African swine fever virus protein p30 interaction with heterogeneous nuclear ribonucleoprotein K (hnRNP-K) during infection

Heterogeneous nuclear ribonucleoprotein K (hnRNP-K) was identified as interacting cellular protein with the abundant immediate early protein p30 from African swine fever virus (ASFV) in a macrophage cDNA library screening. The interacting regions of hnRNP-K with p30 were established within residues 35–197, which represent KH1 and KH2 domains responsible for RNA binding. Colocalization of hnRNP-K and p30 was observed mainly in the nucleus, but not in the cytoplasm of infected cells and infection modified hnRNP-K subcellular distribution and decreased the incorporation of 5-fluorouridine into nascent RNA. Since similar effects were observed in cells transiently expressing p30, this interaction provides new insights into p30 function and could represent a possible additional mechanism by which ASFV downregulates host cell mRNA translation. STRUCTURED SUMMARY: MINT-6742660: hnRNP-K (uniprotkb:P61978) physically interacts (MI:0218); with p30 (uniprotkb:Q8V1E7) by pull down (MI:0096). MINT-6742673, MINT-6742696, MINT-6742729: hnRNP-K (uniprotkb:P61978) physically interacts (MI:0218); with p30 (uniprotkb:Q8V1E7) by two hybrid (MI:0018). MINT-6742711: p30 (uniprotkb:Q8V1E7) and hnRNP-K (uniprotkb:P61978) colocalize (MI:0403) by fluorescence microscopy (MI:0416).