Disease relevance of L1R

• In particular, the myristylated fusion protein containing the first 12 amino acids of the L1R protein abutted to the chloramphenicol acetyltransferase protein was found associated with the envelope of intracellular vaccinia virus particles [1].
• In the absence of L1R expression, only immature virions could be detected by electron microscopy [2].
• By using synthetic oligonucleotides in concert with polymerase chain reaction techniques, a chimeric gene consisting of open reading fram L1R fused to a bacteriophage T7 promoter was constructed and cloned into a plasmid vector [3].

High impact information on L1R

• The results obtained in vitro and in vivo were similar and suggested that although the NH2-terminal 5 amino acids of the L1R protein were the minimum signal required to observe modification by myristate, 12 amino acids were required to obtain wild type levels of myristylation with a modulating role played by the intervening amino acid residues [1].
• Repression of E10R prevented the formation of intramolecular disulfide bonds of the G4L glutaredoxin, the L1R membrane protein, and the structurally related F9L protein [4].
• Transient expression of a plasmid containing the full-length L1R gene driven by its own promoter was able to complement and rescue the defective phenotype [2].
• These data demonstrate that VV open reading frame L1R encodes a myristylated protein and provide evidence that the site of modification of protein L1 is the amino-terminal glycine residue [3].
• This hypothesis was supported by cell-free translation of mutant L1R transcripts in which the penultimate glycine codon had been altered by site-directed mutagenesis to encode either an aspartic acid (pL1D1) or alanine (pL1A1) residue [3].

Biological context of L1R

• In addition, we discovered that the previously described neutralizing monoclonal antibody 2D5 (Y. Ichihashi, T. Takahashi, and M. Oie, 1994, Virology 202, 834-843) also recognizes the L1R protein [5].

Other interactions of L1R

• The L1R-specific MAbs, which bind the intracellular mature virion (IMV), neutralized virus in cell culture, whereas the A33R-specific MAbs, which bind extracellular enveloped virions (EEV), did not [6].
• Four of these proteins were mapped to the E7R, L1R, AI6L and G9R open-reading frames, respectively, because of the predicted presence of the N-myristyltransferase recognition sequence (M-G-X-X-X-S/T/A) at their amino termini [7].

Analytical, diagnostic and therapeutic context of L1R

• Our results indicated that vaccination with both L1R and A33R proteins, intended to evoke mechanistically distinct and complementary forms of protection, was more effective than vaccination with either protein by itself [6].

References