Monoclonal Antibody #5-2-26 Recognizes the Phosphatase-Sensitive Epitope of Rabies Virus Nucleoprotein

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Abstract
We prepared monoclonal antibodies (MAbs) against the rabies virus N protein, among which one antibody (MAb 5‐2‐26) was shown to lack reactivity with the phosphatase‐treated N protein. The MAb was able to recognize the sodium dodecyl sulfate (SDS)‐denatured N protein. The MAb did not recognize the N‐protein analogues produced in Escherichia coli (E. coli), indicating that the N‐gene products were not normally processed in E. coli after translation. On the other hand, the MAb reacted normally with N‐gene products produced in COS‐7 cells, but not with those produced in the presence of K‐252a (a protein kinase inhibitor of a broad spectrum). The MAb displayed weak cross‐reactivity with the Triton‐insoluble network structures composed of several components, while another phosphoprotein (M1) of the virus was not recognized at all. These results suggest that MAb 5‐2‐26 preferentially recognizes a phosphatase‐sensitive linear epitope of N protein, which may enable further investigations to be conducted on the mechanism of N‐protein phosphorylation and its role(s) in virus replication.