Disease relevance of L1R

• Comparison of the variola virus (VAR) and vaccinia virus strain Copenhagen (COP) sequences show that the main differences are between proteins L1R and I5R [1].
• When cells were infected with a mutant vaccinia virus in which the E10R gene encoding an ERV1/ALR family protein was repressed, the disulfide bonds of three other viral proteins-namely, the L1R and F9L proteins and the G4L glutaredoxin-were completely reduced [2].
• Previously we have shown that while the L1R protein is a constituent of both intracellular mature virus particles and extracellular enveloped virions which are released from the infected cell, it is associated exclusively with the primary membranes surrounding the virion core [3].

High impact information on L1R

• Furthermore, subcellular fractionation of infected cells expressing the fusion proteins indicated that the NH2 terminus of the L1R protein was capable of targeting the fusion proteins to membrane-containing fractions only if myristylated [4].
• To this end, a family of chimeric reporter genes containing 0-13 codons from the NH2 terminus of the L1R open reading frame fused in-frame to the bacterial chloramphenicol acetyltransferase gene was constructed [4].
• The 25-kDa protein has previously been identified as that encoded by the L1R open reading frame, leaving the identities of the remaining proteins to be determined [5].
• Dissection of the L fragment and subsequent transfection revealed that the L1R gene induced the 2D5mAb-resistant virus [6].

Chemical compound and disease context of L1R

• Within vaccinia virus-infected cells, the product of the L1R open reading frame is covalently modified by myristic acid at the penultimate NH2-terminal glycine residue [3].

Analytical, diagnostic and therapeutic context of L1R

• Although the N-terminus of the immunoaffinity-purified protein was blocked, sequence analysis of trypic peptides revealed that the MAb 7D11 antigen was identical to the myristylated protein encoded by the L1R open reading frame previously described by C.A. Franke, E.M. Wilson, and D.E. Hruby (1990, J. Virol. 64, 5988-5996) [7].
• The location of the VV L1R protein was determined by using a monospecific anti-L1R serum to detect the L1R protein by immunoblot in INV- and EEV-containing fractions, by examining the proteinase K sensitivity of the L1R protein in intact INV and EEV particles, and by immunoelectron microscopy [8].

References