Identification of conformational and cold-sensitive mutations in the MuLV Envelope protein

Lucille O’reilly, Monica J. Roth

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

The structure and function of the C-terminal domain of the murine leukemia virus Surface protein (MuLV SU) is not well defined. Passage of chimeric ecotropic-amphotropic MuLV viruses with junctions within the SU C-terminus results in the selection of specific point mutations which improve virus viability and Env function. Point mutations were characterized that alter the conformation of the SU/TM heterodimers on the viral particles. Mutation of position E311 within the Moloney MuLV SU protein alters the conformation of the TM protein and its recognition by antibody 42-114 in immunoprecipitation reactions. Mutation of either G541R in the amphotropic 4070A TM, V421M in the 4070A SU, or deletion of S39 and P40 at the N-terminus of the M-MuLV SU results in an irreversible cold-sensitive phenotype at 4°C. This loss of viral titer can be restored by incorporating V421M plus G541R or del S39 P40 plus G541R in cis within the SU/TM.

Original languageEnglish (US)
Pages (from-to)337-349
Number of pages13
JournalVirology
Volume312
Issue number2
DOIs
StatePublished - Aug 1 2003

All Science Journal Classification (ASJC) codes

  • Virology

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