rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1991-5-8
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M37089,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55428,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78944,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78945,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78946,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78947,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78948,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78949,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78950,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S83237,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S83239
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pubmed:abstractText |
We have isolated the gene coding for a new protein (SERP H), highly homologous to the 113-kDa serine-stretch protein SERP which confers protective immunity to monkeys. The gene consists of four exons interrupted by three short introns located at positions corresponding to those of the SERP gene. Both genes were shown to be linked on chromosome 2 of Plasmodium falciparum suggesting that both originate from a common ancestral gene. Both genes are transcribed in the blood-stage form as 3.8-kb mRNAs with high yield. The deduced amino acid sequence of SERP H is highly homologous to SERP, although it does not contain a serine stretch. A highly hydrophilic region specific for the protein which was shown to be identical among different P. falciparum isolates was expressed in Escherichia coli for preparation of SERP H specific antisera. A schizont polypeptide of 130 kDa within the parasitophorous vacuole was detected by Western blot analysis and immunoelectron microscopy. Like SERP, the 130-kDa protein exhibits a region homologous to cysteine proteinases, suggesting that these proteins, or their processing products, may play a role as proteinases at the time of merozoite release from the infected erythrocyte.
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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 |
Jan
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pubmed:issn |
0166-6851
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-13
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1840623-Amino Acid Sequence,
pubmed-meshheading:1840623-Animals,
pubmed-meshheading:1840623-Antigens, Protozoan,
pubmed-meshheading:1840623-Base Sequence,
pubmed-meshheading:1840623-Binding Sites,
pubmed-meshheading:1840623-Cysteine Endopeptidases,
pubmed-meshheading:1840623-Exons,
pubmed-meshheading:1840623-Introns,
pubmed-meshheading:1840623-Molecular Sequence Data,
pubmed-meshheading:1840623-Plasmodium falciparum,
pubmed-meshheading:1840623-Protozoan Proteins,
pubmed-meshheading:1840623-Sequence Alignment
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pubmed:year |
1991
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pubmed:articleTitle |
A new blood stage antigen of Plasmodium falciparum highly homologous to the serine-stretch protein SERP.
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pubmed:affiliation |
Research Department, Behringwerke AG, Marburg, F.R.G.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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