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Distribution and substrate specificity of intracellular proteolytic processing enzyme(s) for paramyxovirus fusion glycoproteins

¹ Department of Bacteriology, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734
and² Institute for Disease Mechanism and Control, Nagoya University School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466, Japan

Intracellular proteolytic processing of fusion glycoprotein precursors (F₀) of paramyxoviruses, i.e. a virulent strain of Newcastle disease virus (NDV), parainfluenza virus type 3 (PIV3) and simian virus 5 (SV5), was examined in NALM6 and BSC40 cells and compared with that in LLCMK₂ cells to investigate the distribution of the virus-activating protease(s) among the cells and its substrate specificity. BSC40 cells lack a processing endoprotease of the neuropeptide precursor, pro-opiomelanocortin (POMC), which possesses multiple cleavage sites at pairs of basic residues, Lys-Arg and Arg-Arg, a motif similar to that found in the cleavage site of the F₀ proteins. In NALM6 cells, only small amounts of the F₀ protein of virulent NDV was cleaved whereas those of PIV3 and SV5 were efficiently cleaved. In BSC40 cells the F₀ proteins of these three viruses were cleaved normally as well as in LLCMK₂ cells. The processing inhibitors monensin, chloroquine and A23187 [GenBank] suppressed the F₀ cleavage in the three cell types. These results indicate that both NALM6 and BSC40 cells possess virus-activating proteases similar to that of LLCMK₂ cells, but suggest that the enzyme of NALM6 may be slightly different in its substrate specificity from those of BSC40 and LLCMK₂. The results also suggest that the virus-activating proteases are different in their distribution and substrate specificity from the processing enzyme of POMC.

Received 24 September 1991; accepted 26 November 1991.

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