Key result
PCBP1 interacts with CSFV N(pro) to promote viral growth and downregulate type I interferon.
Cellular PCBP1 interacts with CSFV N(pro) protein and positively modulates viral growth while downregulating type I interferon.
PCBP1 modulation of CSFV growth and interferon is hypothesis-generating; leaves open its value as antiviral target pending in vivo validation.
N(pro) is a multifunctional autoprotease unique to pestiviruses. The interacting partners of the N(pro) protein of classical swine fever virus (CSFV), a swine pestivirus, have been insufficiently defined. Using a yeast two-hybrid screen, we identified poly(C)-binding protein 1 (PCBP1) as a novel interacting partner of the CSFV N(pro) protein and confirmed this by coimmunoprecipitation, glutathione S-transferase (GST) pulldown, and confocal assays. Knockdown of PCBP1 by small interfering RNA suppressed CSFV growth, while overexpression of PCBP1 promoted CSFV growth. Furthermore, we showed that type I interferon was downregulated by PCBP1, as well as N(pro). Our results suggest that cellular PCBP1 positively modulates CSFV growth.
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Li et al. (2012) studied Classical swine fever virus (CSFV) infection. PCBP1 knockdown or overexpression was evaluated on CSFV growth and type I interferon regulation. Poly(C)-binding protein 1 (PCBP1) interacts with the CSFV N(pro) protein, and its expression positively modulates classical swine fever virus growth while downregulating type I interferon.
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