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Neutralization of viral infectivity by zebrafish c-reactive protein isoforms

Bello-Perez, Melissa, Falco, Alberto, Medina-Gali, Regla, Pereiro, Patricia, Encinar, Jose Antonio, Novoa, Beatriz, Perez, Luis, Coll, Julio
Molecular Immunology 2017 v.91 pp. 145-155
C-reactive protein, Danio rerio, adaptive immunity, antiviral properties, bacterial infections, biomarkers, coronary disease, eggs, genes, inflammation, microarray technology, mutants, neutralization, pathogenicity, protein isoforms, proteomics, viremia, viruses
This work explores the unexpected in vivo and in vitro anti-viral functions of the seven c-reactive protein (crp1-7) genes of zebrafish (Danio rerio). First results showed heterogeneous crp1-7 transcript levels in healthy wild-type zebrafish tissues and organs and how those levels heterogeneously changed not only after bacterial but also after viral infections, including those in adaptive immunity-deficient rag1−/− mutants. As shown by microarray hybridization and proteomic techniques, crp2/CRP2 and crp5/CRP5 transcripts/proteins were among the most modulated during in vivo viral infection situations including the highest responses in the absence of adaptive immunity. In contrast crp1/CRP1/and crp7/CRP7 very often remained unmodulated. All evidences suggested that zebrafish crp2-6/CRP2-6 may have in vivo anti-viral activities in addition to their well known anti-bacterial and/or physiological functions in mammalians. Confirming those expectations, in vitro neutralization and in vivo protection against spring viremia carp virus (SVCV) infections were demonstrated by crp2-6/CRP2-6 using crp1-7 transfected and/or CRP1-7-enriched supernatant-treated fish cells and crp2-5-injected one-cell stage embryo eggs, respectively. All these findings discovered a crp1-7/CRP1-7 primitive anti-viral functional diversity.These findings may help to study similar functions on the one-gene-coded human CRP, which is widely used as a clinical biomarker for bacterial infections, tissue inflammation and coronary heart diseases.