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Biomedical subjects

G Einhorn

Publications and source records attributed to G Einhorn.

5 recordsLinked to original sources
PubMed2002

The potential of pathogens as biological control of parthenium weed (Parthenium hysterophorus L.) in Ethiopia.

P. hsyterophorus is an exotic invasive annual weed now causing severe infestation in Ethiopia. Studies on diagnosis, incidence and distribution of pathogens associated with parthenium weed in Ethiopia were carried out from 1998-2002. Several fungal isolates were obtained from seed and other parts of parthenium plants. Among them were putative pathogenic fungal species of the genus Helminthosporium, Phoma, Curvularia, Chaetomium, Alternaria, and Fusarium. However, pathogenecity test of the isolates obtained showed no or non-specific symptoms. It was concluded that these pathogens could be opportunistic with insignificant potential for biological control of parthenium. Two most important diseases associated with parthenium were a rust disease, caused by Puccinia abrupta var. partheniicola, and a phyllody disease, caused by a phytoplasma of fababean phyllody (PBP) phytoplasma group. The rust was commonly found in cool mid altitude (1500-2500 m) areas while phyllody was observed in low to mid altitude regions (900-2500 m) of Ethiopia, with a disease incidence up to 100% and 75%, respectively, in some locations. Study of the individual effects of the rust and phyllody diseases under field conditions showed a reduction on weed morphological parameters (plant height, leaf area, and dry matter yield). Parthenium seed production was reduced by 42% and 85% due to rust and phyllody, respectively. Phyllody and rust diseases of parthenium showed significant potential for classical biological control of parthenium after further confirmation of insect vectors that transmit phyllody and host range of phyllody disease to the related economic plants in Ethiopia.

Alternaria↗
PubMed1989

Molecular basis of Qa-11 antigen and paradoxical Qa-gene expression in an H-2 recombinant.

The Qa-11 Ag expressed in certain strains with the B2-microglobulin-b allele, apparently maps into the Tla region as well as into the Qa-2 region. Moreover Qa-11 has been shown to be biochemically indistinguishable from Qa-2. Genetic complementation studies combining the right Qa and Tla regions failed to lead to Qa-11 expression. To elucidate the molecular basis of this apparent paradox, we examined the expression of Qa-11 on products of transfected Q-region class I genes. Immunochemical analysis has shown that the Qa-11 Ag is expressed on class I molecules encoded by the Q7 gene from both C57BL/10 (Q7b) and BALB/c (Q7d), but not on the protein product of the Q9 gene isolated from the C57BL/10 strain (Q9b). Inasmuch as the predicted protein products of the Q7b and Q9b genes would differ at a single amino acid, a residue critical for Qa-11 expression has been identified. Based on these results it is proposed that among the beta-2-mb strains, the Qa-11+/Qa-2+ mice are likely to express at least the Q7 gene, whereas Qa-11-/Qa-2+ mice express only Q9. In support of this model, the Qa-2+/Q-11- recombinant B6.K2, essential for the apparent mapping of Qa-11 into the Tla region, expresses only Q9 but not Q7 encoded molecules on the cell surface, and only Q9 and no processed Q7 mRNA is detected in the cytoplasm. This expression pattern in B6.K2 cannot be explained on the basis of a single crossing-over event.

Animals↗
PubMed1988

Further characterization of the membrane anchor found on the tissue-specific class I molecule Qa2.

Previous studies have determined that various Qa2 serologic determinants can be removed from the surface of spleen cells by treatment with a phospholipase C. Our studies have determined that the class I molecule Qa2, expressed on the surface of spleen cells and activated T cells, behaves as an integral membrane protein based on its ability to associate with detergent micelles. Studies utilizing two purified phospholipase C have revealed that although most (90 to 95%) of the Qa2 molecules expressed on the surface of resting spleen cells are released as intact 40-kDa polypeptides associated with beta 2-microglobulin, activated T cells contain a major cell subpopulation expressing lipase-resistant Qa2 molecules. Flow cytometric analysis revealed that L3T4+-activated T cells expressed lipase-sensitive Qa2 molecules, whereas Lyt-2+ cells express lipase-resistant forms of the Qa2 molecule. The relationship between the secreted form of the Qa2 molecule and the lipase-generated soluble Qa2 molecule was investigated. Based on SDS-PAGE analysis, the secreted Qa2 molecules has a Mr of 39 kDa whereas the cell surface form released from either resting spleen or activated T cells by phosphatidylinositol-specific phospholipase C has a Mr of approximately equal to 40 kDa. Furthermore, the secreted Qa2 molecule lacks an epitope, cross-reacting determinant, often present on lipase-solubilized cell surface molecules. Thus, based on serologic and biochemical criteria, the soluble Qa2 molecules generated by an exogenous phospholipase C and the secreted Qa2 molecule are structurally distinct.

Animals↗
PubMed1986

Qa gene expression: biosynthesis and secretion of Qa-2 molecules in activated T cells.

The biosynthesis and expression of the tissue-specific class I molecule Qa-2 have been studied in resting and activated T-cell populations. Polyclonal activation of T lymphocytes induces a 3- to 4-fold increase in the biosynthesis of Qa-2 molecules but no increase in cell-surface levels. Analysis of the biosynthetic pathway of the Qa-2 molecule in activated lymphocytes reveals that approximately equal to 70% of the newly synthesized Qa-2 molecules are secreted as soluble molecules. In resting-cell populations, Qa-2 remains entirely cell-associated. This process is unique to the Qa-2 molecule, since other class I molecules (e.g., H-2Kb and H-2Db) synthesized by activated cells remain cell-associated. The possibility that the secreted Qa-2 molecule is the product of a new Qa gene or an alternatively spliced mRNA is considered. These results indicate that the Qa-2 molecules may not just function as a cell-surface recognition structure but also may serve a role as a soluble factor synthesized by activated lymphoid cell populations.

Animals↗