRocca1, David J Holthausen, Chyongere Hsieh, Christian Renken, Carmen A Mannella, Jorge L Benach.
Abstract
A complement-independent bactericidal IgG1 against the OspB of Borrelia burgdorferi increased the permeability of the outer membrane through the creation of openings of 2.8 - 4.4 nm, resulting in its osmotic lysis. Cryo-electron microscopy and tomography demonstrated that exposure to the antibody causes the formation of outer membrane projections and large breaks which may precede the increase in permeability of the outer membrane. The bactericidal effect of this antibody is not transferable to Escherichia coli expressing rOspB on its outer membrane. Additionally, the porin P66, the only protein that coprecipitated with OspB, is dispensable for the bactericidal mechanism.Entities:
Mesh：
Substances：
Year: 2009 PMID： 19549817 PMCID： PMC2705580 DOI： 10.1073/pnas.0901858106
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205