Although vascular anomalies present a surgical challenge, we have shown the feasibility of performing hand-assisted retroperitoneoscopic live donor nephrectomy in a donor with a double vena cava and short renal vein. With comprehensive preoperative assessment, laparoscopic live donor nephrectomy can be done safely in donors with anatomical anomalies. This may increase the number of living donor kidney transplants as it offers lower postoperative morbidity and economic disincentives for potential donors.

Western blots of proteins of 14 Mycoplasma iowae strains and isolates resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis were probed with three monoclonal antibodies (MAbs), MI6, MI7, and MI8. MAb MI6 reacted with one or more antigens with apparent molecular weights of 60,000, 70,000, and 94,000. In three strains (N-PHN-D13, R-D2497, and K 1805), antigens located on a single peptide band were recognized, while in others additional epitopes at different molecular-weight positions were revealed. A similar pattern was observed with MAb MI7, although it reacted with fewer antigens than did MAb MI6 and failed to recognize antigens in strains N-PHN-D13 and R-D2497. MAb MI8 reacted with an antigen at an apparent molecular-weight position of 28,000 in four of the 14 strains and isolates. The diverse reaction patterns observed with the MAbs in the 14 M. iowae strains and isolates confirms the occurrence of antigenic variation within this species. Antigenic variation in M. iowae may be pivotal in determining host-parasite interactions, pathogenesis, and the outcome of disease.

Serological studies have shown that some antigenic determinants are conserved among several pathogenic Mycoplasma species, including Mycoplasma pneumoniae, M. genitalium, and M. gallisepticum. M. synoviae, an avian pathogen that shares certain morphological and biological features with the above-mentioned mycoplasmas, was examined by the protein immunoblot procedure for its reactivity with hyperimmune rabbit antiserum specific for the major (190,000 molecular-weight [MW]) adhesion P1 protein of M. pneumoniae. A single polypeptide of M. synoviae of approximately 55,000 MW was recognized by the anti-P1 antiserum. The 55,000-MW antigen was electroeluted following electrophoretic separation of M. synoviae polypeptides, and the eluted protein was used for immunization of mice for the production of monoclonal antibodies (MAbs) and polyclonal antiserum. Immunoelectron microscopy with MAbs and gold-conjugated secondary antibodies showed that the 55,000-MW antigen was located at the cell surface and was more densely clustered around the bleb-like protuberance of the cell. Immuno-affinity-purified 55,000-MW antigen, as well as the antibodies produced against it, blocked the hemagglutination by M. synoviae.

An agglutinating monoclonal antibody (MAb S2) specific for a 55,000-molecular-weight surface protein of Mycoplasma synoviae was developed by fusion of spleen cells from immunized BALB/c mice with P3X63 Ag8.653 myeloma cells. Immunogold labeling experiments confirmed the cell surface location of the MAb-recognized antigen. MAb S2-coated Staphylococcus aureus was used in a rapid slide coagglutination assay. Eleven M. synoviae strains, including the type strain WVU 1853, coagglutinated with MAb-coated S. aureus, but five M. gallisepticum strains (PG31, S6, R, F, and A5969) did not.