Disease relevance of Parva

• Role of the integrin-linked kinase/PINCH1/alpha-parvin complex in cardiac myocyte hypertrophy [1].
• Comparative growth of bovine lymphosarcoma cells and lymphoid cells infected with Theileria parva in athymic (nude) mice [2].
• Since antibody to this antigen(s) neutralizes T. parva sporozoites from different stocks, the results could be of relevance to the development of a broad spectrum vaccine against the cattle disease East Coast fever, which is caused by T. parva [3].
• A stage-specific surface antigen of Theileria parva, p67, is the basis for the development of an anti-sporozoite vaccine for the control of East Coast fever (ECF) in cattle [4].
• Production in ascites fluid of biosynthetically labelled monoclonal antibody to Theileria parva sporozoites [5].

High impact information on Parva

• ILK, PINCH and parvin: the tIPP of integrin signalling [6].
• Phosphorylation of actopaxin regulates cell spreading and migration [7].
• Expression of the nonphosphorylatable actopaxin mutant significantly reduced cell migration, whereas expression of the phosphomimetic increased cell migration in scrape wound and Boyden chamber migration assays [7].
• Endogenous and WT actopaxin, but not the nonphosphorylatable mutant, were phosphorylated in vivo during cell adhesion/spreading [7].
• A mouse monoclonal antibody (mAbD1) that neutralizes sporozoites of different stocks of the protozoan parasite Theileria parva has been used to localize and identify a sporozoite antigen [3].

Chemical compound and disease context of Parva

• Recently, we reported the expression and production of different parts of p67 as fusions to either GFP or to the baculovirus GP64 envelope glycoprotein in insect cells, which resulted in stable proteins recognized by a monoclonal specific for native p67 [8].
• Ehrlich ascites tumour (EAT) cells were fused with Theileria parva-infected bovine lymphoid (C2) cells using inactivated Sendai virus [9].

Biological context of Parva

• Furthermore, a marked increase of apoptosis in the podocytes in which the assembly of the PINCH-1-ILK-alpha-parvin complex was compromised was detected [10].
• Genome analysis of Theileria parva [11].
• Linear peptide specificity of bovine antibody responses to p67 of Theileria parva and sequence diversity of sporozoite-neutralizing epitopes: implications for a vaccine [4].
• Peromyscus leucopus (white-footed mouse) and Cryptotis parva (least shrew) possess desirable attributes for biomonitoring contamination of terrestrial ecosystems, but few studies have examined the potential use of these species for monitoring exposure to genotoxic contaminants [12].
• Attempts to produce Theileria parva-infected mouse cells using cell fusion techniques [9].

Anatomical context of Parva

• Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans [13].
• The ternary complex of integrin-linked kinase (ILK), PINCH and parvin functions as a signalling platform for integrins by interfacing with the actin cytoskeleton and many diverse signalling pathways [6].
• Finally, it is shown that alpha-parvin is phosphorylated in podocytes [10].
• De novo expression of T cell markers on Theileria parva-transformed lymphoblasts in cattle [14].
• The results indicated that micronucleated erythrocytes were removed from the circulating blood in P. leucopus, but not in C. parva [12].

Associations of Parva with chemical compounds

• Mutations at the alpha-parvin N-terminal proline-directed serine phosphorylation sites reduced its complex formation with ILK and resulted in defects in podocyte adhesion, architecture, and survival [10].
• P. leucopus and C. parva were more sensitive than M. musculus to MMS [12].
• Only valinomycin and, more particularly, gramicidin D were significantly active against B. rodhaini and T. parva [15].
• When cells were grown in hypoxanthine/aminopterin/thymidine medium (HAT), T parva appeared to be selectively killed by the aminopterin present; this finding would seem to militate against the use of a HAT selection system to clone parasitised hybrids [9].

Other interactions of Parva

• Disruption of the PINCH-1-ILK-alpha-parvin complex significantly reduced the podocyte-matrix adhesion and foot process formation [10].
• This suggests a parasite-mediated event, involving the recruitment and activation of the host IkappaB kinase (IKK) complex, as has been observed with the related protozoan Theileria parva [16].

Analytical, diagnostic and therapeutic context of Parva

• The labelled antibody was used to detect, by autoradiography, a surface coat antigen of T. parva sporozoites in cryostat sections of Theileria-infected tick salivary glands [5].
• The MoAbs did not react, in indirect immunofluorescence or enzyme-linked immunosorbent assays (ELISA), with the common haemoparasites of cattle, namely, T. parva, T. annulata, Babesia bigemina, B. bovis, Anaplasma marginale, Trypanosoma congolense, T. vivax or T. brucei [17].
• Sera from Theileria parva infected, recovered and rechallenged cattle were tested in complement-dependent cytotoxicity, membrane immunofluorescence and antibody-dependent cellular cytotoxicity assays for the presence of antibodies against cell membrane antigens of T. parva transformed cell lines [18].

References