
Effect of Undiluted Passage on the Polypeptides of Measles Virus
Author(s) -
Bertus K. Rima,
Samuel Martin
Publication year - 1979
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/0022-1317-44-1-135
Subject(s) - measles virus , infectivity , virus , mole , biology , measles , virology , viral matrix protein , paramyxoviridae , microbiology and biotechnology , biochemistry , viral disease , vaccination
Measles virus induces a large polypeptide (L; mol. wt. 180 K), a large glycopolypeptide (H; mol. wt. 80 K), a nucleocapsid associated polypeptide (P; mol. wt. 70 K), a nucleocapsid polypeptide (N; mol. wt. 60 K), a second glycopolypeptide (F0; mol. wt. 60 K), a matrix or membrane polypeptide (M; mol. wt. 37 K) and a small polypeptide (S; mol. wt. 15 K). The second glycopolypeptide (F0) appears to be cleaved in purified measles virus. Defective interfering particles accumulate during passage of measles virus leading to a decrease in the amounts of virus-specific protein synthesized in infected cells. Even in the best preparations of purified measles virus, host proteins are always detected and these become more predominant in preparations with low infectivity.