Dissimilar and similar functional properties of complement receptor-3 in microglia and macrophages in combating yeast pathogens by phagocytosis

✍ Scribed by Smadar Hadas; Fanny Reichert; Shlomo Rotshenker

• Publisher: John Wiley and Sons
• Year: 2010
• Tongue: English
• Weight: 397 KB
• Volume: 58
• Category: Article
• ISSN: 0894-1491
• DOI: 10.1002/glia.20966

✦ Synopsis

Abstract

Central nervous system (CNS) microglia (MG) and peripheral tissue macrophages (MO) remove pathogens by phagocytosis. Zymosan, a model yeast pathogen, is a β‐glucan rich particle that readily activates the complement system and then becomes C3bi‐opsonized (op). Complement receptor‐3 (CR3) has initially been implicated in mediating the phagocytosis of both C3bi‐op and non‐opsonized (nop) zymosan by MO through C3bi and β‐glucan binding sites, respectively. Later, the role of CR3 as a phagocytic β‐glucan receptor has been questioned and the supremacy of β‐glucan receptor Dectin‐1 advocated. We compare here between primary mouse CNS MG and peripheral tissue MO with respect to CR3 and Dectin‐1 mediated phagocytosis of C3bi‐op and nop zymosan. We report that MG and MO display similar as well as dissimilar functional properties in this respect. Although CR3 and Dectin‐1 function both as β‐glucan/non‐opsonic receptors in MG during nop zymosan phagocytosis, Dectin‐1, but not CR3, does so in MO. CR3 functions also as a C3bi/opsonic receptor in MG and MO during C3bi‐op zymosan phagocytosis, leading to phagocytosis which is more efficient than that of nop zymosan. Dectin‐1 contributes, albeit less than CR3, to phagocytosis of C3bi‐op zymosan in MG and further less in MO, suggesting that C3bi‐opsonization does not block all β‐glucan sites on zymosan from binding Dectin‐1 on phagocytes. Thus, altogether CR3 and Dectin‐1 contribute both to phagocytosis of nop and C3bi‐op zymosan in MG, whereas MO switch from CR3‐independent/Dectin‐1‐dependent phagocytosis of nop zymosan to phagocytosis of C3bi‐op zymosan where CR3 dominates over Dectin‐1. © 2010 Wiley‐Liss, Inc.