Source:http://linkedlifedata.com/resource/pubmed/id/10092472
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1999-4-13
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pubmed:abstractText |
We demonstrated that in Rhodnius prolixus haemocyte monolayers, both Trypanosoma cruzi and Trypanosoma rangeli are capable of inducing haemocyte/parasite clump formation. We also purified, by one-step affinity chromatography, a haemolymph galactoside-binding lectin from R. prolixus which we believe could play an important role in the development of T. rangeli in the haemocoel of the insect vector. This lectin markedly enhanced the activation of clump formation by T. rangeli in R. prolixus haemocyte monolayers, with an increase in clump size and haemocyte aggregation. The haemolymph lectin also significantly affected the motilitity and survival of T. rangeli culture short forms, but not the long forms, when they were incubated in vitro. This molecule is also one of the few described in insects with agglutination activity independent of calcium ions. The partial N-terminal amino acid sequence of this lectin demonstrated similarity to a bacterial xylulose kinase and in preliminary experiments the purified haemolymph lectin phosphorylated a tyrosine kinase substrate in a dose-dependent manner. The possible role of this haemolymph lectin in the life cycle of T. rangeli is discussed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-4894
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
289-96
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:10092472-Amino Acid Sequence,
pubmed-meshheading:10092472-Animals,
pubmed-meshheading:10092472-Cells, Cultured,
pubmed-meshheading:10092472-Dose-Response Relationship, Drug,
pubmed-meshheading:10092472-Glycoproteins,
pubmed-meshheading:10092472-Hemagglutination,
pubmed-meshheading:10092472-Hemocytes,
pubmed-meshheading:10092472-Hemolymph,
pubmed-meshheading:10092472-Insect Vectors,
pubmed-meshheading:10092472-Lectins,
pubmed-meshheading:10092472-Molecular Sequence Data,
pubmed-meshheading:10092472-Movement,
pubmed-meshheading:10092472-Phosphorylation,
pubmed-meshheading:10092472-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:10092472-Rhodnius,
pubmed-meshheading:10092472-Sequence Alignment,
pubmed-meshheading:10092472-Sequence Homology, Amino Acid,
pubmed-meshheading:10092472-Trypanosoma
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pubmed:year |
1999
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pubmed:articleTitle |
Studies on a haemolymph lectin isolated from Rhodnius prolixus and its interaction with Trypanosoma rangeli.
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pubmed:affiliation |
Department of General Biology, Universidade Federal Fluminense, Niteroi, RJ, CEP 24.001-970, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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