Disease relevance of A33R

• When extracts of cells that had been infected with vaccinia virus and labeled with H(3)(32)PO(4) were immunoprecipitated with antibodies against the A33R protein, two prominent bands were resolved [1].
• Incorporation of the vaccinia virus A36R protein into the outer membrane of intracellular enveloped virions (IEV) is dependent on expression of the A33R protein [2].
• By transfecting vaccinia virus DNA into cells infected with ectromelia virus and assaying for MAb reactivity, we mapped the glycoprotein to the A33R open reading frame [3].
• The A33R interaction site of the A36R protein is highly conserved among orthopoxviruses and may overlap binding sites for cellular proteins needed for microtubular movement and actin tail formation [2].
• To investigate whether a protective response could be generated by vaccination with these genes, we constructed and evaluated DNA vaccines expressing the VACV L1R and/or A33R genes under control of a cytomegalovirus promoter [4].

High impact information on A33R

• Collectively, these results demonstrated that the viral A36R protein interacts directly with the microtubule motor protein kinesin and that the viral protein A33R may regulate this interaction [5].
• The viral membrane glycoprotein genes of the isolates were sequenced; four had mutations causing C-terminal truncations of the A33R protein, and one had a serine replacing proline 189 of the B5R protein [6].
• In addition, tyrosine phosphorylation was specifically inhibited in cells infected with an A33R deletion mutant that still formed IEV [1].
• To determine the role of the protein, two inducible A33R mutants were constructed, one with the late promoter and one with the early and late A33R promoter elements [7].
• Using both an antibiotic resistance gene and a color marker, an A33R deletion mutant, vA33delta, was isolated, indicating that the A33R gene is not essential for VV replication [7].

Chemical compound and disease context of A33R

• Extracellular vaccinia virus envelope glycoprotein encoded by the A33R gene [3].

Biological context of A33R

• The amino acid sequence and hydrophilicity plot predicted that the A33R gene product is a type II membrane protein with two asparagine-linked glycosylation sites [3].
• In contrast, when mice were vaccinated with L1R and A33R loaded on different gold beads, neutralizing (presumably anti-L1R) and anti-A33R antibody responses were detected, and protection was markedly improved [4].
• Pathogenicity and immunogenicity in mice of vaccinia viruses mutated in the viral envelope proteins A33R and B5R [8].

Anatomical context of A33R

• In the absence of the A36R protein, however, the A33R protein still localized to IEV membranes [1].
• The envelope protein encoded by the A33R gene is required for formation of actin-containing microvilli and efficient cell-to-cell spread of vaccinia virus [7].

Associations of A33R with chemical compounds

• Triton X-114 partitioning experiments indicated that the A33R gene product is an integral membrane protein [3].

Other interactions of A33R

• After an intranasal challenge with the VACV IHD strain, three gene candidates B5R, A33R and A27L produced > or =66% survival [9].
• Three of these palmitylproteins are encoded by the A33R, B5R, and F13L open reading frames and migrate by gel electrophoresis with relative molecular masses of 23-28, 42, and 37 kDa, respectively [10].

Analytical, diagnostic and therapeutic context of A33R

• Electron microscopy revealed that the A33R gene product is expressed on the surface of extracellular enveloped virions but not on the intracellular mature form of virus [3].
• 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 [4].
• 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 [4].

References