A leucine-rich repeat motif of Leishmania parasite surface antigen 2 binds to macrophages through the complement receptor 3
- Author(s)
- Kedzierski, L; Montgomery, J; Bullen, D; Curtis, J; Gardiner, E; Jimenez-Ruiz, A; Handman, E;
- Details
- Publication Year 2004-04-15,Volume 172,Issue #8,Page 4902-4906
- Journal Title
- JOURNAL OF IMMUNOLOGY
- Publication Type
- Journal Article
- Abstract
- Membrane glycoconjugates on the Leishmania parasites, notably leishmanolysin and lipophosphoglycan, have been implicated in attachment and invasion of. host macrophages. However, the function of parasite surface Ag 2 (PSA-2) and membrane proteo-phosphoglycan (PPG) has not been elucidated. In this study we demonstrate that native and recombinant Leishmania infantum PSA-2, which consists predominantly of 15 leucine-rich repeats (LRR) and a recombinant LRR domain derived from L. major PPG, bind to macrophages. The interaction is restricted to macrophages and appears to be calcium independent. We have investigated the PSA-2-macrophage interaction to identify the host receptor involved in binding and we show that binding of PSA-2 to macrophages can be blocked by Abs to the complement receptor 3 (CR3, Mac-1). Data derived from mouse macrophage studies were further confirmed using cell lines expressing human CR3, and showed that PSA-2 also binds to the human receptor. This is the first demonstration of a functional role for PSA-2. Our data indicate that in addition to leishmanolysin and lipophosphoglycan, parasite attachment and invasion of macrophages involve a third ligand comprising the LRRs shared by PSA-2 and PPG and that these interactions occur via the CR3.
- Publisher
- AMER ASSOC IMMUNOLOGISTS
- Keywords
- MAJOR SURFACE GLYCOPROTEIN; INTEGRIN MAC-1 CD11B/CD18; LIPOPHOSPHOGLYCAN LPG; PROMASTIGOTES; AMASTIGOTES; PROTEOPHOSPHOGLYCAN; RECOGNITION; PROTEINS; ADHESION; FAMILY
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2004-04-15 12:00:00