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  • Agglutination  (1)
  • Blood Proteins/immunology/pharmacology/*physiology  (1)
  • Hemolymph/parasitology  (1)
  • 1
    Publication Date: 1981-02-06
    Description: Lectins of different activities were found in the crop, midgut, and hemolymph of the insect Rhodnius prolixus. These were not specific for N-acetyl-D-mannosamine, alpha-N-acetyl-D-galactosamine, and alpha- and beta-galactose, respectively. Lectin receptors were detectable in epimastigote but not in trypomastigote forms of Trypanosoma cruzi, a protozoan parasite of the insect and of humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pereira, M E -- Andrade, A F -- Ribeiro, J M -- New York, N.Y. -- Science. 1981 Feb 6;211(4482):597-600.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7006082" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Hemagglutinins ; Hemolymph/parasitology ; Insect Vectors/*parasitology ; *Lectins ; Rhodnius/anatomy & histology/*parasitology ; Triatominae/*parasitology ; Trypanosoma cruzi/growth & development/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1986-04-04
    Description: A lectin in Giardia lamblia was activated by secretions from the human duodenum, the environment where the parasite lives. Incubation of the secretions with trypsin inhibitors prevented the appearance of lectin activity, implicating proteases as the activating agent. Accordingly, lectin activation was also produced by crystalline trypsin and Pronase; other proteases tested were ineffective. When activated, the lectin agglutinated intestinal cells to which the parasite adheres in vivo. The lectin was most specific to mannose-6-phosphate and apparently was bound to the plasma membrane. Activation of a parasite lectin by a host protease represents a novel mechanism of host-parasite interaction and may contribute to the affinity of Giardia lamblia to the infection site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lev, B -- Ward, H -- Keusch, G T -- Pereira, M E -- P-1-P30-AM 39428-01/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):71-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3513312" target="_blank"〉PubMed〈/a〉
    Keywords: Agglutination ; Animals ; Duodenum/enzymology/parasitology ; Giardia/*metabolism ; *Host-Parasite Interactions ; Humans ; Intestine, Small/enzymology/*parasitology ; Lectins/*metabolism ; Mice ; Peptide Hydrolases/*metabolism ; Sheep ; Species Specificity ; Trypsin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1987-12-04
    Description: A specific inhibitor of the neuraminidase of the protozoan parasite Trypanosoma cruzi was isolated recently and named cruzin. It is now shown that cruzin is similar to high-density lipoprotein by amino acid homology, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, by immunoblot analysis, and by isoelectric focusing. Cruzin purified by ion exchange chromatography and high-density lipoprotein isolated by density gradient ultracentrifugation inhibited Trypanosoma cruzi neuraminidase to the same extent. Cruzin or high-density lipoprotein restores to normal the decreased multiplication rate of Trypanosoma cruzi epimastigotes grown in a medium depleted of lipoproteins, suggesting that it may be important for survival of the parasite in nature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prioli, R P -- Ordovas, J M -- Rosenberg, I -- Schaefer, E J -- Pereira, M E -- AI 07380/AI/NIAID NIH HHS/ -- AI 18102/AI/NIAID NIH HHS/ -- HL 35243/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1417-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Geographic Medicine and Infectious Diseases, New England Medical Center Hospitals, Inc., Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3120314" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Anti-Infective Agents ; Apolipoprotein A-I ; Apolipoproteins A/genetics/immunology ; Blood Proteins/immunology/pharmacology/*physiology ; Isoelectric Focusing ; Lipoproteins, HDL/*physiology ; Neuraminidase/antagonists & inhibitors ; Trypanosoma cruzi/*enzymology/growth & development
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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