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Eric A. Lefevre

Researcher at Institute for Animal Health

Publications -  21
Citations -  1261

Eric A. Lefevre is an academic researcher from Institute for Animal Health. The author has contributed to research in topics: B cell & Antigen. The author has an hindex of 14, co-authored 21 publications receiving 1198 citations. Previous affiliations of Eric A. Lefevre include Institut Gustave Roussy & French Institute of Health and Medical Research.

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Regulation of CCR6 chemokine receptor expression and responsiveness to macrophage inflammatory protein-3α/CCL20 in human B cells

TL;DR: Data suggest that restricted patterns of CCR6 expression and MIP-3alpha/CCL20 responsiveness are integral parts of the process of B-lineage maturation and antigen-driven B-cell differentiation.
Journal Article

Antigen receptor engagement selectively induces macrophage inflammatory protein-1 alpha (MIP-1 alpha) and MIP-1 beta chemokine production in human B cells.

TL;DR: It is shown that B cell Ag receptor (BCR) triggering, but not stimulation by CD40 mAb and/or IL-4, rapidly induced the coordinated expression of two closely related T cell chemoattractants, macrophage inflammatory protein-1 beta and MIP-1 alpha, by human B cells.
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BAFF enhances chemotaxis of primary human B cells: a particular synergy between BAFF and CXCL13 on memory B cells

TL;DR: The findings indicate a previously unreported role for the BAFF/BAFF-R pair in mature B-cell chemotaxis and the synergy between CXCL13 and BAFF produced by stromal cells and follicular dendritic cells may have important implications for B- Cell homeostasis, the development of normal B- cell areas, and for the formation of germinal center-like follicles that may be observed in various autoimmune diseases.
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Foot-and-Mouth Disease Virus Can Induce a Specific and Rapid CD4+ T-Cell-Independent Neutralizing and Isotype Class-Switched Antibody Response in Naïve Cattle

TL;DR: CD4+ T-cell-independent antibody responses play a major role in the resolution of foot-and-mouth disease in cattle, and depletion was found to substantially inhibit antibody responses to the G-H peptide loop VP1135-156 on the viral capsid.