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To complete their lifecycle, viruses interacts with variety of cellular proteins. Identifying host proteins involved in the viral lifecycle is an excellent target for drug. In neuro-2a cells, we employed recombinant Chandipura virus (CHPV) nucleoprotein (N) as bait in a protein pull down assay to see which cellular proteins interact with nucleoprotein. A total of ten proteins interact with the CHPV N protein. Out of ten proteins, heat shock cognate 71 (HSC70) protein was investigated further. In CHPV-infected neuro-2a cells, confocal microscopy revealed that HSC70 co-localized with CHPV N protein, and that the expression was altered by viral infection. The association with HSC70 may help to mitigate the negative repercussions of misfolded proteins produced by viral polymerase's erroneous nature. More research on the role of these proteins in viral replication in infected cells is needed.

To complete their lifecycle, viruses interacts with variety of cellular proteins. Identifying host proteins involved in the viral lifecycle is an excellent target for drug. In neuro-2a cells, we employed recombinant Chandipura virus (CHPV) nucleoprotein (N) as bait in a protein pull down assay to see which cellular proteins interact with nucleoprotein. A total of ten proteins interact with the CHPV N protein. Out of ten proteins, heat shock cognate 71 (HSC70) and actin proteins were investigated further. In CHPV-infected neuro-2a cells, confocal microscopy revealed that HSC70 and actin co-localized with CHPV N protein, and that the expression was altered by viral infection. The association with HSC70 may help to mitigate the negative repercussions of misfolded proteins produced by viral polymerase's erroneous nature. More research on the role of these proteins in viral replication in infected cells is needed.