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Proteolytic cleavage of influenza virus matrix protein and nucleoprotein in an in vitro system

, : Proteolytic cleavage of influenza virus matrix protein and nucleoprotein in an in vitro system. Voprosy Virusologii 28(5): 549-556

Proteolytic modification of NP-protein which is a part of influenza virus ribonucleoprotein (RNP) was studied in vitro. NP-protein of influenza virus (mol. weight 56 000) was shown upon RNP treatment with bromeline to undergo proteolytic cleavage revealing 2 more polypeptides with molecular weights of 53 000 and 45 000 daltons. The same classes of NP-proteins were present in RNPs recovered from subviral units obtained by virus treatment with bromeline at buffer pH below 7. Electrophoresis in 12% polyacrylamide gel under reducing conditions of subvirus units obtained by treatment of virions with bromeline at the buffer pH below 7 also demonstrated proteolytic cleavage of M-protein present in them into fragments with molecular weights of 8 500-12 000 daltons. Similar results were obtained upon direct treatment with bromeline of M-protein isolated from virions.


PMID: 6362200

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