|
|
||||||||
1 Department of Virology, Wellcome Biotechnology Limited, Langley Court, Beckenham, Kent BR3 3BS
and2 Coopers Animal Health Limited, Ash Road, Pirbright, Woking, Surrey GU24 ONQ, U.K.
Translation of foot-and-mouth disease virus RNA for extended periods in rabbit reticulocyte lysates results in the appearance of a previously undescribed protein. A protein with similar properties can also be detected in BHK cells at late times after virus infection. Specific immunoprecipitation has shown that this protein (Lb') is closely related to the smaller of the two leader proteins, Lb, although it migrates with an apparently higher Mr in SDS-polyacrylamide gels. The conversion of Lb to Lb' can be mimicked by treatment with carboxypeptidase B. It is suggested that C-terminal trimming of Lb to produce Lb' results in an increase in negative charge and is responsible for its slower migration in SDS-PAGE.
Keywords: FMDV, leader protein, protein modification
Received 29 January 1988;
accepted 2 June 1988.
This article has been cited by other articles:
![]() |
W. Glaser, R. Cencic, and T. Skern Foot-and-Mouth Disease Virus Leader Proteinase. INVOLVEMENT OF C-TERMINAL RESIDUES IN SELF-PROCESSING AND CLEAVAGE OF eIF4GI J. Biol. Chem., September 14, 2001; 276(38): 35473 - 35481. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |