Characterization of U-Mo Foils for AFIP-7

Twelve AFIP in-process foil samples, fabricated by either Y-12 or LANL, were shipped from LANL to PNNL for potential characterization using optical and scanning electron microscopy techniques. Of these twelve, nine different conditions were examined to one degree or another using both techniques. For this report a complete description of the results are provided for one archive foil from each source of material, and one unirradiated piece of a foil of each source that was irradiated in the Advanced Test Reactor. Additional data from two other LANL conditions are summarized in very brief form in an appendix. The characterization revealed that all four characterized conditions contained a cold worked microstructure to different degrees. The Y-12 foils exhibited a higher degree of cold working compared to the LANL foils, as evidenced by the highly elongated and obscure U-Mo grain structure present in each foil. The longitudinal orientations for both of the Y-12 foils possesses a highly laminar appearance with such a distorted grain structure that it was very difficult to even offer a range of grain sizes. The U-Mo grain structure of the LANL foils, by comparison, consisted of a more easily discernible grain structure with a mix of equiaxed and elongated grains. Both materials have an inhomogenous grain structure in that all of the characterized foils possess abnormally coarse grains

Characterization of U-Mo Foils for AFIP-7

Twelve AFIP in-process foil samples, fabricated by either Y-12 or LANL, were shipped from LANL to PNNL for potential characterization using optical and scanning electron microscopy techniques. Of these twelve, nine different conditions were examined to one degree or another using both techniques. For this report a complete description of the results are provided for one archive foil from each source of material, and one unirradiated piece of a foil of each source that was irradiated in the Advanced Test Reactor. Additional data from two other LANL conditions are summarized in very brief form in an appendix. The characterization revealed that all four characterized conditions contained a cold worked microstructure to different degrees. The Y-12 foils exhibited a higher degree of cold working compared to the LANL foils, as evidenced by the highly elongated and obscure U-Mo grain structure present in each foil. The longitudinal orientations for both of the Y-12 foils possesses a highly laminar appearance with such a distorted grain structure that it was very difficult to even offer a range of grain sizes. The U-Mo grain structure of the LANL foils, by comparison, consisted of a more easily discernible grain structure with a mix of equiaxed and elongated grains. Both materials have an inhomogenous grain structure in that all of the characterized foils possess abnormally coarse grains

Antigenicity and Immunogenicity of RV144 Vaccine AIDSVAX Clade E Envelope Immunogen Is Enhanced by a gp120 N-Terminal Deletion

An immune correlates analysis of the RV144 HIV-1 vaccine trial revealed that antibody responses to the gp120 V1/V2 region correlated inversely with infection risk. The RV144 protein immunogens (A244-rp120 and MN-rgp120) were modified by an N-terminal 11-amino-acid deletion (Δ11) and addition of a herpes simplex virus (HSV) gD protein-derived tag (gD). We investigated the effects of these modifications on gp120 expression, antigenicity, and immunogenicity by comparing unmodified A244 gp120 with both Δ11 deletion and gD tag and with Δ11 only. Analysis of A244 gp120, with or without Δ11 or gD, demonstrated that the Δ11 deletion, without the addition of gD, was sufficient for enhanced antigenicity to gp120 C1 region, conformational V2, and V1/V2 gp120 conformational epitopes. RV144 vaccinee serum IgGs bound more avidly to A244 gp120 Δ11 than to the unmodified gp120, and their binding was blocked by C1, V2, and V1/V2 antibodies. Rhesus macaques immunized with the three different forms of A244 gp120 proteins gave similar levels of gp120 antibody titers, although higher antibody titers developed earlier in A244 Δ11 gp120-immunized animals. Conformational V1/V2 monoclonal antibodies (MAbs) gave significantly higher levels of blocking of plasma IgG from A244 Δ11 gp120-immunized animals than IgG from animals immunized with unmodified A244 gp120, thus indicating a qualitative difference in the V1/V2 antibodies induced by A244 Δ11 gp120. These results demonstrate that deletion of N-terminal residues in the RV144 A244 gp120 immunogen improves both envelope antigenicity and immunogenicity