Ribosome-inactivating proteins from plants inhibit ribosome activity of Trypanosoma and Leishmania. 1988

P Cenini, and A Bolognesi, and F Stirpe
Dipartimento di Patologia sperimentale, Università di Bologna, Italy.

Ribosomes from Trypanosoma brucei rhodesiense and from Leishmania infantum were isolated and optimal conditions for in vitro translation were established. The effect of ribosome-inactivating proteins extracted from several plants was then assessed in order to identify those suitable for the preparation of immunotoxins against these organisms. Ribosomes from both species were inactivated by some ribosome-inactivating proteins (dianthins, saporins, pokeweed antiviral proteins, and the ribosome-inactivating chain of abrin). The similarity of the effects on the ribosomes from the two species examined indicates that ribosome-inactivating proteins should also be effective in a similar way on ribosomes from other species of Trypanosoma and Leishmania.

UI MeSH Term Description Entries
D007893 Leishmania donovani A parasitic hemoflagellate of the subgenus Leishmania leishmania that infects man and animals and causes visceral leishmaniasis (LEISHMANIASIS, VISCERAL). The sandfly genera Phlebotomus and Lutzomyia are the vectors. Leishmania (Leishmania) donovani,Leishmania leishmania donovani,Leishmania donovanus,Leishmania leishmania donovanus,donovani, Leishmania leishmania,donovanus, Leishmania,donovanus, Leishmania leishmania,leishmania donovanus, Leishmania
D009699 N-Glycosyl Hydrolases A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars. Glycoside Hydrolases, Nitrogen-linked,Hydrolases, N-Glycosyl,Nucleosidase,Nucleosidases,Nucleoside Hydrolase,Nitrogen-linked Glycoside Hydrolases,Nucleoside Hydrolases,Glycoside Hydrolases, Nitrogen linked,Hydrolase, Nucleoside,Hydrolases, N Glycosyl,Hydrolases, Nitrogen-linked Glycoside,Hydrolases, Nucleoside,N Glycosyl Hydrolases,Nitrogen linked Glycoside Hydrolases
D010940 Plant Proteins Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. Plant Protein,Protein, Plant,Proteins, Plant
D000036 Abrin A toxic lectin from the seeds of jequirity, Abrus precatorius L. Very active poison. Five different proteins have so far been isolated: Abrus agglutinin, the component responsible for: hemagglutinating activity, & abrins a-d, the toxic principals each consisting of two peptide chains are held together by disulfide bonds. Abrin A,Abrin C
D000076985 Saporins Type 1 ribosome-inactivating proteins derived from SAPONARIA OFFICINALIS that function through endohydrolysis of the N-glycosidic bond at single ADENOSINE residues of 28S RIBOSOMAL RNA. They are used as IMMUNOTOXINS. RIP Ribosome-Inactivating Protein,Ribosome-Inactivating Protein,SAP5 Protein,SAP6 Protein,Saporin,Saporin 5 Protein,Saporin 6 Protein,Saporin Protein,Saporin-S9 Protein,Protein, RIP Ribosome-Inactivating,RIP Ribosome Inactivating Protein,Ribosome Inactivating Protein,Ribosome-Inactivating Protein, RIP,Saporin S9 Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000922 Immunotoxins Semisynthetic conjugates of various toxic molecules, including RADIOACTIVE ISOTOPES and bacterial or plant toxins, with specific immune substances such as IMMUNOGLOBULINS; MONOCLONAL ANTIBODIES; and ANTIGENS. The antitumor or antiviral immune substance carries the toxin to the tumor or infected cell where the toxin exerts its poisonous effect. Affinotoxin,Antibody-Toxin Conjugate,Antibody-Toxin Conjugates,Antibody-Toxin Hybrid,Antibody-Toxin Hybrids,Chimeric Toxins,Cytotoxin-Antibody Conjugate,Cytotoxin-Antibody Conjugates,Monoclonal Antibody-Toxin Conjugate,Targeted Toxin,Targeted Toxins,Toxin Carriers,Toxin Conjugates,Toxin-Antibody Conjugate,Toxin-Antibody Conjugates,Toxin-Antibody Hybrid,Toxin-Antibody Hybrids,Toxins, Chimeric,Toxins, Targeted,Affinotoxins,Chimeric Toxin,Immunotoxin,Monoclonal Antibody-Toxin Conjugates,Toxin Carrier,Toxin Conjugate,Antibody Toxin Conjugate,Antibody Toxin Conjugates,Antibody Toxin Hybrid,Antibody Toxin Hybrids,Antibody-Toxin Conjugate, Monoclonal,Antibody-Toxin Conjugates, Monoclonal,Carrier, Toxin,Carriers, Toxin,Conjugate, Antibody-Toxin,Conjugate, Cytotoxin-Antibody,Conjugate, Monoclonal Antibody-Toxin,Conjugate, Toxin,Conjugate, Toxin-Antibody,Conjugates, Antibody-Toxin,Conjugates, Cytotoxin-Antibody,Conjugates, Monoclonal Antibody-Toxin,Conjugates, Toxin,Conjugates, Toxin-Antibody,Cytotoxin Antibody Conjugate,Cytotoxin Antibody Conjugates,Hybrid, Antibody-Toxin,Hybrid, Toxin-Antibody,Hybrids, Antibody-Toxin,Hybrids, Toxin-Antibody,Monoclonal Antibody Toxin Conjugate,Monoclonal Antibody Toxin Conjugates,Toxin Antibody Conjugate,Toxin Antibody Conjugates,Toxin Antibody Hybrid,Toxin Antibody Hybrids,Toxin, Chimeric,Toxin, Targeted
D000972 Antineoplastic Agents, Phytogenic Agents obtained from higher plants that have demonstrable cytostatic or antineoplastic activity. Antineoplastics, Botanical,Antineoplastics, Phytogenic,Agents, Phytogenic Antineoplastic,Botanical Antineoplastics,Phytogenic Antineoplastic Agents,Phytogenic Antineoplastics
D000998 Antiviral Agents Agents used in the prophylaxis or therapy of VIRUS DISEASES. Some of the ways they may act include preventing viral replication by inhibiting viral DNA polymerase; binding to specific cell-surface receptors and inhibiting viral penetration or uncoating; inhibiting viral protein synthesis; or blocking late stages of virus assembly. Antiviral,Antiviral Agent,Antiviral Drug,Antivirals,Antiviral Drugs,Agent, Antiviral,Agents, Antiviral,Drug, Antiviral,Drugs, Antiviral
D012270 Ribosomes Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION. Ribosome

Related Publications

P Cenini, and A Bolognesi, and F Stirpe
December 1993, Biochimica et biophysica acta,
P Cenini, and A Bolognesi, and F Stirpe
February 1991, Seminars in cell biology,
P Cenini, and A Bolognesi, and F Stirpe
December 2011, Virologica Sinica,
P Cenini, and A Bolognesi, and F Stirpe
November 2016, Molecules (Basel, Switzerland),
P Cenini, and A Bolognesi, and F Stirpe
April 1992, Bio/technology (Nature Publishing Company),
P Cenini, and A Bolognesi, and F Stirpe
January 2006, Molekuliarnaia biologiia,
P Cenini, and A Bolognesi, and F Stirpe
February 1988, Nucleic acids research,
P Cenini, and A Bolognesi, and F Stirpe
July 2001, FASEB journal : official publication of the Federation of American Societies for Experimental Biology,
P Cenini, and A Bolognesi, and F Stirpe
January 1991, Biochimie,
Copied contents to your clipboard!