ROLE OF CONSERVED CYSTEINE RESIDUES IN THE CAIC MOTIF OF THE SU GLYCOPROTEIN IN THE MATURATION AND FUSION ACTIVITY OF BOVINE LEUKAEMIA VIRUS

Authors    Serroni A, Forti K, De Giuseppe A

Abstract   The surface (SU) and transmembrane (TM) glycoproteins of many retroviruses are linked by disulphide bonds, and the interaction of SU with a cellular receptor results in disulphide bond isomerisation triggered by the CXXC motif in SU. This reaction leads to the fusion of viral and host cell membranes. In this work, we show that the cysteine at amino acid position 212 in the CAIC motif of the SU glycoprotein of bovine leukaemia virus has a free thiol group. A C-to-A mutation at position 212, either individually or in combination with a C-to-A mutation at position 215, was found to inhibit the maturation process, suggesting its involvement in the formation of the covalent bond with TM.

Publish Date  2019

Volume   164 (9)

ISSN    1432-8798

DOI   doi.org/10.1007/s00705-019-04294-x

URL    https://link.springer.com/article/10.1007/s00705-019-04294-x

Journal    Archives of Virology

Pages  2309-2314

PMID  31172288