Commercially Available Complement Component-Depleted Sera Are Unexpectedly Codepleted of Ficolin-2

Autor: Moon H. Nahm, Allison M. Brady, Xiaogang Cheng, K. Aaron Geno, Alex G. Dalecki
Rok vydání: 2014
Předmět:
Zdroj: Clinical and Vaccine Immunology. 21:1323-1329
ISSN: 1556-679X
1556-6811
DOI: 10.1128/cvi.00370-14
Popis: The ficolins are a family of innate pattern recognition molecules that are known to bind acetylated compounds and activate complement through the association of mannose binding lectin (MBL)/ficolin-associated serine proteases (MASPs). Their importance has more recently become appreciated, as they have been shown to play a role in a variety of disease processes from infection to autoimmunity. While studying ficolin-2-mediated complement deposition onStreptococcus pneumoniae, we found that sera depleted of C1q or other complement components were also codepleted of ficolin-2 but not ficolin-1, ficolin-3, or MBL. MBL present in C1q-depleted sera was able to mediate complement deposition onSaccharomyces cerevisiae, suggesting the presence of MASPs. We found that complement was activated on pneumococci in C1q-depleted serum only after opsonization with exogenous recombinant ficolin-2 (rFicolin-2). Also, no complement deposition was observed in C1q-depleted serum when pneumococci were opsonized with rFicolin-2 mutated at its lysine-57 residue, where MASPs are known to associate. Thus, these depleted sera are a unique tool to study ficolin-2-mediated complement pathways; however, one should be aware that ficolin-2 is absent from complement component-depleted sera.
Databáze: OpenAIRE