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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0033684,
umls-concept:C0041221,
umls-concept:C0079429,
umls-concept:C0680022,
umls-concept:C1101145,
umls-concept:C1171362,
umls-concept:C1515670,
umls-concept:C1517488,
umls-concept:C2258907,
umls-concept:C2700640
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pubmed:issue |
11
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pubmed:dateCreated |
1992-11-19
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pubmed:databankReference |
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pubmed:abstractText |
Trypomastigotes, the blood stage form of the human parasite Trypanosoma cruzi, contain an enzyme on their surface, trans-sialidase, which catalyses the transfer of sialic acid from host glycoconjugates to acceptors on its own cell surface. At least a subset of the sialic acid-bearing acceptor molecules are involved in parasite invasion of host cells, an essential step in the life cycle of the parasite. Another trypomastigote surface enzyme that affects host cell invasion is neuraminidase and recent evidence suggests that both trans-sialidase and neuraminidase activities may be expressed by the same proteins on the parasite surface. We describe here the isolation and expression of several members of a trans-sialidase--neuraminidase gene family from T.cruzi. One of the isolated genes does indeed encode a protein with both trans-sialidase and neuraminidase activities, while other members of the gene family encode closely related proteins that express neither enzymatic activity. Chimeric protein constructs combining different portions of active and inactive genes identified a region of the gene necessary for enzymatic activity. Sequence analysis of this portion of the gene revealed a limited number of amino acid differences between the predicted active and inactive gene products.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1311053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1374711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1695668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1711561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1712251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1732417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1762630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1833644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1840626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-1993466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-2034687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-2111345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-2270104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-2562507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-2684649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-2684692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-2693963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-2825196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-3121750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-3306372,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-3315736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-6338592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-6352717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-6354906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1396577-6825172
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3837-44
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1396577-Amino Acid Sequence,
pubmed-meshheading:1396577-Animals,
pubmed-meshheading:1396577-Base Sequence,
pubmed-meshheading:1396577-Cloning, Molecular,
pubmed-meshheading:1396577-DNA, Protozoan,
pubmed-meshheading:1396577-Escherichia coli,
pubmed-meshheading:1396577-Gene Library,
pubmed-meshheading:1396577-Humans,
pubmed-meshheading:1396577-Molecular Sequence Data,
pubmed-meshheading:1396577-Multigene Family,
pubmed-meshheading:1396577-Neuraminidase,
pubmed-meshheading:1396577-Oligonucleotide Probes,
pubmed-meshheading:1396577-Recombinant Proteins,
pubmed-meshheading:1396577-Sequence Homology, Amino Acid,
pubmed-meshheading:1396577-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1396577-Trypanosoma cruzi
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pubmed:year |
1992
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pubmed:articleTitle |
Only some members of a gene family in Trypanosoma cruzi encode proteins that express both trans-sialidase and neuraminidase activities.
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pubmed:affiliation |
Institute of Tropical Medicine, Nagasaki University, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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