Commercially available complement component-depleted sera are unexpectedly codepleted of ficolin-2.
Commercially available complement component-depleted sera are unexpectedly codepleted of ficolin-2.
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市售的补体成分耗尽血清意外地同时去除了 ficolin-2。
DOI:
10.1128/cvi.00370-14
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发表时间:
2014
期刊:
影响因子:
--
通讯作者:
Nahm,MoonH
中科院分区:
文献类型:
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作者:
Brady,AllisonM;Geno,KAaron;Dalecki,AlexG;Cheng,Xiaogang;Nahm,MoonH
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 on Streptococcus 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 on Saccharomyces 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.