Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein

Figure 3

The C-terminal of the M alone can compensate for the ability of the C-terminal truncation mutant to encapsulate N into the VLP. (a) N-Myc, HA-M, MΔC120, MΔC170, MΔC190, and MΔC210 plasmids were transfected alone or cotransfected into 293T cells. After transfection, anti-HA was used for immunoprecipitation. The protein level was detected by WB. Asterisks indicate specific proteins detected. (b) The ability of M or mutant to interact with N. The data is from the average of the results of three independent experiments. . (c) N-Myc plasmid was cotransfected with HA-M, MΔC120, or MΔC170 plasmids, respectively, into 293T cells, and after transfection, anti-anti-Myc was used for coimmunoprecipitation. The protein level was detected by WB. (d) Relative ability to interact with N in the same group as M+N and MΔC120/MΔC170+N. The data is derived from the average of the results from three independent experiments. and . (e) N-Myc, HA-M, HA-MC190, HA-MΔC120, or HA-MΔC170 plasmids were cotransfected into 293T cells. After transfection, cells and VLPs were collected and protein expression was detected by WB. Asterisks indicate specific proteins detected. (f) Relative germination index of M and mutant integrating N into VLP. The data are from the average of three independent experiments. ns: not significant ().

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